data_4771 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4771 _Entry.Title ; Assignment of the 1H, 15N and 13C resonances of the C-terminal domain of the TolA protein of Escherichia coli, involved in the cell envelope integrity ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-06-28 _Entry.Accession_date 2000-06-28 _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 . _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 Christophe Deprez . . . 4771 2 Laurence Blanchard . . . 4771 3 Jean-Pierre Simorre . . . 4771 4 Marthe Gavioli . . . 4771 5 Francoise Guerlesquin . . . 4771 6 Claude Lazdunski . . . 4771 7 Roland Lloubes . . . 4771 8 Dominique Marion . . . 4771 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4771 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 597 4771 '13C chemical shifts' 390 4771 '15N chemical shifts' 91 4771 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 . . 2004-07-21 . update author 'addition of relationship loop' 4771 2 . . 2000-10-30 . original author 'original release' 4771 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6258 'TolAIII in complex with g3pN1' 4771 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4771 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Assignment of the 1H, 15N and 13C resonances of the C-terminal domain of the TolA protein of Escherichia coli, involved in cell envelope integrity ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of Biomolecular NMR' _Citation.Journal_volume 18 _Citation.Journal_issue 2 _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 179 _Citation.Page_last 180 _Citation.Year 2000 _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 Christophe Deprez . . . 4771 1 2 Laurence Blanchard . . . 4771 1 3 Jean-Pierre Simorre . . . 4771 1 4 Marthe Gavioli . . . 4771 1 5 Francoise Guerlesquin . . . 4771 1 6 Claude Lazdunski . . . 4771 1 7 Roland Lloubes . . . 4771 1 8 Dominique Marion . . . 4771 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'TolA protein' 4771 1 'Tol-Pal system' 4771 1 'colicin translocation' 4771 1 'heteronuclear NMR assignment' 4771 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_tola3 _Assembly.Sf_category assembly _Assembly.Sf_framecode tola3 _Assembly.Entry_ID 4771 _Assembly.ID 1 _Assembly.Name tola3 _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 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4771 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 tola3 1 $TolA . . . native . . . . . 4771 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 42 42 SG . 1 . 1 CYS 67 67 SG . . . . . . . . . . 4771 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID tola3 system 4771 1 tola3 abbreviation 4771 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TolA _Entity.Sf_category entity _Entity.Sf_framecode TolA _Entity.Entry_ID 4771 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name TolA _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 ; AEFGNTKNNGASGADINNYA GQIKSAIESKFYDASSYAGK TCTLRIKLAPDGMLLDIKPE GGDPALCQAALAAAKLAKIP KPPSQAVYEVFKNAPLDFKP HHHHHH ; _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 106 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _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 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . REF NP_706495 . 'cell envelope integrity inner membrane protein TolA [Shigella flexneri 2a str. 301]' . . . . . 91.51 413 100.00 100.00 5.89e-54 . . . . 4771 1 . . SWISS-PROT P19934 . 'Protein tolA' . . . . . 91.51 421 100.00 100.00 3.34e-54 . . . . 4771 1 . . REF NP_308801 . 'cell envelope integrity inner membrane protein TolA [Escherichia coli O157:H7 str. Sakai]' . . . . . 91.51 394 100.00 100.00 1.21e-53 . . . . 4771 1 . . REF NP_415267 . 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli str. K-12 substr. MG1655]' . . . . . 91.51 421 100.00 100.00 3.34e-54 . . . . 4771 1 . . REF AP_001377 . 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli W3110]' . . . . . 91.51 421 100.00 100.00 3.34e-54 . . . . 4771 1 . . REF NP_286467 . 'cell envelope integrity inner membrane protein TolA [Escherichia coli O157:H7 EDL933]' . . . . . 91.51 394 100.00 100.00 1.21e-53 . . . . 4771 1 . . GenBank AAN42202 . 'membrane spanning protein [Shigella flexneri 2a str. 301]' . . . . . 91.51 413 100.00 100.00 5.89e-54 . . . . 4771 1 . . GenBank AAN79291 . 'TolA protein [Escherichia coli CFT073]' . . . . . 91.51 421 100.00 100.00 4.05e-54 . . . . 4771 1 . . GenBank AAC73833 . 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli str. K-12 substr. MG1655]' . . . . . 91.51 421 100.00 100.00 3.34e-54 . . . . 4771 1 . . GenBank AAG55075 . 'membrane spanning protein, required for outer membrane integrity [Escherichia coli O157:H7 EDL933]' . . . . . 91.51 394 100.00 100.00 1.21e-53 . . . . 4771 1 . . DBJ BAB34197 . 'membrane spanning protein TolA [Escherichia coli O157:H7 str. Sakai]' . . . . . 91.51 394 100.00 100.00 1.21e-53 . . . . 4771 1 . . GenBank AAA24683 . tolA . . . . . 91.51 421 100.00 100.00 3.34e-54 . . . . 4771 1 . . PDB 1TOL . 'Fusion Of N-Terminal Domain Of The Minor Coat Protein From Gene Iii In Phage M13, And C-Terminal Domain Of E. Coli Protein-Tola' . . . . . 91.51 222 100.00 100.00 7.78e-44 . . . . 4771 1 . . DBJ BAA35405 . 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli W3110]' . . . . . 91.51 421 100.00 100.00 3.34e-54 . . . . 4771 1 . . BMRB 6258 . 'TolA domain III' . . . . . 100.00 106 100.00 100.00 3.66e-55 . . . . 4771 1 . . PDB 1S62 . 'Solution Structure Of The Escherichia Coli Tola C-Terminal Domain' . . . . . 100.00 106 100.00 100.00 3.66e-55 . . . . 4771 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID TolA common 4771 1 TolA abbreviation 4771 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 . ALA . 4771 1 2 . GLU . 4771 1 3 . PHE . 4771 1 4 . GLY . 4771 1 5 . ASN . 4771 1 6 . THR . 4771 1 7 . LYS . 4771 1 8 . ASN . 4771 1 9 . ASN . 4771 1 10 . GLY . 4771 1 11 . ALA . 4771 1 12 . SER . 4771 1 13 . GLY . 4771 1 14 . ALA . 4771 1 15 . ASP . 4771 1 16 . ILE . 4771 1 17 . ASN . 4771 1 18 . ASN . 4771 1 19 . TYR . 4771 1 20 . ALA . 4771 1 21 . GLY . 4771 1 22 . GLN . 4771 1 23 . ILE . 4771 1 24 . LYS . 4771 1 25 . SER . 4771 1 26 . ALA . 4771 1 27 . ILE . 4771 1 28 . GLU . 4771 1 29 . SER . 4771 1 30 . LYS . 4771 1 31 . PHE . 4771 1 32 . TYR . 4771 1 33 . ASP . 4771 1 34 . ALA . 4771 1 35 . SER . 4771 1 36 . SER . 4771 1 37 . TYR . 4771 1 38 . ALA . 4771 1 39 . GLY . 4771 1 40 . LYS . 4771 1 41 . THR . 4771 1 42 . CYS . 4771 1 43 . THR . 4771 1 44 . LEU . 4771 1 45 . ARG . 4771 1 46 . ILE . 4771 1 47 . LYS . 4771 1 48 . LEU . 4771 1 49 . ALA . 4771 1 50 . PRO . 4771 1 51 . ASP . 4771 1 52 . GLY . 4771 1 53 . MET . 4771 1 54 . LEU . 4771 1 55 . LEU . 4771 1 56 . ASP . 4771 1 57 . ILE . 4771 1 58 . LYS . 4771 1 59 . PRO . 4771 1 60 . GLU . 4771 1 61 . GLY . 4771 1 62 . GLY . 4771 1 63 . ASP . 4771 1 64 . PRO . 4771 1 65 . ALA . 4771 1 66 . LEU . 4771 1 67 . CYS . 4771 1 68 . GLN . 4771 1 69 . ALA . 4771 1 70 . ALA . 4771 1 71 . LEU . 4771 1 72 . ALA . 4771 1 73 . ALA . 4771 1 74 . ALA . 4771 1 75 . LYS . 4771 1 76 . LEU . 4771 1 77 . ALA . 4771 1 78 . LYS . 4771 1 79 . ILE . 4771 1 80 . PRO . 4771 1 81 . LYS . 4771 1 82 . PRO . 4771 1 83 . PRO . 4771 1 84 . SER . 4771 1 85 . GLN . 4771 1 86 . ALA . 4771 1 87 . VAL . 4771 1 88 . TYR . 4771 1 89 . GLU . 4771 1 90 . VAL . 4771 1 91 . PHE . 4771 1 92 . LYS . 4771 1 93 . ASN . 4771 1 94 . ALA . 4771 1 95 . PRO . 4771 1 96 . LEU . 4771 1 97 . ASP . 4771 1 98 . PHE . 4771 1 99 . LYS . 4771 1 100 . PRO . 4771 1 101 . HIS . 4771 1 102 . HIS . 4771 1 103 . HIS . 4771 1 104 . HIS . 4771 1 105 . HIS . 4771 1 106 . HIS . 4771 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 4771 1 . GLU 2 2 4771 1 . PHE 3 3 4771 1 . GLY 4 4 4771 1 . ASN 5 5 4771 1 . THR 6 6 4771 1 . LYS 7 7 4771 1 . ASN 8 8 4771 1 . ASN 9 9 4771 1 . GLY 10 10 4771 1 . ALA 11 11 4771 1 . SER 12 12 4771 1 . GLY 13 13 4771 1 . ALA 14 14 4771 1 . ASP 15 15 4771 1 . ILE 16 16 4771 1 . ASN 17 17 4771 1 . ASN 18 18 4771 1 . TYR 19 19 4771 1 . ALA 20 20 4771 1 . GLY 21 21 4771 1 . GLN 22 22 4771 1 . ILE 23 23 4771 1 . LYS 24 24 4771 1 . SER 25 25 4771 1 . ALA 26 26 4771 1 . ILE 27 27 4771 1 . GLU 28 28 4771 1 . SER 29 29 4771 1 . LYS 30 30 4771 1 . PHE 31 31 4771 1 . TYR 32 32 4771 1 . ASP 33 33 4771 1 . ALA 34 34 4771 1 . SER 35 35 4771 1 . SER 36 36 4771 1 . TYR 37 37 4771 1 . ALA 38 38 4771 1 . GLY 39 39 4771 1 . LYS 40 40 4771 1 . THR 41 41 4771 1 . CYS 42 42 4771 1 . THR 43 43 4771 1 . LEU 44 44 4771 1 . ARG 45 45 4771 1 . ILE 46 46 4771 1 . LYS 47 47 4771 1 . LEU 48 48 4771 1 . ALA 49 49 4771 1 . PRO 50 50 4771 1 . ASP 51 51 4771 1 . GLY 52 52 4771 1 . MET 53 53 4771 1 . LEU 54 54 4771 1 . LEU 55 55 4771 1 . ASP 56 56 4771 1 . ILE 57 57 4771 1 . LYS 58 58 4771 1 . PRO 59 59 4771 1 . GLU 60 60 4771 1 . GLY 61 61 4771 1 . GLY 62 62 4771 1 . ASP 63 63 4771 1 . PRO 64 64 4771 1 . ALA 65 65 4771 1 . LEU 66 66 4771 1 . CYS 67 67 4771 1 . GLN 68 68 4771 1 . ALA 69 69 4771 1 . ALA 70 70 4771 1 . LEU 71 71 4771 1 . ALA 72 72 4771 1 . ALA 73 73 4771 1 . ALA 74 74 4771 1 . LYS 75 75 4771 1 . LEU 76 76 4771 1 . ALA 77 77 4771 1 . LYS 78 78 4771 1 . ILE 79 79 4771 1 . PRO 80 80 4771 1 . LYS 81 81 4771 1 . PRO 82 82 4771 1 . PRO 83 83 4771 1 . SER 84 84 4771 1 . GLN 85 85 4771 1 . ALA 86 86 4771 1 . VAL 87 87 4771 1 . TYR 88 88 4771 1 . GLU 89 89 4771 1 . VAL 90 90 4771 1 . PHE 91 91 4771 1 . LYS 92 92 4771 1 . ASN 93 93 4771 1 . ALA 94 94 4771 1 . PRO 95 95 4771 1 . LEU 96 96 4771 1 . ASP 97 97 4771 1 . PHE 98 98 4771 1 . LYS 99 99 4771 1 . PRO 100 100 4771 1 . HIS 101 101 4771 1 . HIS 102 102 4771 1 . HIS 103 103 4771 1 . HIS 104 104 4771 1 . HIS 105 105 4771 1 . HIS 106 106 4771 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 4771 _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 $TolA . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli . . . . . . . . . . . . periplasm . . . . . . . . 4771 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 4771 _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 $TolA . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli W3110 . . . . . . . . . . . . . . . . . . . 'The protein was overexpressed into the periplasm.' . . 4771 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Sample.Sf_category sample _Sample.Sf_framecode sample _Sample.Entry_ID 4771 _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 TolA [U-15N] . . 1 $TolA . . 0.5 . . mM . . . . 4771 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition _Sample_condition_list.Entry_ID 4771 _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 6.8 0.1 n/a 4771 1 temperature 300 1 K 4771 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 4771 _Software.ID 1 _Software.Name FELIX _Software.Version 2000 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data processing and visualization' 4771 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4771 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4771 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4771 _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_1 Varian INOVA . 600 . . . 4771 1 2 NMR_spectrometer_2 Varian INOVA . 800 . . . 4771 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 4771 _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 . . . . . . . . . . . . 1 $sample . . . 1 $condition . . . . . . . . . . . . . . . . . . . . . 4771 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_csr _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode csr _Chem_shift_reference.Entry_ID 4771 _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 H 1 H2O protons . . . . ppm 4.6388 internal direct 1 internal cylindrical parallel_to_Bo 1 $entry_citation 'temperature, pH' . 1 $entry_citation 4771 1 N 15 'liquid NH3' nitrogen . . . . ppm 0.00 external indirect 0.101329118 external_to_the_sample cylindrical parallel_to_Bo 1 $entry_citation . . 1 $entry_citation 4771 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 external indirect 0.251449530 external_to_the_sample cylindrical parallel_to_Bo 1 $entry_citation . . 1 $entry_citation 4771 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_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shifts _Assigned_chem_shift_list.Entry_ID 4771 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $csr _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 . _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 . 4771 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 CA C 13 51.77 0.10 . 1 . . . . . . . . 4771 1 2 . 1 1 1 1 ALA CB C 13 19.33 0.10 . 1 . . . . . . . . 4771 1 3 . 1 1 1 1 ALA HA H 1 3.93 0.01 . 1 . . . . . . . . 4771 1 4 . 1 1 1 1 ALA HB1 H 1 1.34 0.01 . 1 . . . . . . . . 4771 1 5 . 1 1 1 1 ALA HB2 H 1 1.34 0.01 . 1 . . . . . . . . 4771 1 6 . 1 1 1 1 ALA HB3 H 1 1.34 0.01 . 1 . . . . . . . . 4771 1 7 . 1 1 2 2 GLU C C 13 175.87 0.10 . 1 . . . . . . . . 4771 1 8 . 1 1 2 2 GLU CA C 13 56.25 0.12 . 1 . . . . . . . . 4771 1 9 . 1 1 2 2 GLU CB C 13 30.35 0.10 . 1 . . . . . . . . 4771 1 10 . 1 1 2 2 GLU CG C 13 35.93 0.10 . 1 . . . . . . . . 4771 1 11 . 1 1 2 2 GLU HA H 1 4.21 0.01 . 1 . . . . . . . . 4771 1 12 . 1 1 2 2 GLU HB2 H 1 1.86 0.01 . 2 . . . . . . . . 4771 1 13 . 1 1 2 2 GLU HB3 H 1 1.75 0.01 . 2 . . . . . . . . 4771 1 14 . 1 1 2 2 GLU HG2 H 1 2.08 0.01 . 2 . . . . . . . . 4771 1 15 . 1 1 2 2 GLU HG3 H 1 2.04 0.01 . 2 . . . . . . . . 4771 1 16 . 1 1 3 3 PHE C C 13 176.18 0.10 . 1 . . . . . . . . 4771 1 17 . 1 1 3 3 PHE CA C 13 57.57 0.10 . 1 . . . . . . . . 4771 1 18 . 1 1 3 3 PHE CB C 13 39.58 0.10 . 1 . . . . . . . . 4771 1 19 . 1 1 3 3 PHE H H 1 8.29 0.01 . 1 . . . . . . . . 4771 1 20 . 1 1 3 3 PHE HA H 1 4.55 0.01 . 1 . . . . . . . . 4771 1 21 . 1 1 3 3 PHE HB2 H 1 3.09 0.01 . 2 . . . . . . . . 4771 1 22 . 1 1 3 3 PHE HB3 H 1 2.93 0.01 . 2 . . . . . . . . 4771 1 23 . 1 1 3 3 PHE N N 15 121.05 0.10 . 1 . . . . . . . . 4771 1 24 . 1 1 4 4 GLY C C 13 173.75 0.10 . 1 . . . . . . . . 4771 1 25 . 1 1 4 4 GLY CA C 13 45.22 0.10 . 1 . . . . . . . . 4771 1 26 . 1 1 4 4 GLY H H 1 8.28 0.01 . 1 . . . . . . . . 4771 1 27 . 1 1 4 4 GLY HA2 H 1 3.85 0.01 . 2 . . . . . . . . 4771 1 28 . 1 1 4 4 GLY N N 15 110.28 0.10 . 1 . . . . . . . . 4771 1 29 . 1 1 5 5 ASN CA C 13 53.15 0.10 . 1 . . . . . . . . 4771 1 30 . 1 1 5 5 ASN CB C 13 38.77 0.10 . 1 . . . . . . . . 4771 1 31 . 1 1 5 5 ASN H H 1 8.21 0.01 . 1 . . . . . . . . 4771 1 32 . 1 1 5 5 ASN HA H 1 4.71 0.01 . 1 . . . . . . . . 4771 1 33 . 1 1 5 5 ASN HB2 H 1 2.69 0.01 . 2 . . . . . . . . 4771 1 34 . 1 1 5 5 ASN HB3 H 1 2.77 0.01 . 2 . . . . . . . . 4771 1 35 . 1 1 5 5 ASN N N 15 118.80 0.10 . 1 . . . . . . . . 4771 1 36 . 1 1 6 6 THR CA C 13 61.95 0.10 . 1 . . . . . . . . 4771 1 37 . 1 1 6 6 THR CB C 13 69.78 0.10 . 1 . . . . . . . . 4771 1 38 . 1 1 6 6 THR CG2 C 13 21.44 0.10 . 1 . . . . . . . . 4771 1 39 . 1 1 6 6 THR H H 1 8.04 0.01 . 1 . . . . . . . . 4771 1 40 . 1 1 6 6 THR HA H 1 4.24 0.01 . 1 . . . . . . . . 4771 1 41 . 1 1 6 6 THR HB H 1 4.18 0.01 . 2 . . . . . . . . 4771 1 42 . 1 1 6 6 THR HG21 H 1 1.12 0.01 . 1 . . . . . . . . 4771 1 43 . 1 1 6 6 THR HG22 H 1 1.12 0.01 . 1 . . . . . . . . 4771 1 44 . 1 1 6 6 THR HG23 H 1 1.12 0.01 . 1 . . . . . . . . 4771 1 45 . 1 1 6 6 THR N N 15 114.33 0.10 . 1 . . . . . . . . 4771 1 46 . 1 1 7 7 LYS CA C 13 56.18 0.10 . 1 . . . . . . . . 4771 1 47 . 1 1 7 7 LYS CB C 13 32.75 0.10 . 1 . . . . . . . . 4771 1 48 . 1 1 7 7 LYS CD C 13 28.84 0.10 . 1 . . . . . . . . 4771 1 49 . 1 1 7 7 LYS CE C 13 41.98 0.10 . 1 . . . . . . . . 4771 1 50 . 1 1 7 7 LYS CG C 13 24.54 0.10 . 1 . . . . . . . . 4771 1 51 . 1 1 7 7 LYS H H 1 8.20 0.01 . 1 . . . . . . . . 4771 1 52 . 1 1 7 7 LYS HA H 1 4.23 0.01 . 1 . . . . . . . . 4771 1 53 . 1 1 7 7 LYS HB2 H 1 1.69 0.02 . 2 . . . . . . . . 4771 1 54 . 1 1 7 7 LYS HB3 H 1 1.74 0.01 . 2 . . . . . . . . 4771 1 55 . 1 1 7 7 LYS HD2 H 1 1.58 0.01 . 2 . . . . . . . . 4771 1 56 . 1 1 7 7 LYS HE2 H 1 2.90 0.01 . 2 . . . . . . . . 4771 1 57 . 1 1 7 7 LYS HG2 H 1 1.33 0.01 . 2 . . . . . . . . 4771 1 58 . 1 1 7 7 LYS HG3 H 1 1.31 0.01 . 2 . . . . . . . . 4771 1 59 . 1 1 7 7 LYS N N 15 123.12 0.10 . 1 . . . . . . . . 4771 1 60 . 1 1 8 8 ASN C C 13 176.10 0.10 . 1 . . . . . . . . 4771 1 61 . 1 1 8 8 ASN CA C 13 54.69 0.12 . 1 . . . . . . . . 4771 1 62 . 1 1 8 8 ASN CB C 13 40.71 0.13 . 1 . . . . . . . . 4771 1 63 . 1 1 8 8 ASN HA H 1 4.38 0.01 . 1 . . . . . . . . 4771 1 64 . 1 1 8 8 ASN HB2 H 1 2.72 0.01 . 2 . . . . . . . . 4771 1 65 . 1 1 8 8 ASN HB3 H 1 2.62 0.01 . 2 . . . . . . . . 4771 1 66 . 1 1 9 9 ASN C C 13 175.54 0.10 . 1 . . . . . . . . 4771 1 67 . 1 1 9 9 ASN H H 1 8.12 0.01 . 1 . . . . . . . . 4771 1 68 . 1 1 9 9 ASN N N 15 113.61 0.10 . 1 . . . . . . . . 4771 1 69 . 1 1 10 10 GLY C C 13 173.56 0.10 . 1 . . . . . . . . 4771 1 70 . 1 1 10 10 GLY CA C 13 45.03 0.10 . 1 . . . . . . . . 4771 1 71 . 1 1 10 10 GLY H H 1 8.21 0.01 . 1 . . . . . . . . 4771 1 72 . 1 1 10 10 GLY HA2 H 1 3.80 0.01 . 2 . . . . . . . . 4771 1 73 . 1 1 10 10 GLY HA3 H 1 3.89 0.01 . 2 . . . . . . . . 4771 1 74 . 1 1 10 10 GLY N N 15 108.62 0.10 . 1 . . . . . . . . 4771 1 75 . 1 1 11 11 ALA C C 13 177.19 0.10 . 1 . . . . . . . . 4771 1 76 . 1 1 11 11 ALA CA C 13 51.61 0.10 . 1 . . . . . . . . 4771 1 77 . 1 1 11 11 ALA CB C 13 19.41 0.10 . 1 . . . . . . . . 4771 1 78 . 1 1 11 11 ALA H H 1 8.06 0.01 . 1 . . . . . . . . 4771 1 79 . 1 1 11 11 ALA HA H 1 4.39 0.01 . 1 . . . . . . . . 4771 1 80 . 1 1 11 11 ALA HB1 H 1 1.21 0.01 . 1 . . . . . . . . 4771 1 81 . 1 1 11 11 ALA HB2 H 1 1.21 0.01 . 1 . . . . . . . . 4771 1 82 . 1 1 11 11 ALA HB3 H 1 1.21 0.01 . 1 . . . . . . . . 4771 1 83 . 1 1 11 11 ALA N N 15 123.47 0.10 . 1 . . . . . . . . 4771 1 84 . 1 1 12 12 SER C C 13 175.29 0.10 . 1 . . . . . . . . 4771 1 85 . 1 1 12 12 SER CA C 13 57.65 0.10 . 1 . . . . . . . . 4771 1 86 . 1 1 12 12 SER CB C 13 64.55 0.10 . 1 . . . . . . . . 4771 1 87 . 1 1 12 12 SER H H 1 8.71 0.01 . 1 . . . . . . . . 4771 1 88 . 1 1 12 12 SER HA H 1 4.43 0.01 . 1 . . . . . . . . 4771 1 89 . 1 1 12 12 SER HB2 H 1 4.07 0.01 . 2 . . . . . . . . 4771 1 90 . 1 1 12 12 SER HB3 H 1 3.90 0.01 . 2 . . . . . . . . 4771 1 91 . 1 1 12 12 SER N N 15 117.44 0.10 . 1 . . . . . . . . 4771 1 92 . 1 1 13 13 GLY C C 13 175.75 0.10 . 1 . . . . . . . . 4771 1 93 . 1 1 13 13 GLY CA C 13 46.92 0.10 . 1 . . . . . . . . 4771 1 94 . 1 1 13 13 GLY H H 1 8.65 0.01 . 1 . . . . . . . . 4771 1 95 . 1 1 13 13 GLY HA2 H 1 3.78 0.01 . 2 . . . . . . . . 4771 1 96 . 1 1 13 13 GLY HA3 H 1 3.92 0.01 . 2 . . . . . . . . 4771 1 97 . 1 1 13 13 GLY N N 15 110.27 0.10 . 1 . . . . . . . . 4771 1 98 . 1 1 14 14 ALA C C 13 173.02 0.10 . 5 . . . . . . . . 4771 1 99 . 1 1 14 14 ALA CA C 13 54.72 0.10 . 1 . . . . . . . . 4771 1 100 . 1 1 14 14 ALA CB C 13 18.08 0.10 . 1 . . . . . . . . 4771 1 101 . 1 1 14 14 ALA H H 1 8.16 0.01 . 1 . . . . . . . . 4771 1 102 . 1 1 14 14 ALA HA H 1 4.16 0.01 . 1 . . . . . . . . 4771 1 103 . 1 1 14 14 ALA HB1 H 1 1.33 0.01 . 1 . . . . . . . . 4771 1 104 . 1 1 14 14 ALA HB2 H 1 1.33 0.01 . 1 . . . . . . . . 4771 1 105 . 1 1 14 14 ALA HB3 H 1 1.33 0.01 . 1 . . . . . . . . 4771 1 106 . 1 1 14 14 ALA N N 15 123.55 0.10 . 1 . . . . . . . . 4771 1 107 . 1 1 15 15 ASP C C 13 177.80 0.10 . 5 . . . . . . . . 4771 1 108 . 1 1 15 15 ASP CA C 13 56.95 0.10 . 1 . . . . . . . . 4771 1 109 . 1 1 15 15 ASP CB C 13 40.26 0.10 . 1 . . . . . . . . 4771 1 110 . 1 1 15 15 ASP H H 1 7.90 0.01 . 1 . . . . . . . . 4771 1 111 . 1 1 15 15 ASP HA H 1 4.37 0.01 . 1 . . . . . . . . 4771 1 112 . 1 1 15 15 ASP HB2 H 1 2.75 0.01 . 2 . . . . . . . . 4771 1 113 . 1 1 15 15 ASP HB3 H 1 2.48 0.01 . 2 . . . . . . . . 4771 1 114 . 1 1 15 15 ASP N N 15 119.29 0.10 . 1 . . . . . . . . 4771 1 115 . 1 1 16 16 ILE C C 13 177.22 0.10 . 5 . . . . . . . . 4771 1 116 . 1 1 16 16 ILE CA C 13 65.31 0.10 . 1 . . . . . . . . 4771 1 117 . 1 1 16 16 ILE CB C 13 38.14 0.10 . 1 . . . . . . . . 4771 1 118 . 1 1 16 16 ILE CD1 C 13 13.35 0.10 . 1 . . . . . . . . 4771 1 119 . 1 1 16 16 ILE CG1 C 13 29.45 0.10 . 1 . . . . . . . . 4771 1 120 . 1 1 16 16 ILE CG2 C 13 17.18 0.10 . 1 . . . . . . . . 4771 1 121 . 1 1 16 16 ILE H H 1 8.02 0.01 . 1 . . . . . . . . 4771 1 122 . 1 1 16 16 ILE HA H 1 3.83 0.01 . 1 . . . . . . . . 4771 1 123 . 1 1 16 16 ILE HB H 1 2.01 0.01 . 2 . . . . . . . . 4771 1 124 . 1 1 16 16 ILE HD11 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 125 . 1 1 16 16 ILE HD12 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 126 . 1 1 16 16 ILE HD13 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 127 . 1 1 16 16 ILE HG12 H 1 1.71 0.01 . 2 . . . . . . . . 4771 1 128 . 1 1 16 16 ILE HG13 H 1 1.10 0.01 . 2 . . . . . . . . 4771 1 129 . 1 1 16 16 ILE HG21 H 1 1.04 0.01 . 1 . . . . . . . . 4771 1 130 . 1 1 16 16 ILE HG22 H 1 1.04 0.01 . 1 . . . . . . . . 4771 1 131 . 1 1 16 16 ILE HG23 H 1 1.04 0.01 . 1 . . . . . . . . 4771 1 132 . 1 1 16 16 ILE N N 15 121.38 0.10 . 1 . . . . . . . . 4771 1 133 . 1 1 17 17 ASN C C 13 178.75 0.10 . 1 . . . . . . . . 4771 1 134 . 1 1 17 17 ASN CA C 13 56.20 0.10 . 1 . . . . . . . . 4771 1 135 . 1 1 17 17 ASN CB C 13 38.17 0.10 . 1 . . . . . . . . 4771 1 136 . 1 1 17 17 ASN H H 1 8.33 0.01 . 1 . . . . . . . . 4771 1 137 . 1 1 17 17 ASN HA H 1 4.49 0.01 . 1 . . . . . . . . 4771 1 138 . 1 1 17 17 ASN HB2 H 1 2.79 0.01 . 2 . . . . . . . . 4771 1 139 . 1 1 17 17 ASN N N 15 118.28 0.10 . 1 . . . . . . . . 4771 1 140 . 1 1 18 18 ASN C C 13 178.11 0.10 . 1 . . . . . . . . 4771 1 141 . 1 1 18 18 ASN CA C 13 55.92 0.10 . 1 . . . . . . . . 4771 1 142 . 1 1 18 18 ASN CB C 13 38.22 0.10 . 1 . . . . . . . . 4771 1 143 . 1 1 18 18 ASN H H 1 8.63 0.01 . 1 . . . . . . . . 4771 1 144 . 1 1 18 18 ASN HA H 1 4.46 0.01 . 1 . . . . . . . . 4771 1 145 . 1 1 18 18 ASN HB2 H 1 2.96 0.01 . 2 . . . . . . . . 4771 1 146 . 1 1 18 18 ASN HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4771 1 147 . 1 1 18 18 ASN N N 15 119.40 0.10 . 1 . . . . . . . . 4771 1 148 . 1 1 19 19 TYR C C 13 177.08 0.10 . 1 . . . . . . . . 4771 1 149 . 1 1 19 19 TYR CA C 13 61.16 0.10 . 1 . . . . . . . . 4771 1 150 . 1 1 19 19 TYR CB C 13 37.69 0.10 . 1 . . . . . . . . 4771 1 151 . 1 1 19 19 TYR H H 1 7.93 0.01 . 1 . . . . . . . . 4771 1 152 . 1 1 19 19 TYR HA H 1 4.34 0.01 . 1 . . . . . . . . 4771 1 153 . 1 1 19 19 TYR HB2 H 1 3.00 0.01 . 2 . . . . . . . . 4771 1 154 . 1 1 19 19 TYR HB3 H 1 2.53 0.01 . 2 . . . . . . . . 4771 1 155 . 1 1 19 19 TYR N N 15 121.83 0.10 . 1 . . . . . . . . 4771 1 156 . 1 1 20 20 ALA C C 13 180.30 0.10 . 1 . . . . . . . . 4771 1 157 . 1 1 20 20 ALA CA C 13 55.54 0.10 . 1 . . . . . . . . 4771 1 158 . 1 1 20 20 ALA CB C 13 17.83 0.10 . 1 . . . . . . . . 4771 1 159 . 1 1 20 20 ALA H H 1 8.49 0.01 . 1 . . . . . . . . 4771 1 160 . 1 1 20 20 ALA HA H 1 3.50 0.01 . 1 . . . . . . . . 4771 1 161 . 1 1 20 20 ALA HB1 H 1 1.62 0.01 . 1 . . . . . . . . 4771 1 162 . 1 1 20 20 ALA HB2 H 1 1.62 0.01 . 1 . . . . . . . . 4771 1 163 . 1 1 20 20 ALA HB3 H 1 1.62 0.01 . 1 . . . . . . . . 4771 1 164 . 1 1 20 20 ALA N N 15 121.15 0.10 . 1 . . . . . . . . 4771 1 165 . 1 1 21 21 GLY C C 13 176.62 0.10 . 1 . . . . . . . . 4771 1 166 . 1 1 21 21 GLY CA C 13 46.89 0.10 . 1 . . . . . . . . 4771 1 167 . 1 1 21 21 GLY H H 1 7.84 0.01 . 1 . . . . . . . . 4771 1 168 . 1 1 21 21 GLY HA2 H 1 3.71 0.01 . 2 . . . . . . . . 4771 1 169 . 1 1 21 21 GLY HA3 H 1 3.94 0.01 . 2 . . . . . . . . 4771 1 170 . 1 1 21 21 GLY N N 15 103.37 0.10 . 1 . . . . . . . . 4771 1 171 . 1 1 22 22 GLN C C 13 179.70 0.10 . 1 . . . . . . . . 4771 1 172 . 1 1 22 22 GLN CA C 13 58.84 0.13 . 1 . . . . . . . . 4771 1 173 . 1 1 22 22 GLN CB C 13 28.50 0.11 . 1 . . . . . . . . 4771 1 174 . 1 1 22 22 GLN CG C 13 34.34 0.10 . 1 . . . . . . . . 4771 1 175 . 1 1 22 22 GLN H H 1 7.65 0.01 . 1 . . . . . . . . 4771 1 176 . 1 1 22 22 GLN HA H 1 4.02 0.01 . 1 . . . . . . . . 4771 1 177 . 1 1 22 22 GLN HB2 H 1 2.17 0.01 . 2 . . . . . . . . 4771 1 178 . 1 1 22 22 GLN HB3 H 1 1.82 0.01 . 2 . . . . . . . . 4771 1 179 . 1 1 22 22 GLN HG2 H 1 2.53 0.01 . 2 . . . . . . . . 4771 1 180 . 1 1 22 22 GLN HG3 H 1 2.30 0.01 . 2 . . . . . . . . 4771 1 181 . 1 1 22 22 GLN N N 15 122.68 0.10 . 1 . . . . . . . . 4771 1 182 . 1 1 23 23 ILE C C 13 177.60 0.10 . 1 . . . . . . . . 4771 1 183 . 1 1 23 23 ILE CA C 13 66.13 0.10 . 1 . . . . . . . . 4771 1 184 . 1 1 23 23 ILE CB C 13 37.69 0.10 . 1 . . . . . . . . 4771 1 185 . 1 1 23 23 ILE CD1 C 13 14.46 0.10 . 1 . . . . . . . . 4771 1 186 . 1 1 23 23 ILE CG1 C 13 27.01 0.11 . 1 . . . . . . . . 4771 1 187 . 1 1 23 23 ILE CG2 C 13 17.20 0.10 . 1 . . . . . . . . 4771 1 188 . 1 1 23 23 ILE H H 1 7.90 0.01 . 1 . . . . . . . . 4771 1 189 . 1 1 23 23 ILE HA H 1 3.23 0.01 . 1 . . . . . . . . 4771 1 190 . 1 1 23 23 ILE HB H 1 1.55 0.01 . 2 . . . . . . . . 4771 1 191 . 1 1 23 23 ILE HD11 H 1 0.08 0.01 . 1 . . . . . . . . 4771 1 192 . 1 1 23 23 ILE HD12 H 1 0.08 0.01 . 1 . . . . . . . . 4771 1 193 . 1 1 23 23 ILE HD13 H 1 0.08 0.01 . 1 . . . . . . . . 4771 1 194 . 1 1 23 23 ILE HG12 H 1 0.74 0.02 . 2 . . . . . . . . 4771 1 195 . 1 1 23 23 ILE HG13 H 1 0.23 0.01 . 2 . . . . . . . . 4771 1 196 . 1 1 23 23 ILE HG21 H 1 0.60 0.01 . 1 . . . . . . . . 4771 1 197 . 1 1 23 23 ILE HG22 H 1 0.60 0.01 . 1 . . . . . . . . 4771 1 198 . 1 1 23 23 ILE HG23 H 1 0.60 0.01 . 1 . . . . . . . . 4771 1 199 . 1 1 23 23 ILE N N 15 121.37 0.10 . 1 . . . . . . . . 4771 1 200 . 1 1 24 24 LYS C C 13 178.74 0.10 . 1 . . . . . . . . 4771 1 201 . 1 1 24 24 LYS CA C 13 61.34 0.10 . 1 . . . . . . . . 4771 1 202 . 1 1 24 24 LYS CB C 13 31.86 0.11 . 1 . . . . . . . . 4771 1 203 . 1 1 24 24 LYS CD C 13 29.57 0.15 . 1 . . . . . . . . 4771 1 204 . 1 1 24 24 LYS CE C 13 41.95 0.10 . 1 . . . . . . . . 4771 1 205 . 1 1 24 24 LYS CG C 13 26.60 0.10 . 1 . . . . . . . . 4771 1 206 . 1 1 24 24 LYS H H 1 8.10 0.01 . 1 . . . . . . . . 4771 1 207 . 1 1 24 24 LYS HA H 1 3.69 0.01 . 1 . . . . . . . . 4771 1 208 . 1 1 24 24 LYS HB2 H 1 2.01 0.02 . 2 . . . . . . . . 4771 1 209 . 1 1 24 24 LYS HB3 H 1 1.87 0.02 . 2 . . . . . . . . 4771 1 210 . 1 1 24 24 LYS HD2 H 1 1.78 0.01 . 2 . . . . . . . . 4771 1 211 . 1 1 24 24 LYS HD3 H 1 1.62 0.01 . 2 . . . . . . . . 4771 1 212 . 1 1 24 24 LYS HE2 H 1 2.76 0.01 . 2 . . . . . . . . 4771 1 213 . 1 1 24 24 LYS HG2 H 1 1.68 0.01 . 2 . . . . . . . . 4771 1 214 . 1 1 24 24 LYS HG3 H 1 1.26 0.01 . 2 . . . . . . . . 4771 1 215 . 1 1 24 24 LYS N N 15 118.03 0.10 . 1 . . . . . . . . 4771 1 216 . 1 1 25 25 SER C C 13 176.76 0.10 . 1 . . . . . . . . 4771 1 217 . 1 1 25 25 SER CA C 13 61.67 0.10 . 1 . . . . . . . . 4771 1 218 . 1 1 25 25 SER CB C 13 62.76 0.10 . 1 . . . . . . . . 4771 1 219 . 1 1 25 25 SER H H 1 8.32 0.01 . 1 . . . . . . . . 4771 1 220 . 1 1 25 25 SER HA H 1 4.21 0.01 . 1 . . . . . . . . 4771 1 221 . 1 1 25 25 SER HB2 H 1 3.86 0.01 . 2 . . . . . . . . 4771 1 222 . 1 1 25 25 SER N N 15 113.77 0.10 . 1 . . . . . . . . 4771 1 223 . 1 1 26 26 ALA C C 13 180.50 0.10 . 1 . . . . . . . . 4771 1 224 . 1 1 26 26 ALA CA C 13 55.22 0.11 . 1 . . . . . . . . 4771 1 225 . 1 1 26 26 ALA CB C 13 17.91 0.10 . 1 . . . . . . . . 4771 1 226 . 1 1 26 26 ALA H H 1 7.74 0.01 . 1 . . . . . . . . 4771 1 227 . 1 1 26 26 ALA HA H 1 4.11 0.01 . 1 . . . . . . . . 4771 1 228 . 1 1 26 26 ALA HB1 H 1 1.44 0.01 . 1 . . . . . . . . 4771 1 229 . 1 1 26 26 ALA HB2 H 1 1.44 0.01 . 1 . . . . . . . . 4771 1 230 . 1 1 26 26 ALA HB3 H 1 1.44 0.01 . 1 . . . . . . . . 4771 1 231 . 1 1 26 26 ALA N N 15 125.20 0.10 . 1 . . . . . . . . 4771 1 232 . 1 1 27 27 ILE C C 13 177.74 0.10 . 1 . . . . . . . . 4771 1 233 . 1 1 27 27 ILE CA C 13 66.06 0.10 . 1 . . . . . . . . 4771 1 234 . 1 1 27 27 ILE CB C 13 37.86 0.10 . 1 . . . . . . . . 4771 1 235 . 1 1 27 27 ILE CD1 C 13 13.03 0.10 . 1 . . . . . . . . 4771 1 236 . 1 1 27 27 ILE CG1 C 13 28.53 0.10 . 1 . . . . . . . . 4771 1 237 . 1 1 27 27 ILE CG2 C 13 16.96 0.10 . 1 . . . . . . . . 4771 1 238 . 1 1 27 27 ILE H H 1 7.78 0.01 . 1 . . . . . . . . 4771 1 239 . 1 1 27 27 ILE HA H 1 3.25 0.01 . 1 . . . . . . . . 4771 1 240 . 1 1 27 27 ILE HB H 1 1.69 0.01 . 2 . . . . . . . . 4771 1 241 . 1 1 27 27 ILE HD11 H 1 0.41 0.01 . 1 . . . . . . . . 4771 1 242 . 1 1 27 27 ILE HD12 H 1 0.41 0.01 . 1 . . . . . . . . 4771 1 243 . 1 1 27 27 ILE HD13 H 1 0.41 0.01 . 1 . . . . . . . . 4771 1 244 . 1 1 27 27 ILE HG12 H 1 1.83 0.01 . 2 . . . . . . . . 4771 1 245 . 1 1 27 27 ILE HG21 H 1 0.30 0.01 . 1 . . . . . . . . 4771 1 246 . 1 1 27 27 ILE HG22 H 1 0.30 0.01 . 1 . . . . . . . . 4771 1 247 . 1 1 27 27 ILE HG23 H 1 0.30 0.01 . 1 . . . . . . . . 4771 1 248 . 1 1 27 27 ILE N N 15 118.31 0.10 . 1 . . . . . . . . 4771 1 249 . 1 1 28 28 GLU C C 13 179.12 0.10 . 1 . . . . . . . . 4771 1 250 . 1 1 28 28 GLU CA C 13 60.18 0.10 . 1 . . . . . . . . 4771 1 251 . 1 1 28 28 GLU CB C 13 29.55 0.10 . 1 . . . . . . . . 4771 1 252 . 1 1 28 28 GLU CG C 13 37.40 0.10 . 1 . . . . . . . . 4771 1 253 . 1 1 28 28 GLU H H 1 8.77 0.01 . 1 . . . . . . . . 4771 1 254 . 1 1 28 28 GLU HA H 1 3.88 0.01 . 1 . . . . . . . . 4771 1 255 . 1 1 28 28 GLU HB2 H 1 2.09 0.01 . 2 . . . . . . . . 4771 1 256 . 1 1 28 28 GLU HG2 H 1 2.24 0.01 . 2 . . . . . . . . 4771 1 257 . 1 1 28 28 GLU N N 15 119.04 0.10 . 1 . . . . . . . . 4771 1 258 . 1 1 29 29 SER C C 13 174.90 0.10 . 1 . . . . . . . . 4771 1 259 . 1 1 29 29 SER CA C 13 61.43 0.10 . 1 . . . . . . . . 4771 1 260 . 1 1 29 29 SER CB C 13 63.27 0.10 . 1 . . . . . . . . 4771 1 261 . 1 1 29 29 SER H H 1 7.94 0.01 . 1 . . . . . . . . 4771 1 262 . 1 1 29 29 SER HA H 1 4.23 0.01 . 1 . . . . . . . . 4771 1 263 . 1 1 29 29 SER HB2 H 1 3.99 0.01 . 2 . . . . . . . . 4771 1 264 . 1 1 29 29 SER N N 15 112.96 0.10 . 1 . . . . . . . . 4771 1 265 . 1 1 30 30 LYS C C 13 175.00 0.10 . 1 . . . . . . . . 4771 1 266 . 1 1 30 30 LYS CA C 13 52.89 0.10 . 1 . . . . . . . . 4771 1 267 . 1 1 30 30 LYS CB C 13 32.05 0.10 . 1 . . . . . . . . 4771 1 268 . 1 1 30 30 LYS CD C 13 27.40 0.10 . 1 . . . . . . . . 4771 1 269 . 1 1 30 30 LYS CE C 13 42.06 0.11 . 1 . . . . . . . . 4771 1 270 . 1 1 30 30 LYS CG C 13 22.85 0.10 . 1 . . . . . . . . 4771 1 271 . 1 1 30 30 LYS H H 1 7.21 0.01 . 1 . . . . . . . . 4771 1 272 . 1 1 30 30 LYS HA H 1 4.47 0.01 . 1 . . . . . . . . 4771 1 273 . 1 1 30 30 LYS HB2 H 1 2.02 0.01 . 2 . . . . . . . . 4771 1 274 . 1 1 30 30 LYS HB3 H 1 1.78 0.01 . 2 . . . . . . . . 4771 1 275 . 1 1 30 30 LYS HD2 H 1 1.64 0.01 . 2 . . . . . . . . 4771 1 276 . 1 1 30 30 LYS HD3 H 1 1.44 0.01 . 2 . . . . . . . . 4771 1 277 . 1 1 30 30 LYS HE2 H 1 2.98 0.01 . 2 . . . . . . . . 4771 1 278 . 1 1 30 30 LYS HE3 H 1 2.90 0.01 . 2 . . . . . . . . 4771 1 279 . 1 1 30 30 LYS HG2 H 1 1.11 0.01 . 2 . . . . . . . . 4771 1 280 . 1 1 30 30 LYS HG3 H 1 1.42 0.01 . 2 . . . . . . . . 4771 1 281 . 1 1 30 30 LYS N N 15 118.09 0.10 . 1 . . . . . . . . 4771 1 282 . 1 1 31 31 PHE C C 13 175.39 0.10 . 1 . . . . . . . . 4771 1 283 . 1 1 31 31 PHE CA C 13 56.18 0.12 . 1 . . . . . . . . 4771 1 284 . 1 1 31 31 PHE CB C 13 39.62 0.10 . 1 . . . . . . . . 4771 1 285 . 1 1 31 31 PHE H H 1 7.61 0.01 . 1 . . . . . . . . 4771 1 286 . 1 1 31 31 PHE HA H 1 4.40 0.01 . 1 . . . . . . . . 4771 1 287 . 1 1 31 31 PHE HB2 H 1 3.27 0.01 . 2 . . . . . . . . 4771 1 288 . 1 1 31 31 PHE HB3 H 1 3.00 0.01 . 2 . . . . . . . . 4771 1 289 . 1 1 31 31 PHE N N 15 122.61 0.10 . 1 . . . . . . . . 4771 1 290 . 1 1 32 32 TYR C C 13 175.76 0.10 . 1 . . . . . . . . 4771 1 291 . 1 1 32 32 TYR CA C 13 59.13 0.10 . 1 . . . . . . . . 4771 1 292 . 1 1 32 32 TYR CB C 13 38.04 0.10 . 1 . . . . . . . . 4771 1 293 . 1 1 32 32 TYR H H 1 7.93 0.01 . 1 . . . . . . . . 4771 1 294 . 1 1 32 32 TYR HA H 1 4.46 0.01 . 1 . . . . . . . . 4771 1 295 . 1 1 32 32 TYR HB2 H 1 3.00 0.01 . 2 . . . . . . . . 4771 1 296 . 1 1 32 32 TYR HB3 H 1 2.89 0.01 . 2 . . . . . . . . 4771 1 297 . 1 1 32 32 TYR N N 15 124.43 0.10 . 1 . . . . . . . . 4771 1 298 . 1 1 33 33 ASP C C 13 176.03 0.10 . 1 . . . . . . . . 4771 1 299 . 1 1 33 33 ASP CA C 13 53.34 0.10 . 1 . . . . . . . . 4771 1 300 . 1 1 33 33 ASP CB C 13 40.15 0.10 . 1 . . . . . . . . 4771 1 301 . 1 1 33 33 ASP H H 1 8.28 0.01 . 1 . . . . . . . . 4771 1 302 . 1 1 33 33 ASP HA H 1 4.62 0.01 . 1 . . . . . . . . 4771 1 303 . 1 1 33 33 ASP HB2 H 1 2.67 0.01 . 2 . . . . . . . . 4771 1 304 . 1 1 33 33 ASP HB3 H 1 2.48 0.01 . 2 . . . . . . . . 4771 1 305 . 1 1 33 33 ASP N N 15 119.35 0.10 . 1 . . . . . . . . 4771 1 306 . 1 1 34 34 ALA C C 13 178.90 0.10 . 1 . . . . . . . . 4771 1 307 . 1 1 34 34 ALA CA C 13 54.94 0.12 . 1 . . . . . . . . 4771 1 308 . 1 1 34 34 ALA CB C 13 18.34 0.10 . 1 . . . . . . . . 4771 1 309 . 1 1 34 34 ALA H H 1 8.16 0.01 . 1 . . . . . . . . 4771 1 310 . 1 1 34 34 ALA HA H 1 3.73 0.01 . 1 . . . . . . . . 4771 1 311 . 1 1 34 34 ALA HB1 H 1 1.03 0.01 . 1 . . . . . . . . 4771 1 312 . 1 1 34 34 ALA HB2 H 1 1.03 0.01 . 1 . . . . . . . . 4771 1 313 . 1 1 34 34 ALA HB3 H 1 1.03 0.01 . 1 . . . . . . . . 4771 1 314 . 1 1 34 34 ALA N N 15 124.23 0.10 . 1 . . . . . . . . 4771 1 315 . 1 1 35 35 SER C C 13 176.43 0.10 . 1 . . . . . . . . 4771 1 316 . 1 1 35 35 SER CA C 13 60.85 0.10 . 1 . . . . . . . . 4771 1 317 . 1 1 35 35 SER CB C 13 62.48 0.10 . 1 . . . . . . . . 4771 1 318 . 1 1 35 35 SER H H 1 8.39 0.01 . 1 . . . . . . . . 4771 1 319 . 1 1 35 35 SER HA H 1 3.86 0.01 . 1 . . . . . . . . 4771 1 320 . 1 1 35 35 SER HB2 H 1 3.72 0.01 . 2 . . . . . . . . 4771 1 321 . 1 1 35 35 SER HB3 H 1 3.69 0.02 . 2 . . . . . . . . 4771 1 322 . 1 1 35 35 SER N N 15 112.21 0.10 . 1 . . . . . . . . 4771 1 323 . 1 1 36 36 SER C C 13 174.34 0.10 . 1 . . . . . . . . 4771 1 324 . 1 1 36 36 SER CA C 13 60.14 0.10 . 1 . . . . . . . . 4771 1 325 . 1 1 36 36 SER CB C 13 62.64 0.10 . 1 . . . . . . . . 4771 1 326 . 1 1 36 36 SER H H 1 7.72 0.01 . 1 . . . . . . . . 4771 1 327 . 1 1 36 36 SER HA H 1 4.12 0.01 . 1 . . . . . . . . 4771 1 328 . 1 1 36 36 SER HB2 H 1 3.54 0.01 . 2 . . . . . . . . 4771 1 329 . 1 1 36 36 SER HB3 H 1 3.50 0.01 . 2 . . . . . . . . 4771 1 330 . 1 1 36 36 SER N N 15 117.41 0.10 . 1 . . . . . . . . 4771 1 331 . 1 1 37 37 TYR C C 13 174.14 0.10 . 1 . . . . . . . . 4771 1 332 . 1 1 37 37 TYR CA C 13 56.68 0.10 . 1 . . . . . . . . 4771 1 333 . 1 1 37 37 TYR CB C 13 39.43 0.10 . 1 . . . . . . . . 4771 1 334 . 1 1 37 37 TYR H H 1 7.69 0.01 . 1 . . . . . . . . 4771 1 335 . 1 1 37 37 TYR HA H 1 4.48 0.01 . 1 . . . . . . . . 4771 1 336 . 1 1 37 37 TYR HB2 H 1 3.29 0.01 . 2 . . . . . . . . 4771 1 337 . 1 1 37 37 TYR HB3 H 1 2.64 0.01 . 2 . . . . . . . . 4771 1 338 . 1 1 37 37 TYR N N 15 119.08 0.10 . 1 . . . . . . . . 4771 1 339 . 1 1 38 38 ALA C C 13 178.47 0.10 . 1 . . . . . . . . 4771 1 340 . 1 1 38 38 ALA CA C 13 53.95 0.10 . 1 . . . . . . . . 4771 1 341 . 1 1 38 38 ALA CB C 13 17.89 0.10 . 1 . . . . . . . . 4771 1 342 . 1 1 38 38 ALA H H 1 7.00 0.01 . 1 . . . . . . . . 4771 1 343 . 1 1 38 38 ALA HA H 1 3.82 0.01 . 1 . . . . . . . . 4771 1 344 . 1 1 38 38 ALA HB1 H 1 1.11 0.01 . 1 . . . . . . . . 4771 1 345 . 1 1 38 38 ALA HB2 H 1 1.11 0.01 . 1 . . . . . . . . 4771 1 346 . 1 1 38 38 ALA HB3 H 1 1.11 0.01 . 1 . . . . . . . . 4771 1 347 . 1 1 38 38 ALA N N 15 121.75 0.10 . 1 . . . . . . . . 4771 1 348 . 1 1 39 39 GLY C C 13 174.14 0.10 . 1 . . . . . . . . 4771 1 349 . 1 1 39 39 GLY CA C 13 45.18 0.10 . 1 . . . . . . . . 4771 1 350 . 1 1 39 39 GLY H H 1 8.57 0.01 . 1 . . . . . . . . 4771 1 351 . 1 1 39 39 GLY HA2 H 1 4.16 0.01 . 2 . . . . . . . . 4771 1 352 . 1 1 39 39 GLY HA3 H 1 3.56 0.01 . 2 . . . . . . . . 4771 1 353 . 1 1 39 39 GLY N N 15 111.06 0.10 . 1 . . . . . . . . 4771 1 354 . 1 1 40 40 LYS C C 13 174.43 0.10 . 1 . . . . . . . . 4771 1 355 . 1 1 40 40 LYS CA C 13 54.71 0.10 . 1 . . . . . . . . 4771 1 356 . 1 1 40 40 LYS CB C 13 34.83 0.11 . 1 . . . . . . . . 4771 1 357 . 1 1 40 40 LYS CD C 13 28.94 0.10 . 1 . . . . . . . . 4771 1 358 . 1 1 40 40 LYS CE C 13 42.43 0.10 . 1 . . . . . . . . 4771 1 359 . 1 1 40 40 LYS CG C 13 25.26 0.10 . 1 . . . . . . . . 4771 1 360 . 1 1 40 40 LYS H H 1 7.83 0.01 . 1 . . . . . . . . 4771 1 361 . 1 1 40 40 LYS HA H 1 4.65 0.02 . 1 . . . . . . . . 4771 1 362 . 1 1 40 40 LYS HB2 H 1 2.08 0.01 . 2 . . . . . . . . 4771 1 363 . 1 1 40 40 LYS HB3 H 1 1.81 0.02 . 2 . . . . . . . . 4771 1 364 . 1 1 40 40 LYS HD2 H 1 1.65 0.02 . 2 . . . . . . . . 4771 1 365 . 1 1 40 40 LYS HD3 H 1 1.55 0.01 . 2 . . . . . . . . 4771 1 366 . 1 1 40 40 LYS HE2 H 1 2.98 0.01 . 2 . . . . . . . . 4771 1 367 . 1 1 40 40 LYS HG2 H 1 1.36 0.01 . 2 . . . . . . . . 4771 1 368 . 1 1 40 40 LYS N N 15 120.34 0.10 . 1 . . . . . . . . 4771 1 369 . 1 1 41 41 THR C C 13 173.25 0.10 . 1 . . . . . . . . 4771 1 370 . 1 1 41 41 THR CA C 13 60.83 0.10 . 1 . . . . . . . . 4771 1 371 . 1 1 41 41 THR CB C 13 71.80 0.10 . 1 . . . . . . . . 4771 1 372 . 1 1 41 41 THR CG2 C 13 20.84 0.10 . 1 . . . . . . . . 4771 1 373 . 1 1 41 41 THR H H 1 8.13 0.01 . 1 . . . . . . . . 4771 1 374 . 1 1 41 41 THR HA H 1 4.99 0.01 . 1 . . . . . . . . 4771 1 375 . 1 1 41 41 THR HB H 1 3.81 0.01 . 2 . . . . . . . . 4771 1 376 . 1 1 41 41 THR HG21 H 1 0.92 0.01 . 1 . . . . . . . . 4771 1 377 . 1 1 41 41 THR HG22 H 1 0.92 0.01 . 1 . . . . . . . . 4771 1 378 . 1 1 41 41 THR HG23 H 1 0.92 0.01 . 1 . . . . . . . . 4771 1 379 . 1 1 41 41 THR N N 15 111.81 0.10 . 1 . . . . . . . . 4771 1 380 . 1 1 42 42 CYS C C 13 173.63 0.10 . 5 . . . . . . . . 4771 1 381 . 1 1 42 42 CYS CA C 13 56.58 0.10 . 1 . . . . . . . . 4771 1 382 . 1 1 42 42 CYS CB C 13 48.71 0.10 . 1 . . . . . . . . 4771 1 383 . 1 1 42 42 CYS H H 1 8.58 0.01 . 1 . . . . . . . . 4771 1 384 . 1 1 42 42 CYS HA H 1 5.05 0.01 . 1 . . . . . . . . 4771 1 385 . 1 1 42 42 CYS HB2 H 1 2.96 0.01 . 2 . . . . . . . . 4771 1 386 . 1 1 42 42 CYS HB3 H 1 2.53 0.01 . 2 . . . . . . . . 4771 1 387 . 1 1 42 42 CYS N N 15 121.86 0.10 . 1 . . . . . . . . 4771 1 388 . 1 1 43 43 THR C C 13 172.85 0.10 . 1 . . . . . . . . 4771 1 389 . 1 1 43 43 THR CA C 13 62.48 0.10 . 1 . . . . . . . . 4771 1 390 . 1 1 43 43 THR CB C 13 69.62 0.10 . 1 . . . . . . . . 4771 1 391 . 1 1 43 43 THR CG2 C 13 21.52 0.10 . 1 . . . . . . . . 4771 1 392 . 1 1 43 43 THR H H 1 8.92 0.01 . 1 . . . . . . . . 4771 1 393 . 1 1 43 43 THR HA H 1 4.95 0.01 . 1 . . . . . . . . 4771 1 394 . 1 1 43 43 THR HB H 1 3.62 0.01 . 2 . . . . . . . . 4771 1 395 . 1 1 43 43 THR HG21 H 1 1.04 0.01 . 1 . . . . . . . . 4771 1 396 . 1 1 43 43 THR HG22 H 1 1.04 0.01 . 1 . . . . . . . . 4771 1 397 . 1 1 43 43 THR HG23 H 1 1.04 0.01 . 1 . . . . . . . . 4771 1 398 . 1 1 43 43 THR N N 15 128.91 0.10 . 1 . . . . . . . . 4771 1 399 . 1 1 44 44 LEU C C 13 174.52 0.10 . 1 . . . . . . . . 4771 1 400 . 1 1 44 44 LEU CA C 13 52.89 0.14 . 1 . . . . . . . . 4771 1 401 . 1 1 44 44 LEU CB C 13 44.70 0.10 . 1 . . . . . . . . 4771 1 402 . 1 1 44 44 LEU CD1 C 13 23.87 0.10 . 2 . . . . . . . . 4771 1 403 . 1 1 44 44 LEU CD2 C 13 25.44 0.10 . 2 . . . . . . . . 4771 1 404 . 1 1 44 44 LEU CG C 13 26.13 0.10 . 1 . . . . . . . . 4771 1 405 . 1 1 44 44 LEU H H 1 9.13 0.01 . 1 . . . . . . . . 4771 1 406 . 1 1 44 44 LEU HA H 1 4.74 0.01 . 1 . . . . . . . . 4771 1 407 . 1 1 44 44 LEU HB2 H 1 1.65 0.01 . 2 . . . . . . . . 4771 1 408 . 1 1 44 44 LEU HB3 H 1 1.06 0.01 . 2 . . . . . . . . 4771 1 409 . 1 1 44 44 LEU HD11 H 1 0.57 0.02 . 2 . . . . . . . . 4771 1 410 . 1 1 44 44 LEU HD12 H 1 0.57 0.02 . 2 . . . . . . . . 4771 1 411 . 1 1 44 44 LEU HD13 H 1 0.57 0.02 . 2 . . . . . . . . 4771 1 412 . 1 1 44 44 LEU HD21 H 1 0.53 0.01 . 2 . . . . . . . . 4771 1 413 . 1 1 44 44 LEU HD22 H 1 0.53 0.01 . 2 . . . . . . . . 4771 1 414 . 1 1 44 44 LEU HD23 H 1 0.53 0.01 . 2 . . . . . . . . 4771 1 415 . 1 1 44 44 LEU HG H 1 1.60 0.01 . 2 . . . . . . . . 4771 1 416 . 1 1 44 44 LEU N N 15 128.45 0.10 . 1 . . . . . . . . 4771 1 417 . 1 1 45 45 ARG C C 13 175.26 0.10 . 1 . . . . . . . . 4771 1 418 . 1 1 45 45 ARG CA C 13 54.63 0.10 . 1 . . . . . . . . 4771 1 419 . 1 1 45 45 ARG CB C 13 29.72 0.10 . 1 . . . . . . . . 4771 1 420 . 1 1 45 45 ARG CD C 13 41.18 0.10 . 1 . . . . . . . . 4771 1 421 . 1 1 45 45 ARG CG C 13 26.16 0.12 . 1 . . . . . . . . 4771 1 422 . 1 1 45 45 ARG H H 1 9.12 0.01 . 1 . . . . . . . . 4771 1 423 . 1 1 45 45 ARG HA H 1 4.66 0.01 . 1 . . . . . . . . 4771 1 424 . 1 1 45 45 ARG HB2 H 1 1.70 0.01 . 2 . . . . . . . . 4771 1 425 . 1 1 45 45 ARG HB3 H 1 1.58 0.01 . 2 . . . . . . . . 4771 1 426 . 1 1 45 45 ARG HD2 H 1 3.08 0.01 . 2 . . . . . . . . 4771 1 427 . 1 1 45 45 ARG HD3 H 1 2.93 0.01 . 2 . . . . . . . . 4771 1 428 . 1 1 45 45 ARG HG2 H 1 1.36 0.01 . 2 . . . . . . . . 4771 1 429 . 1 1 45 45 ARG HG3 H 1 1.10 0.01 . 2 . . . . . . . . 4771 1 430 . 1 1 45 45 ARG N N 15 123.21 0.10 . 1 . . . . . . . . 4771 1 431 . 1 1 46 46 ILE C C 13 173.01 0.10 . 1 . . . . . . . . 4771 1 432 . 1 1 46 46 ILE CA C 13 59.89 0.11 . 1 . . . . . . . . 4771 1 433 . 1 1 46 46 ILE CB C 13 41.62 0.10 . 1 . . . . . . . . 4771 1 434 . 1 1 46 46 ILE CD1 C 13 14.30 0.10 . 1 . . . . . . . . 4771 1 435 . 1 1 46 46 ILE CG1 C 13 26.70 0.10 . 1 . . . . . . . . 4771 1 436 . 1 1 46 46 ILE CG2 C 13 16.82 0.10 . 1 . . . . . . . . 4771 1 437 . 1 1 46 46 ILE H H 1 8.89 0.01 . 1 . . . . . . . . 4771 1 438 . 1 1 46 46 ILE HA H 1 4.74 0.01 . 1 . . . . . . . . 4771 1 439 . 1 1 46 46 ILE HB H 1 1.69 0.01 . 2 . . . . . . . . 4771 1 440 . 1 1 46 46 ILE HD11 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 441 . 1 1 46 46 ILE HD12 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 442 . 1 1 46 46 ILE HD13 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 443 . 1 1 46 46 ILE HG12 H 1 1.62 0.01 . 2 . . . . . . . . 4771 1 444 . 1 1 46 46 ILE HG13 H 1 1.17 0.01 . 2 . . . . . . . . 4771 1 445 . 1 1 46 46 ILE HG21 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 446 . 1 1 46 46 ILE HG22 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 447 . 1 1 46 46 ILE HG23 H 1 0.83 0.01 . 1 . . . . . . . . 4771 1 448 . 1 1 46 46 ILE N N 15 126.60 0.10 . 1 . . . . . . . . 4771 1 449 . 1 1 47 47 LYS C C 13 175.40 0.10 . 1 . . . . . . . . 4771 1 450 . 1 1 47 47 LYS CA C 13 55.26 0.10 . 1 . . . . . . . . 4771 1 451 . 1 1 47 47 LYS CB C 13 35.22 0.10 . 1 . . . . . . . . 4771 1 452 . 1 1 47 47 LYS CD C 13 29.64 0.10 . 1 . . . . . . . . 4771 1 453 . 1 1 47 47 LYS CE C 13 42.03 0.10 . 1 . . . . . . . . 4771 1 454 . 1 1 47 47 LYS CG C 13 24.69 0.12 . 1 . . . . . . . . 4771 1 455 . 1 1 47 47 LYS H H 1 7.86 0.01 . 1 . . . . . . . . 4771 1 456 . 1 1 47 47 LYS HA H 1 4.99 0.01 . 1 . . . . . . . . 4771 1 457 . 1 1 47 47 LYS HB2 H 1 1.73 0.01 . 2 . . . . . . . . 4771 1 458 . 1 1 47 47 LYS HB3 H 1 1.58 0.01 . 2 . . . . . . . . 4771 1 459 . 1 1 47 47 LYS HD2 H 1 1.52 0.01 . 2 . . . . . . . . 4771 1 460 . 1 1 47 47 LYS HE2 H 1 2.78 0.01 . 2 . . . . . . . . 4771 1 461 . 1 1 47 47 LYS HG2 H 1 1.40 0.02 . 2 . . . . . . . . 4771 1 462 . 1 1 47 47 LYS N N 15 121.60 0.10 . 1 . . . . . . . . 4771 1 463 . 1 1 48 48 LEU C C 13 177.14 0.10 . 1 . . . . . . . . 4771 1 464 . 1 1 48 48 LEU CA C 13 53.19 0.10 . 1 . . . . . . . . 4771 1 465 . 1 1 48 48 LEU CB C 13 45.76 0.10 . 1 . . . . . . . . 4771 1 466 . 1 1 48 48 LEU CD1 C 13 26.47 0.10 . 2 . . . . . . . . 4771 1 467 . 1 1 48 48 LEU CD2 C 13 24.13 0.10 . 2 . . . . . . . . 4771 1 468 . 1 1 48 48 LEU CG C 13 26.56 0.10 . 1 . . . . . . . . 4771 1 469 . 1 1 48 48 LEU H H 1 8.12 0.01 . 1 . . . . . . . . 4771 1 470 . 1 1 48 48 LEU HA H 1 5.23 0.01 . 1 . . . . . . . . 4771 1 471 . 1 1 48 48 LEU HB2 H 1 1.65 0.02 . 2 . . . . . . . . 4771 1 472 . 1 1 48 48 LEU HD11 H 1 0.96 0.01 . 2 . . . . . . . . 4771 1 473 . 1 1 48 48 LEU HD12 H 1 0.96 0.01 . 2 . . . . . . . . 4771 1 474 . 1 1 48 48 LEU HD13 H 1 0.96 0.01 . 2 . . . . . . . . 4771 1 475 . 1 1 48 48 LEU HD21 H 1 0.87 0.01 . 2 . . . . . . . . 4771 1 476 . 1 1 48 48 LEU HD22 H 1 0.87 0.01 . 2 . . . . . . . . 4771 1 477 . 1 1 48 48 LEU HD23 H 1 0.87 0.01 . 2 . . . . . . . . 4771 1 478 . 1 1 48 48 LEU HG H 1 1.86 0.01 . 2 . . . . . . . . 4771 1 479 . 1 1 48 48 LEU N N 15 123.90 0.10 . 1 . . . . . . . . 4771 1 480 . 1 1 49 49 ALA CA C 13 50.31 0.10 . 1 . . . . . . . . 4771 1 481 . 1 1 49 49 ALA CB C 13 19.15 0.10 . 1 . . . . . . . . 4771 1 482 . 1 1 49 49 ALA H H 1 9.02 0.01 . 1 . . . . . . . . 4771 1 483 . 1 1 49 49 ALA HA H 1 4.79 0.01 . 1 . . . . . . . . 4771 1 484 . 1 1 49 49 ALA HB1 H 1 1.59 0.01 . 1 . . . . . . . . 4771 1 485 . 1 1 49 49 ALA HB2 H 1 1.59 0.01 . 1 . . . . . . . . 4771 1 486 . 1 1 49 49 ALA HB3 H 1 1.59 0.01 . 1 . . . . . . . . 4771 1 487 . 1 1 49 49 ALA N N 15 126.15 0.10 . 1 . . . . . . . . 4771 1 488 . 1 1 50 50 PRO C C 13 175.78 0.10 . 1 . . . . . . . . 4771 1 489 . 1 1 50 50 PRO CA C 13 64.83 0.10 . 1 . . . . . . . . 4771 1 490 . 1 1 50 50 PRO CB C 13 31.08 0.12 . 1 . . . . . . . . 4771 1 491 . 1 1 50 50 PRO CD C 13 50.27 0.10 . 1 . . . . . . . . 4771 1 492 . 1 1 50 50 PRO CG C 13 27.00 0.10 . 1 . . . . . . . . 4771 1 493 . 1 1 50 50 PRO HA H 1 3.21 0.01 . 1 . . . . . . . . 4771 1 494 . 1 1 50 50 PRO HB2 H 1 1.53 0.01 . 2 . . . . . . . . 4771 1 495 . 1 1 50 50 PRO HD2 H 1 3.70 0.01 . 2 . . . . . . . . 4771 1 496 . 1 1 50 50 PRO HD3 H 1 3.62 0.01 . 2 . . . . . . . . 4771 1 497 . 1 1 50 50 PRO HG2 H 1 1.82 0.01 . 2 . . . . . . . . 4771 1 498 . 1 1 50 50 PRO HG3 H 1 1.47 0.01 . 2 . . . . . . . . 4771 1 499 . 1 1 51 51 ASP C C 13 176.99 0.10 . 1 . . . . . . . . 4771 1 500 . 1 1 51 51 ASP CA C 13 52.60 0.10 . 1 . . . . . . . . 4771 1 501 . 1 1 51 51 ASP CB C 13 39.90 0.10 . 1 . . . . . . . . 4771 1 502 . 1 1 51 51 ASP H H 1 7.47 0.01 . 1 . . . . . . . . 4771 1 503 . 1 1 51 51 ASP HA H 1 4.34 0.01 . 1 . . . . . . . . 4771 1 504 . 1 1 51 51 ASP HB2 H 1 2.89 0.01 . 2 . . . . . . . . 4771 1 505 . 1 1 51 51 ASP HB3 H 1 2.41 0.02 . 2 . . . . . . . . 4771 1 506 . 1 1 51 51 ASP N N 15 111.79 0.10 . 1 . . . . . . . . 4771 1 507 . 1 1 52 52 GLY C C 13 171.58 0.10 . 1 . . . . . . . . 4771 1 508 . 1 1 52 52 GLY CA C 13 44.83 0.10 . 1 . . . . . . . . 4771 1 509 . 1 1 52 52 GLY H H 1 8.40 0.01 . 1 . . . . . . . . 4771 1 510 . 1 1 52 52 GLY HA2 H 1 3.25 0.01 . 2 . . . . . . . . 4771 1 511 . 1 1 52 52 GLY HA3 H 1 4.07 0.01 . 2 . . . . . . . . 4771 1 512 . 1 1 52 52 GLY N N 15 109.03 0.10 . 1 . . . . . . . . 4771 1 513 . 1 1 53 53 MET C C 13 175.76 0.10 . 1 . . . . . . . . 4771 1 514 . 1 1 53 53 MET CA C 13 56.56 0.10 . 1 . . . . . . . . 4771 1 515 . 1 1 53 53 MET CB C 13 32.31 0.10 . 1 . . . . . . . . 4771 1 516 . 1 1 53 53 MET CG C 13 32.61 0.10 . 1 . . . . . . . . 4771 1 517 . 1 1 53 53 MET H H 1 7.37 0.01 . 1 . . . . . . . . 4771 1 518 . 1 1 53 53 MET HA H 1 4.01 0.01 . 1 . . . . . . . . 4771 1 519 . 1 1 53 53 MET HB2 H 1 2.50 0.01 . 2 . . . . . . . . 4771 1 520 . 1 1 53 53 MET HB3 H 1 2.36 0.01 . 2 . . . . . . . . 4771 1 521 . 1 1 53 53 MET HG2 H 1 2.07 0.01 . 2 . . . . . . . . 4771 1 522 . 1 1 53 53 MET HG3 H 1 1.80 0.01 . 2 . . . . . . . . 4771 1 523 . 1 1 53 53 MET N N 15 117.46 0.10 . 1 . . . . . . . . 4771 1 524 . 1 1 54 54 LEU C C 13 176.25 0.10 . 5 . . . . . . . . 4771 1 525 . 1 1 54 54 LEU CA C 13 55.21 0.10 . 1 . . . . . . . . 4771 1 526 . 1 1 54 54 LEU CB C 13 42.19 0.10 . 1 . . . . . . . . 4771 1 527 . 1 1 54 54 LEU CD1 C 13 24.88 0.10 . 2 . . . . . . . . 4771 1 528 . 1 1 54 54 LEU CD2 C 13 25.84 0.10 . 2 . . . . . . . . 4771 1 529 . 1 1 54 54 LEU CG C 13 26.69 0.10 . 1 . . . . . . . . 4771 1 530 . 1 1 54 54 LEU H H 1 8.58 0.01 . 1 . . . . . . . . 4771 1 531 . 1 1 54 54 LEU HA H 1 4.37 0.01 . 1 . . . . . . . . 4771 1 532 . 1 1 54 54 LEU HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4771 1 533 . 1 1 54 54 LEU HB3 H 1 1.31 0.01 . 2 . . . . . . . . 4771 1 534 . 1 1 54 54 LEU HD11 H 1 0.79 0.01 . 2 . . . . . . . . 4771 1 535 . 1 1 54 54 LEU HD12 H 1 0.79 0.01 . 2 . . . . . . . . 4771 1 536 . 1 1 54 54 LEU HD13 H 1 0.79 0.01 . 2 . . . . . . . . 4771 1 537 . 1 1 54 54 LEU HD21 H 1 0.68 0.01 . 2 . . . . . . . . 4771 1 538 . 1 1 54 54 LEU HD22 H 1 0.68 0.01 . 2 . . . . . . . . 4771 1 539 . 1 1 54 54 LEU HD23 H 1 0.68 0.01 . 2 . . . . . . . . 4771 1 540 . 1 1 54 54 LEU HG H 1 1.30 0.01 . 2 . . . . . . . . 4771 1 541 . 1 1 54 54 LEU N N 15 125.39 0.10 . 1 . . . . . . . . 4771 1 542 . 1 1 55 55 LEU C C 13 177.53 0.10 . 1 . . . . . . . . 4771 1 543 . 1 1 55 55 LEU CA C 13 55.75 0.10 . 1 . . . . . . . . 4771 1 544 . 1 1 55 55 LEU CB C 13 42.45 0.10 . 1 . . . . . . . . 4771 1 545 . 1 1 55 55 LEU CD1 C 13 25.42 0.10 . 2 . . . . . . . . 4771 1 546 . 1 1 55 55 LEU CD2 C 13 22.03 0.10 . 2 . . . . . . . . 4771 1 547 . 1 1 55 55 LEU CG C 13 26.47 0.10 . 1 . . . . . . . . 4771 1 548 . 1 1 55 55 LEU H H 1 8.92 0.01 . 1 . . . . . . . . 4771 1 549 . 1 1 55 55 LEU HA H 1 4.29 0.01 . 1 . . . . . . . . 4771 1 550 . 1 1 55 55 LEU HB2 H 1 1.49 0.01 . 2 . . . . . . . . 4771 1 551 . 1 1 55 55 LEU HB3 H 1 1.40 0.01 . 2 . . . . . . . . 4771 1 552 . 1 1 55 55 LEU HD11 H 1 0.79 0.01 . 1 . . . . . . . . 4771 1 553 . 1 1 55 55 LEU HD12 H 1 0.79 0.01 . 1 . . . . . . . . 4771 1 554 . 1 1 55 55 LEU HD13 H 1 0.79 0.01 . 1 . . . . . . . . 4771 1 555 . 1 1 55 55 LEU HD21 H 1 0.79 0.01 . 1 . . . . . . . . 4771 1 556 . 1 1 55 55 LEU HD22 H 1 0.79 0.01 . 1 . . . . . . . . 4771 1 557 . 1 1 55 55 LEU HD23 H 1 0.79 0.01 . 1 . . . . . . . . 4771 1 558 . 1 1 55 55 LEU HG H 1 1.62 0.01 . 2 . . . . . . . . 4771 1 559 . 1 1 55 55 LEU N N 15 128.91 0.10 . 1 . . . . . . . . 4771 1 560 . 1 1 56 56 ASP C C 13 179.43 0.10 . 5 . . . . . . . . 4771 1 561 . 1 1 56 56 ASP CA C 13 53.55 0.12 . 1 . . . . . . . . 4771 1 562 . 1 1 56 56 ASP CB C 13 44.65 0.10 . 1 . . . . . . . . 4771 1 563 . 1 1 56 56 ASP H H 1 7.72 0.01 . 1 . . . . . . . . 4771 1 564 . 1 1 56 56 ASP HA H 1 4.69 0.01 . 1 . . . . . . . . 4771 1 565 . 1 1 56 56 ASP HB2 H 1 2.68 0.01 . 2 . . . . . . . . 4771 1 566 . 1 1 56 56 ASP HB3 H 1 2.23 0.01 . 2 . . . . . . . . 4771 1 567 . 1 1 56 56 ASP N N 15 115.16 0.10 . 1 . . . . . . . . 4771 1 568 . 1 1 57 57 ILE C C 13 172.21 0.10 . 1 . . . . . . . . 4771 1 569 . 1 1 57 57 ILE CA C 13 59.56 0.10 . 1 . . . . . . . . 4771 1 570 . 1 1 57 57 ILE CB C 13 40.24 0.10 . 1 . . . . . . . . 4771 1 571 . 1 1 57 57 ILE CD1 C 13 15.00 0.10 . 1 . . . . . . . . 4771 1 572 . 1 1 57 57 ILE CG1 C 13 27.77 0.11 . 1 . . . . . . . . 4771 1 573 . 1 1 57 57 ILE CG2 C 13 14.28 0.10 . 1 . . . . . . . . 4771 1 574 . 1 1 57 57 ILE H H 1 7.90 0.01 . 1 . . . . . . . . 4771 1 575 . 1 1 57 57 ILE HA H 1 5.17 0.01 . 1 . . . . . . . . 4771 1 576 . 1 1 57 57 ILE HB H 1 1.87 0.01 . 2 . . . . . . . . 4771 1 577 . 1 1 57 57 ILE HD11 H 1 0.64 0.01 . 1 . . . . . . . . 4771 1 578 . 1 1 57 57 ILE HD12 H 1 0.64 0.01 . 1 . . . . . . . . 4771 1 579 . 1 1 57 57 ILE HD13 H 1 0.64 0.01 . 1 . . . . . . . . 4771 1 580 . 1 1 57 57 ILE HG12 H 1 1.35 0.03 . 2 . . . . . . . . 4771 1 581 . 1 1 57 57 ILE HG13 H 1 0.76 0.01 . 2 . . . . . . . . 4771 1 582 . 1 1 57 57 ILE HG21 H 1 0.77 0.03 . 1 . . . . . . . . 4771 1 583 . 1 1 57 57 ILE HG22 H 1 0.77 0.03 . 1 . . . . . . . . 4771 1 584 . 1 1 57 57 ILE HG23 H 1 0.77 0.03 . 1 . . . . . . . . 4771 1 585 . 1 1 57 57 ILE N N 15 119.29 0.10 . 1 . . . . . . . . 4771 1 586 . 1 1 58 58 LYS CA C 13 52.65 0.10 . 1 . . . . . . . . 4771 1 587 . 1 1 58 58 LYS CB C 13 35.71 0.11 . 1 . . . . . . . . 4771 1 588 . 1 1 58 58 LYS CD C 13 28.93 0.10 . 1 . . . . . . . . 4771 1 589 . 1 1 58 58 LYS CE C 13 41.95 0.10 . 1 . . . . . . . . 4771 1 590 . 1 1 58 58 LYS CG C 13 24.07 0.10 . 1 . . . . . . . . 4771 1 591 . 1 1 58 58 LYS H H 1 8.31 0.01 . 1 . . . . . . . . 4771 1 592 . 1 1 58 58 LYS HA H 1 4.86 0.01 . 1 . . . . . . . . 4771 1 593 . 1 1 58 58 LYS HB2 H 1 1.73 0.01 . 2 . . . . . . . . 4771 1 594 . 1 1 58 58 LYS HB3 H 1 1.64 0.01 . 2 . . . . . . . . 4771 1 595 . 1 1 58 58 LYS HD2 H 1 1.61 0.01 . 2 . . . . . . . . 4771 1 596 . 1 1 58 58 LYS HE2 H 1 2.92 0.01 . 2 . . . . . . . . 4771 1 597 . 1 1 58 58 LYS HG2 H 1 1.32 0.01 . 2 . . . . . . . . 4771 1 598 . 1 1 58 58 LYS N N 15 124.67 0.10 . 1 . . . . . . . . 4771 1 599 . 1 1 59 59 PRO C C 13 176.33 0.10 . 1 . . . . . . . . 4771 1 600 . 1 1 59 59 PRO CA C 13 62.60 0.10 . 1 . . . . . . . . 4771 1 601 . 1 1 59 59 PRO CB C 13 31.67 0.10 . 1 . . . . . . . . 4771 1 602 . 1 1 59 59 PRO CD C 13 50.44 0.10 . 1 . . . . . . . . 4771 1 603 . 1 1 59 59 PRO CG C 13 27.37 0.10 . 1 . . . . . . . . 4771 1 604 . 1 1 59 59 PRO HA H 1 4.71 0.01 . 1 . . . . . . . . 4771 1 605 . 1 1 59 59 PRO HB2 H 1 2.02 0.01 . 2 . . . . . . . . 4771 1 606 . 1 1 59 59 PRO HB3 H 1 1.91 0.02 . 2 . . . . . . . . 4771 1 607 . 1 1 59 59 PRO HD2 H 1 3.69 0.01 . 2 . . . . . . . . 4771 1 608 . 1 1 59 59 PRO HD3 H 1 3.66 0.01 . 2 . . . . . . . . 4771 1 609 . 1 1 59 59 PRO HG2 H 1 2.21 0.01 . 2 . . . . . . . . 4771 1 610 . 1 1 59 59 PRO HG3 H 1 1.72 0.01 . 2 . . . . . . . . 4771 1 611 . 1 1 60 60 GLU C C 13 175.77 0.10 . 1 . . . . . . . . 4771 1 612 . 1 1 60 60 GLU CA C 13 56.01 0.10 . 1 . . . . . . . . 4771 1 613 . 1 1 60 60 GLU CB C 13 31.51 0.13 . 1 . . . . . . . . 4771 1 614 . 1 1 60 60 GLU CG C 13 36.95 0.10 . 1 . . . . . . . . 4771 1 615 . 1 1 60 60 GLU H H 1 9.30 0.01 . 1 . . . . . . . . 4771 1 616 . 1 1 60 60 GLU HA H 1 4.48 0.01 . 1 . . . . . . . . 4771 1 617 . 1 1 60 60 GLU HB2 H 1 1.92 0.01 . 2 . . . . . . . . 4771 1 618 . 1 1 60 60 GLU HB3 H 1 1.58 0.01 . 2 . . . . . . . . 4771 1 619 . 1 1 60 60 GLU HG2 H 1 2.05 0.01 . 2 . . . . . . . . 4771 1 620 . 1 1 60 60 GLU N N 15 123.66 0.10 . 1 . . . . . . . . 4771 1 621 . 1 1 61 61 GLY C C 13 171.78 0.10 . 1 . . . . . . . . 4771 1 622 . 1 1 61 61 GLY CA C 13 45.05 0.10 . 1 . . . . . . . . 4771 1 623 . 1 1 61 61 GLY H H 1 7.58 0.01 . 1 . . . . . . . . 4771 1 624 . 1 1 61 61 GLY HA2 H 1 3.99 0.01 . 2 . . . . . . . . 4771 1 625 . 1 1 61 61 GLY HA3 H 1 4.16 0.01 . 2 . . . . . . . . 4771 1 626 . 1 1 61 61 GLY N N 15 107.03 0.10 . 1 . . . . . . . . 4771 1 627 . 1 1 62 62 GLY C C 13 174.67 0.10 . 1 . . . . . . . . 4771 1 628 . 1 1 62 62 GLY CA C 13 43.80 0.10 . 1 . . . . . . . . 4771 1 629 . 1 1 62 62 GLY H H 1 8.28 0.01 . 1 . . . . . . . . 4771 1 630 . 1 1 62 62 GLY HA2 H 1 3.68 0.01 . 2 . . . . . . . . 4771 1 631 . 1 1 62 62 GLY HA3 H 1 4.82 0.01 . 2 . . . . . . . . 4771 1 632 . 1 1 62 62 GLY N N 15 106.92 0.10 . 1 . . . . . . . . 4771 1 633 . 1 1 63 63 ASP CA C 13 52.66 0.10 . 1 . . . . . . . . 4771 1 634 . 1 1 63 63 ASP CB C 13 43.61 0.10 . 1 . . . . . . . . 4771 1 635 . 1 1 63 63 ASP H H 1 8.36 0.01 . 1 . . . . . . . . 4771 1 636 . 1 1 63 63 ASP HA H 1 4.80 0.01 . 1 . . . . . . . . 4771 1 637 . 1 1 63 63 ASP HB2 H 1 2.87 0.01 . 2 . . . . . . . . 4771 1 638 . 1 1 63 63 ASP HB3 H 1 2.68 0.01 . 2 . . . . . . . . 4771 1 639 . 1 1 63 63 ASP N N 15 122.61 0.10 . 1 . . . . . . . . 4771 1 640 . 1 1 64 64 PRO C C 13 178.96 0.10 . 1 . . . . . . . . 4771 1 641 . 1 1 64 64 PRO CA C 13 65.92 0.10 . 1 . . . . . . . . 4771 1 642 . 1 1 64 64 PRO CB C 13 32.20 0.11 . 1 . . . . . . . . 4771 1 643 . 1 1 64 64 PRO CD C 13 51.19 0.10 . 1 . . . . . . . . 4771 1 644 . 1 1 64 64 PRO CG C 13 27.46 0.11 . 1 . . . . . . . . 4771 1 645 . 1 1 64 64 PRO HA H 1 4.00 0.01 . 1 . . . . . . . . 4771 1 646 . 1 1 64 64 PRO HB2 H 1 2.31 0.01 . 2 . . . . . . . . 4771 1 647 . 1 1 64 64 PRO HB3 H 1 1.97 0.02 . 2 . . . . . . . . 4771 1 648 . 1 1 64 64 PRO HD2 H 1 4.27 0.01 . 2 . . . . . . . . 4771 1 649 . 1 1 64 64 PRO HD3 H 1 3.78 0.01 . 2 . . . . . . . . 4771 1 650 . 1 1 64 64 PRO HG2 H 1 2.14 0.01 . 2 . . . . . . . . 4771 1 651 . 1 1 64 64 PRO HG3 H 1 2.00 0.02 . 2 . . . . . . . . 4771 1 652 . 1 1 65 65 ALA C C 13 180.94 0.10 . 1 . . . . . . . . 4771 1 653 . 1 1 65 65 ALA CA C 13 55.18 0.10 . 1 . . . . . . . . 4771 1 654 . 1 1 65 65 ALA CB C 13 18.04 0.10 . 1 . . . . . . . . 4771 1 655 . 1 1 65 65 ALA H H 1 7.88 0.01 . 1 . . . . . . . . 4771 1 656 . 1 1 65 65 ALA HA H 1 4.18 0.01 . 1 . . . . . . . . 4771 1 657 . 1 1 65 65 ALA HB1 H 1 1.63 0.01 . 1 . . . . . . . . 4771 1 658 . 1 1 65 65 ALA HB2 H 1 1.63 0.01 . 1 . . . . . . . . 4771 1 659 . 1 1 65 65 ALA HB3 H 1 1.63 0.01 . 1 . . . . . . . . 4771 1 660 . 1 1 65 65 ALA N N 15 120.97 0.10 . 1 . . . . . . . . 4771 1 661 . 1 1 66 66 LEU C C 13 178.56 0.10 . 1 . . . . . . . . 4771 1 662 . 1 1 66 66 LEU CA C 13 57.53 0.10 . 1 . . . . . . . . 4771 1 663 . 1 1 66 66 LEU CB C 13 40.30 0.11 . 1 . . . . . . . . 4771 1 664 . 1 1 66 66 LEU CD1 C 13 27.06 0.10 . 2 . . . . . . . . 4771 1 665 . 1 1 66 66 LEU CD2 C 13 22.94 0.10 . 2 . . . . . . . . 4771 1 666 . 1 1 66 66 LEU CG C 13 27.77 0.10 . 1 . . . . . . . . 4771 1 667 . 1 1 66 66 LEU H H 1 8.72 0.01 . 1 . . . . . . . . 4771 1 668 . 1 1 66 66 LEU HA H 1 3.43 0.01 . 1 . . . . . . . . 4771 1 669 . 1 1 66 66 LEU HB2 H 1 1.87 0.01 . 2 . . . . . . . . 4771 1 670 . 1 1 66 66 LEU HB3 H 1 1.41 0.01 . 2 . . . . . . . . 4771 1 671 . 1 1 66 66 LEU HD11 H 1 0.82 0.01 . 2 . . . . . . . . 4771 1 672 . 1 1 66 66 LEU HD12 H 1 0.82 0.01 . 2 . . . . . . . . 4771 1 673 . 1 1 66 66 LEU HD13 H 1 0.82 0.01 . 2 . . . . . . . . 4771 1 674 . 1 1 66 66 LEU HD21 H 1 0.75 0.01 . 2 . . . . . . . . 4771 1 675 . 1 1 66 66 LEU HD22 H 1 0.75 0.01 . 2 . . . . . . . . 4771 1 676 . 1 1 66 66 LEU HD23 H 1 0.75 0.01 . 2 . . . . . . . . 4771 1 677 . 1 1 66 66 LEU HG H 1 1.29 0.02 . 2 . . . . . . . . 4771 1 678 . 1 1 66 66 LEU N N 15 121.96 0.10 . 1 . . . . . . . . 4771 1 679 . 1 1 67 67 CYS C C 13 176.53 0.10 . 1 . . . . . . . . 4771 1 680 . 1 1 67 67 CYS CA C 13 56.18 0.10 . 1 . . . . . . . . 4771 1 681 . 1 1 67 67 CYS CB C 13 37.62 0.10 . 1 . . . . . . . . 4771 1 682 . 1 1 67 67 CYS H H 1 9.01 0.01 . 1 . . . . . . . . 4771 1 683 . 1 1 67 67 CYS HA H 1 4.44 0.01 . 1 . . . . . . . . 4771 1 684 . 1 1 67 67 CYS HB2 H 1 2.99 0.01 . 2 . . . . . . . . 4771 1 685 . 1 1 67 67 CYS HB3 H 1 2.52 0.01 . 2 . . . . . . . . 4771 1 686 . 1 1 67 67 CYS N N 15 115.22 0.10 . 1 . . . . . . . . 4771 1 687 . 1 1 68 68 GLN C C 13 178.48 0.10 . 1 . . . . . . . . 4771 1 688 . 1 1 68 68 GLN CA C 13 59.13 0.10 . 1 . . . . . . . . 4771 1 689 . 1 1 68 68 GLN CB C 13 28.19 0.10 . 1 . . . . . . . . 4771 1 690 . 1 1 68 68 GLN CG C 13 33.57 0.10 . 1 . . . . . . . . 4771 1 691 . 1 1 68 68 GLN H H 1 7.97 0.01 . 1 . . . . . . . . 4771 1 692 . 1 1 68 68 GLN HA H 1 3.85 0.01 . 1 . . . . . . . . 4771 1 693 . 1 1 68 68 GLN HB2 H 1 2.08 0.01 . 2 . . . . . . . . 4771 1 694 . 1 1 68 68 GLN HE21 H 1 6.72 0.01 . 2 . . . . . . . . 4771 1 695 . 1 1 68 68 GLN HE22 H 1 7.42 0.01 . 2 . . . . . . . . 4771 1 696 . 1 1 68 68 GLN HG2 H 1 2.38 0.01 . 2 . . . . . . . . 4771 1 697 . 1 1 68 68 GLN N N 15 118.56 0.10 . 1 . . . . . . . . 4771 1 698 . 1 1 68 68 GLN NE2 N 15 112.30 0.10 . 1 . . . . . . . . 4771 1 699 . 1 1 69 69 ALA C C 13 180.15 0.10 . 1 . . . . . . . . 4771 1 700 . 1 1 69 69 ALA CA C 13 54.53 0.10 . 1 . . . . . . . . 4771 1 701 . 1 1 69 69 ALA CB C 13 18.57 0.10 . 1 . . . . . . . . 4771 1 702 . 1 1 69 69 ALA H H 1 7.61 0.01 . 1 . . . . . . . . 4771 1 703 . 1 1 69 69 ALA HA H 1 3.99 0.01 . 1 . . . . . . . . 4771 1 704 . 1 1 69 69 ALA HB1 H 1 1.21 0.01 . 1 . . . . . . . . 4771 1 705 . 1 1 69 69 ALA HB2 H 1 1.21 0.01 . 1 . . . . . . . . 4771 1 706 . 1 1 69 69 ALA HB3 H 1 1.21 0.01 . 1 . . . . . . . . 4771 1 707 . 1 1 69 69 ALA N N 15 123.24 0.10 . 1 . . . . . . . . 4771 1 708 . 1 1 70 70 ALA C C 13 178.25 0.10 . 1 . . . . . . . . 4771 1 709 . 1 1 70 70 ALA CA C 13 54.48 0.10 . 1 . . . . . . . . 4771 1 710 . 1 1 70 70 ALA CB C 13 17.79 0.10 . 1 . . . . . . . . 4771 1 711 . 1 1 70 70 ALA H H 1 8.97 0.01 . 1 . . . . . . . . 4771 1 712 . 1 1 70 70 ALA HA H 1 3.46 0.01 . 1 . . . . . . . . 4771 1 713 . 1 1 70 70 ALA HB1 H 1 0.97 0.01 . 1 . . . . . . . . 4771 1 714 . 1 1 70 70 ALA HB2 H 1 0.97 0.01 . 1 . . . . . . . . 4771 1 715 . 1 1 70 70 ALA HB3 H 1 0.97 0.01 . 1 . . . . . . . . 4771 1 716 . 1 1 70 70 ALA N N 15 122.38 0.10 . 1 . . . . . . . . 4771 1 717 . 1 1 71 71 LEU C C 13 178.34 0.10 . 1 . . . . . . . . 4771 1 718 . 1 1 71 71 LEU CA C 13 58.33 0.10 . 1 . . . . . . . . 4771 1 719 . 1 1 71 71 LEU CB C 13 41.87 0.10 . 1 . . . . . . . . 4771 1 720 . 1 1 71 71 LEU CD1 C 13 25.32 0.10 . 2 . . . . . . . . 4771 1 721 . 1 1 71 71 LEU CD2 C 13 24.57 0.10 . 2 . . . . . . . . 4771 1 722 . 1 1 71 71 LEU CG C 13 26.97 0.10 . 1 . . . . . . . . 4771 1 723 . 1 1 71 71 LEU H H 1 7.94 0.01 . 1 . . . . . . . . 4771 1 724 . 1 1 71 71 LEU HA H 1 3.60 0.01 . 1 . . . . . . . . 4771 1 725 . 1 1 71 71 LEU HB2 H 1 1.68 0.01 . 2 . . . . . . . . 4771 1 726 . 1 1 71 71 LEU HB3 H 1 1.44 0.01 . 2 . . . . . . . . 4771 1 727 . 1 1 71 71 LEU HD11 H 1 0.70 0.01 . 2 . . . . . . . . 4771 1 728 . 1 1 71 71 LEU HD12 H 1 0.70 0.01 . 2 . . . . . . . . 4771 1 729 . 1 1 71 71 LEU HD13 H 1 0.70 0.01 . 2 . . . . . . . . 4771 1 730 . 1 1 71 71 LEU HD21 H 1 0.64 0.01 . 2 . . . . . . . . 4771 1 731 . 1 1 71 71 LEU HD22 H 1 0.64 0.01 . 2 . . . . . . . . 4771 1 732 . 1 1 71 71 LEU HD23 H 1 0.64 0.01 . 2 . . . . . . . . 4771 1 733 . 1 1 71 71 LEU HG H 1 1.69 0.01 . 2 . . . . . . . . 4771 1 734 . 1 1 71 71 LEU N N 15 118.44 0.10 . 1 . . . . . . . . 4771 1 735 . 1 1 72 72 ALA C C 13 180.28 0.10 . 1 . . . . . . . . 4771 1 736 . 1 1 72 72 ALA CA C 13 54.70 0.10 . 1 . . . . . . . . 4771 1 737 . 1 1 72 72 ALA CB C 13 17.64 0.10 . 1 . . . . . . . . 4771 1 738 . 1 1 72 72 ALA H H 1 7.02 0.01 . 1 . . . . . . . . 4771 1 739 . 1 1 72 72 ALA HA H 1 3.88 0.01 . 1 . . . . . . . . 4771 1 740 . 1 1 72 72 ALA HB1 H 1 1.32 0.01 . 1 . . . . . . . . 4771 1 741 . 1 1 72 72 ALA HB2 H 1 1.32 0.01 . 1 . . . . . . . . 4771 1 742 . 1 1 72 72 ALA HB3 H 1 1.32 0.01 . 1 . . . . . . . . 4771 1 743 . 1 1 72 72 ALA N N 15 119.11 0.10 . 1 . . . . . . . . 4771 1 744 . 1 1 73 73 ALA C C 13 179.57 0.10 . 5 . . . . . . . . 4771 1 745 . 1 1 73 73 ALA CA C 13 54.39 0.10 . 1 . . . . . . . . 4771 1 746 . 1 1 73 73 ALA CB C 13 18.88 0.10 . 1 . . . . . . . . 4771 1 747 . 1 1 73 73 ALA H H 1 7.26 0.01 . 1 . . . . . . . . 4771 1 748 . 1 1 73 73 ALA HA H 1 3.83 0.01 . 1 . . . . . . . . 4771 1 749 . 1 1 73 73 ALA HB1 H 1 1.14 0.01 . 1 . . . . . . . . 4771 1 750 . 1 1 73 73 ALA HB2 H 1 1.14 0.01 . 1 . . . . . . . . 4771 1 751 . 1 1 73 73 ALA HB3 H 1 1.14 0.01 . 1 . . . . . . . . 4771 1 752 . 1 1 73 73 ALA N N 15 119.92 0.10 . 1 . . . . . . . . 4771 1 753 . 1 1 74 74 ALA C C 13 178.73 0.10 . 1 . . . . . . . . 4771 1 754 . 1 1 74 74 ALA CA C 13 55.00 0.10 . 1 . . . . . . . . 4771 1 755 . 1 1 74 74 ALA CB C 13 18.23 0.10 . 1 . . . . . . . . 4771 1 756 . 1 1 74 74 ALA H H 1 8.33 0.01 . 1 . . . . . . . . 4771 1 757 . 1 1 74 74 ALA HA H 1 3.63 0.01 . 1 . . . . . . . . 4771 1 758 . 1 1 74 74 ALA HB1 H 1 1.17 0.01 . 1 . . . . . . . . 4771 1 759 . 1 1 74 74 ALA HB2 H 1 1.17 0.01 . 1 . . . . . . . . 4771 1 760 . 1 1 74 74 ALA HB3 H 1 1.17 0.01 . 1 . . . . . . . . 4771 1 761 . 1 1 74 74 ALA N N 15 118.28 0.10 . 1 . . . . . . . . 4771 1 762 . 1 1 75 75 LYS C C 13 177.13 0.10 . 1 . . . . . . . . 4771 1 763 . 1 1 75 75 LYS CA C 13 58.41 0.10 . 1 . . . . . . . . 4771 1 764 . 1 1 75 75 LYS CB C 13 32.48 0.10 . 1 . . . . . . . . 4771 1 765 . 1 1 75 75 LYS CD C 13 29.18 0.10 . 1 . . . . . . . . 4771 1 766 . 1 1 75 75 LYS CE C 13 41.90 0.10 . 1 . . . . . . . . 4771 1 767 . 1 1 75 75 LYS CG C 13 25.59 0.12 . 1 . . . . . . . . 4771 1 768 . 1 1 75 75 LYS H H 1 7.16 0.01 . 1 . . . . . . . . 4771 1 769 . 1 1 75 75 LYS HA H 1 3.91 0.01 . 1 . . . . . . . . 4771 1 770 . 1 1 75 75 LYS HB2 H 1 1.86 0.01 . 2 . . . . . . . . 4771 1 771 . 1 1 75 75 LYS HB3 H 1 1.70 0.01 . 2 . . . . . . . . 4771 1 772 . 1 1 75 75 LYS HD2 H 1 1.57 0.01 . 2 . . . . . . . . 4771 1 773 . 1 1 75 75 LYS HE2 H 1 2.83 0.01 . 2 . . . . . . . . 4771 1 774 . 1 1 75 75 LYS HG2 H 1 1.60 0.01 . 2 . . . . . . . . 4771 1 775 . 1 1 75 75 LYS HG3 H 1 1.36 0.01 . 2 . . . . . . . . 4771 1 776 . 1 1 75 75 LYS N N 15 113.56 0.10 . 1 . . . . . . . . 4771 1 777 . 1 1 76 76 LEU C C 13 176.90 0.10 . 1 . . . . . . . . 4771 1 778 . 1 1 76 76 LEU CA C 13 54.21 0.10 . 1 . . . . . . . . 4771 1 779 . 1 1 76 76 LEU CB C 13 43.64 0.10 . 1 . . . . . . . . 4771 1 780 . 1 1 76 76 LEU CD1 C 13 25.49 0.10 . 2 . . . . . . . . 4771 1 781 . 1 1 76 76 LEU CD2 C 13 22.10 0.10 . 2 . . . . . . . . 4771 1 782 . 1 1 76 76 LEU CG C 13 26.24 0.10 . 1 . . . . . . . . 4771 1 783 . 1 1 76 76 LEU H H 1 7.10 0.01 . 1 . . . . . . . . 4771 1 784 . 1 1 76 76 LEU HA H 1 4.33 0.01 . 1 . . . . . . . . 4771 1 785 . 1 1 76 76 LEU HB2 H 1 1.76 0.01 . 2 . . . . . . . . 4771 1 786 . 1 1 76 76 LEU HB3 H 1 1.47 0.02 . 2 . . . . . . . . 4771 1 787 . 1 1 76 76 LEU HD11 H 1 0.90 0.01 . 2 . . . . . . . . 4771 1 788 . 1 1 76 76 LEU HD12 H 1 0.90 0.01 . 2 . . . . . . . . 4771 1 789 . 1 1 76 76 LEU HD13 H 1 0.90 0.01 . 2 . . . . . . . . 4771 1 790 . 1 1 76 76 LEU HD21 H 1 0.80 0.01 . 2 . . . . . . . . 4771 1 791 . 1 1 76 76 LEU HD22 H 1 0.80 0.01 . 2 . . . . . . . . 4771 1 792 . 1 1 76 76 LEU HD23 H 1 0.80 0.01 . 2 . . . . . . . . 4771 1 793 . 1 1 76 76 LEU HG H 1 1.69 0.01 . 2 . . . . . . . . 4771 1 794 . 1 1 76 76 LEU N N 15 116.80 0.10 . 1 . . . . . . . . 4771 1 795 . 1 1 77 77 ALA C C 13 176.26 0.10 . 1 . . . . . . . . 4771 1 796 . 1 1 77 77 ALA CA C 13 52.24 0.10 . 1 . . . . . . . . 4771 1 797 . 1 1 77 77 ALA CB C 13 20.02 0.10 . 1 . . . . . . . . 4771 1 798 . 1 1 77 77 ALA H H 1 7.07 0.01 . 1 . . . . . . . . 4771 1 799 . 1 1 77 77 ALA HA H 1 3.93 0.01 . 1 . . . . . . . . 4771 1 800 . 1 1 77 77 ALA HB1 H 1 1.08 0.01 . 1 . . . . . . . . 4771 1 801 . 1 1 77 77 ALA HB2 H 1 1.08 0.01 . 1 . . . . . . . . 4771 1 802 . 1 1 77 77 ALA HB3 H 1 1.08 0.01 . 1 . . . . . . . . 4771 1 803 . 1 1 77 77 ALA N N 15 121.65 0.10 . 1 . . . . . . . . 4771 1 804 . 1 1 78 78 LYS C C 13 174.75 0.10 . 1 . . . . . . . . 4771 1 805 . 1 1 78 78 LYS CA C 13 54.26 0.10 . 1 . . . . . . . . 4771 1 806 . 1 1 78 78 LYS CB C 13 31.49 0.10 . 1 . . . . . . . . 4771 1 807 . 1 1 78 78 LYS CD C 13 28.67 0.10 . 1 . . . . . . . . 4771 1 808 . 1 1 78 78 LYS CE C 13 42.09 0.10 . 1 . . . . . . . . 4771 1 809 . 1 1 78 78 LYS CG C 13 24.31 0.10 . 1 . . . . . . . . 4771 1 810 . 1 1 78 78 LYS H H 1 8.43 0.01 . 1 . . . . . . . . 4771 1 811 . 1 1 78 78 LYS HA H 1 4.43 0.01 . 1 . . . . . . . . 4771 1 812 . 1 1 78 78 LYS HB2 H 1 1.67 0.01 . 2 . . . . . . . . 4771 1 813 . 1 1 78 78 LYS HB3 H 1 1.57 0.01 . 2 . . . . . . . . 4771 1 814 . 1 1 78 78 LYS HD2 H 1 1.56 0.01 . 2 . . . . . . . . 4771 1 815 . 1 1 78 78 LYS HE2 H 1 2.89 0.01 . 2 . . . . . . . . 4771 1 816 . 1 1 78 78 LYS HG2 H 1 1.27 0.01 . 2 . . . . . . . . 4771 1 817 . 1 1 78 78 LYS HG3 H 1 1.19 0.01 . 2 . . . . . . . . 4771 1 818 . 1 1 78 78 LYS N N 15 123.24 0.10 . 1 . . . . . . . . 4771 1 819 . 1 1 79 79 ILE CA C 13 58.32 0.10 . 1 . . . . . . . . 4771 1 820 . 1 1 79 79 ILE CB C 13 37.15 0.10 . 1 . . . . . . . . 4771 1 821 . 1 1 79 79 ILE CD1 C 13 11.71 0.10 . 1 . . . . . . . . 4771 1 822 . 1 1 79 79 ILE CG1 C 13 28.44 0.10 . 1 . . . . . . . . 4771 1 823 . 1 1 79 79 ILE CG2 C 13 17.47 0.10 . 1 . . . . . . . . 4771 1 824 . 1 1 79 79 ILE H H 1 8.46 0.01 . 1 . . . . . . . . 4771 1 825 . 1 1 79 79 ILE HA H 1 3.92 0.01 . 1 . . . . . . . . 4771 1 826 . 1 1 79 79 ILE HB H 1 2.20 0.01 . 2 . . . . . . . . 4771 1 827 . 1 1 79 79 ILE HD11 H 1 0.68 0.01 . 1 . . . . . . . . 4771 1 828 . 1 1 79 79 ILE HD12 H 1 0.68 0.01 . 1 . . . . . . . . 4771 1 829 . 1 1 79 79 ILE HD13 H 1 0.68 0.01 . 1 . . . . . . . . 4771 1 830 . 1 1 79 79 ILE HG12 H 1 1.42 0.01 . 2 . . . . . . . . 4771 1 831 . 1 1 79 79 ILE HG13 H 1 1.01 0.01 . 2 . . . . . . . . 4771 1 832 . 1 1 79 79 ILE HG21 H 1 0.88 0.01 . 1 . . . . . . . . 4771 1 833 . 1 1 79 79 ILE HG22 H 1 0.88 0.01 . 1 . . . . . . . . 4771 1 834 . 1 1 79 79 ILE HG23 H 1 0.88 0.01 . 1 . . . . . . . . 4771 1 835 . 1 1 79 79 ILE N N 15 129.56 0.10 . 1 . . . . . . . . 4771 1 836 . 1 1 80 80 PRO C C 13 175.09 0.10 . 1 . . . . . . . . 4771 1 837 . 1 1 80 80 PRO CA C 13 61.99 0.10 . 1 . . . . . . . . 4771 1 838 . 1 1 80 80 PRO CB C 13 31.87 0.11 . 1 . . . . . . . . 4771 1 839 . 1 1 80 80 PRO CD C 13 50.54 0.10 . 1 . . . . . . . . 4771 1 840 . 1 1 80 80 PRO CG C 13 27.52 0.10 . 1 . . . . . . . . 4771 1 841 . 1 1 80 80 PRO HA H 1 4.35 0.01 . 1 . . . . . . . . 4771 1 842 . 1 1 80 80 PRO HB2 H 1 2.28 0.01 . 2 . . . . . . . . 4771 1 843 . 1 1 80 80 PRO HB3 H 1 1.86 0.01 . 2 . . . . . . . . 4771 1 844 . 1 1 80 80 PRO HD2 H 1 3.69 0.01 . 2 . . . . . . . . 4771 1 845 . 1 1 80 80 PRO HD3 H 1 3.19 0.01 . 2 . . . . . . . . 4771 1 846 . 1 1 80 80 PRO HG2 H 1 1.84 0.01 . 2 . . . . . . . . 4771 1 847 . 1 1 81 81 LYS CA C 13 54.70 0.10 . 1 . . . . . . . . 4771 1 848 . 1 1 81 81 LYS CB C 13 32.06 0.10 . 1 . . . . . . . . 4771 1 849 . 1 1 81 81 LYS CD C 13 23.82 0.10 . 1 . . . . . . . . 4771 1 850 . 1 1 81 81 LYS CE C 13 41.96 0.10 . 1 . . . . . . . . 4771 1 851 . 1 1 81 81 LYS CG C 13 24.28 0.10 . 1 . . . . . . . . 4771 1 852 . 1 1 81 81 LYS H H 1 8.34 0.01 . 1 . . . . . . . . 4771 1 853 . 1 1 81 81 LYS HA H 1 3.90 0.01 . 1 . . . . . . . . 4771 1 854 . 1 1 81 81 LYS HB2 H 1 1.67 0.01 . 2 . . . . . . . . 4771 1 855 . 1 1 81 81 LYS HB3 H 1 1.54 0.02 . 2 . . . . . . . . 4771 1 856 . 1 1 81 81 LYS HD2 H 1 1.40 0.01 . 2 . . . . . . . . 4771 1 857 . 1 1 81 81 LYS HD3 H 1 1.28 0.01 . 2 . . . . . . . . 4771 1 858 . 1 1 81 81 LYS HE2 H 1 2.86 0.02 . 2 . . . . . . . . 4771 1 859 . 1 1 81 81 LYS HG2 H 1 1.21 0.01 . 2 . . . . . . . . 4771 1 860 . 1 1 81 81 LYS N N 15 122.90 0.10 . 1 . . . . . . . . 4771 1 861 . 1 1 82 82 PRO CA C 13 60.60 0.10 . 1 . . . . . . . . 4771 1 862 . 1 1 82 82 PRO CB C 13 30.53 0.10 . 1 . . . . . . . . 4771 1 863 . 1 1 82 82 PRO CD C 13 49.87 0.10 . 1 . . . . . . . . 4771 1 864 . 1 1 82 82 PRO CG C 13 27.21 0.10 . 1 . . . . . . . . 4771 1 865 . 1 1 82 82 PRO HA H 1 3.65 0.01 . 1 . . . . . . . . 4771 1 866 . 1 1 82 82 PRO HB2 H 1 1.62 0.01 . 2 . . . . . . . . 4771 1 867 . 1 1 82 82 PRO HB3 H 1 1.51 0.01 . 2 . . . . . . . . 4771 1 868 . 1 1 82 82 PRO HD2 H 1 3.49 0.01 . 2 . . . . . . . . 4771 1 869 . 1 1 82 82 PRO HG2 H 1 2.01 0.01 . 2 . . . . . . . . 4771 1 870 . 1 1 82 82 PRO HG3 H 1 1.98 0.01 . 2 . . . . . . . . 4771 1 871 . 1 1 83 83 PRO C C 13 175.17 0.10 . 1 . . . . . . . . 4771 1 872 . 1 1 83 83 PRO CA C 13 63.87 0.10 . 1 . . . . . . . . 4771 1 873 . 1 1 83 83 PRO CB C 13 31.89 0.10 . 1 . . . . . . . . 4771 1 874 . 1 1 83 83 PRO CD C 13 50.75 0.10 . 1 . . . . . . . . 4771 1 875 . 1 1 83 83 PRO CG C 13 26.88 0.10 . 1 . . . . . . . . 4771 1 876 . 1 1 83 83 PRO HA H 1 4.21 0.01 . 1 . . . . . . . . 4771 1 877 . 1 1 83 83 PRO HB2 H 1 2.21 0.01 . 2 . . . . . . . . 4771 1 878 . 1 1 83 83 PRO HB3 H 1 1.93 0.02 . 2 . . . . . . . . 4771 1 879 . 1 1 83 83 PRO HD2 H 1 3.29 0.01 . 2 . . . . . . . . 4771 1 880 . 1 1 83 83 PRO HD3 H 1 2.61 0.01 . 2 . . . . . . . . 4771 1 881 . 1 1 83 83 PRO HG2 H 1 2.10 0.01 . 2 . . . . . . . . 4771 1 882 . 1 1 83 83 PRO HG3 H 1 1.71 0.01 . 2 . . . . . . . . 4771 1 883 . 1 1 84 84 SER CA C 13 56.16 0.10 . 1 . . . . . . . . 4771 1 884 . 1 1 84 84 SER CB C 13 65.97 0.10 . 1 . . . . . . . . 4771 1 885 . 1 1 84 84 SER H H 1 6.73 0.01 . 1 . . . . . . . . 4771 1 886 . 1 1 84 84 SER HA H 1 4.54 0.01 . 1 . . . . . . . . 4771 1 887 . 1 1 84 84 SER HB2 H 1 4.09 0.01 . 2 . . . . . . . . 4771 1 888 . 1 1 84 84 SER HB3 H 1 3.88 0.01 . 2 . . . . . . . . 4771 1 889 . 1 1 84 84 SER N N 15 108.00 0.10 . 1 . . . . . . . . 4771 1 890 . 1 1 85 85 GLN C C 13 177.51 0.10 . 1 . . . . . . . . 4771 1 891 . 1 1 85 85 GLN CA C 13 58.56 0.10 . 1 . . . . . . . . 4771 1 892 . 1 1 85 85 GLN CB C 13 27.67 0.10 . 1 . . . . . . . . 4771 1 893 . 1 1 85 85 GLN CG C 13 33.13 0.10 . 1 . . . . . . . . 4771 1 894 . 1 1 85 85 GLN HA H 1 4.10 0.01 . 1 . . . . . . . . 4771 1 895 . 1 1 85 85 GLN HB2 H 1 2.14 0.01 . 2 . . . . . . . . 4771 1 896 . 1 1 85 85 GLN HB3 H 1 2.02 0.01 . 2 . . . . . . . . 4771 1 897 . 1 1 85 85 GLN HG2 H 1 2.44 0.01 . 2 . . . . . . . . 4771 1 898 . 1 1 86 86 ALA C C 13 180.36 0.10 . 1 . . . . . . . . 4771 1 899 . 1 1 86 86 ALA CA C 13 54.96 0.10 . 1 . . . . . . . . 4771 1 900 . 1 1 86 86 ALA CB C 13 17.97 0.10 . 1 . . . . . . . . 4771 1 901 . 1 1 86 86 ALA H H 1 8.27 0.01 . 1 . . . . . . . . 4771 1 902 . 1 1 86 86 ALA HA H 1 4.04 0.01 . 1 . . . . . . . . 4771 1 903 . 1 1 86 86 ALA HB1 H 1 1.32 0.01 . 1 . . . . . . . . 4771 1 904 . 1 1 86 86 ALA HB2 H 1 1.32 0.01 . 1 . . . . . . . . 4771 1 905 . 1 1 86 86 ALA HB3 H 1 1.32 0.01 . 1 . . . . . . . . 4771 1 906 . 1 1 86 86 ALA N N 15 120.28 0.10 . 1 . . . . . . . . 4771 1 907 . 1 1 87 87 VAL C C 13 179.40 0.10 . 5 . . . . . . . . 4771 1 908 . 1 1 87 87 VAL CA C 13 66.26 0.10 . 1 . . . . . . . . 4771 1 909 . 1 1 87 87 VAL CB C 13 31.68 0.10 . 1 . . . . . . . . 4771 1 910 . 1 1 87 87 VAL CG1 C 13 24.03 0.10 . 2 . . . . . . . . 4771 1 911 . 1 1 87 87 VAL CG2 C 13 23.56 0.10 . 2 . . . . . . . . 4771 1 912 . 1 1 87 87 VAL H H 1 7.38 0.01 . 1 . . . . . . . . 4771 1 913 . 1 1 87 87 VAL HA H 1 3.61 0.01 . 1 . . . . . . . . 4771 1 914 . 1 1 87 87 VAL HB H 1 1.69 0.01 . 2 . . . . . . . . 4771 1 915 . 1 1 87 87 VAL HG11 H 1 0.86 0.01 . 2 . . . . . . . . 4771 1 916 . 1 1 87 87 VAL HG12 H 1 0.86 0.01 . 2 . . . . . . . . 4771 1 917 . 1 1 87 87 VAL HG13 H 1 0.86 0.01 . 2 . . . . . . . . 4771 1 918 . 1 1 87 87 VAL HG21 H 1 0.76 0.01 . 2 . . . . . . . . 4771 1 919 . 1 1 87 87 VAL HG22 H 1 0.76 0.01 . 2 . . . . . . . . 4771 1 920 . 1 1 87 87 VAL HG23 H 1 0.76 0.01 . 2 . . . . . . . . 4771 1 921 . 1 1 87 87 VAL N N 15 116.41 0.10 . 1 . . . . . . . . 4771 1 922 . 1 1 88 88 TYR C C 13 175.55 0.10 . 1 . . . . . . . . 4771 1 923 . 1 1 88 88 TYR CA C 13 61.43 0.10 . 1 . . . . . . . . 4771 1 924 . 1 1 88 88 TYR CB C 13 37.10 0.10 . 1 . . . . . . . . 4771 1 925 . 1 1 88 88 TYR H H 1 8.02 0.01 . 1 . . . . . . . . 4771 1 926 . 1 1 88 88 TYR HA H 1 3.93 0.01 . 1 . . . . . . . . 4771 1 927 . 1 1 88 88 TYR HB2 H 1 3.14 0.01 . 2 . . . . . . . . 4771 1 928 . 1 1 88 88 TYR HB3 H 1 3.06 0.01 . 2 . . . . . . . . 4771 1 929 . 1 1 88 88 TYR N N 15 121.38 0.10 . 1 . . . . . . . . 4771 1 930 . 1 1 89 89 GLU C C 13 178.67 0.10 . 1 . . . . . . . . 4771 1 931 . 1 1 89 89 GLU CA C 13 59.03 0.10 . 1 . . . . . . . . 4771 1 932 . 1 1 89 89 GLU CB C 13 29.02 0.10 . 1 . . . . . . . . 4771 1 933 . 1 1 89 89 GLU CG C 13 36.01 0.10 . 1 . . . . . . . . 4771 1 934 . 1 1 89 89 GLU H H 1 8.08 0.01 . 1 . . . . . . . . 4771 1 935 . 1 1 89 89 GLU HA H 1 3.31 0.01 . 1 . . . . . . . . 4771 1 936 . 1 1 89 89 GLU HB2 H 1 1.94 0.01 . 2 . . . . . . . . 4771 1 937 . 1 1 89 89 GLU HG2 H 1 2.37 0.01 . 2 . . . . . . . . 4771 1 938 . 1 1 89 89 GLU N N 15 114.60 0.10 . 1 . . . . . . . . 4771 1 939 . 1 1 90 90 VAL C C 13 176.89 0.10 . 1 . . . . . . . . 4771 1 940 . 1 1 90 90 VAL CA C 13 65.27 0.10 . 1 . . . . . . . . 4771 1 941 . 1 1 90 90 VAL CB C 13 31.85 0.12 . 1 . . . . . . . . 4771 1 942 . 1 1 90 90 VAL CG1 C 13 21.89 0.10 . 2 . . . . . . . . 4771 1 943 . 1 1 90 90 VAL CG2 C 13 20.61 0.10 . 2 . . . . . . . . 4771 1 944 . 1 1 90 90 VAL H H 1 6.92 0.01 . 1 . . . . . . . . 4771 1 945 . 1 1 90 90 VAL HA H 1 3.56 0.01 . 1 . . . . . . . . 4771 1 946 . 1 1 90 90 VAL HB H 1 2.09 0.01 . 2 . . . . . . . . 4771 1 947 . 1 1 90 90 VAL HG11 H 1 0.94 0.01 . 2 . . . . . . . . 4771 1 948 . 1 1 90 90 VAL HG12 H 1 0.94 0.01 . 2 . . . . . . . . 4771 1 949 . 1 1 90 90 VAL HG13 H 1 0.94 0.01 . 2 . . . . . . . . 4771 1 950 . 1 1 90 90 VAL HG21 H 1 0.29 0.01 . 2 . . . . . . . . 4771 1 951 . 1 1 90 90 VAL HG22 H 1 0.29 0.01 . 2 . . . . . . . . 4771 1 952 . 1 1 90 90 VAL HG23 H 1 0.29 0.01 . 2 . . . . . . . . 4771 1 953 . 1 1 90 90 VAL N N 15 116.50 0.10 . 1 . . . . . . . . 4771 1 954 . 1 1 91 91 PHE C C 13 173.93 0.10 . 1 . . . . . . . . 4771 1 955 . 1 1 91 91 PHE CA C 13 60.57 0.11 . 1 . . . . . . . . 4771 1 956 . 1 1 91 91 PHE CB C 13 39.36 0.10 . 1 . . . . . . . . 4771 1 957 . 1 1 91 91 PHE H H 1 7.42 0.01 . 1 . . . . . . . . 4771 1 958 . 1 1 91 91 PHE HA H 1 4.11 0.01 . 1 . . . . . . . . 4771 1 959 . 1 1 91 91 PHE HB2 H 1 3.51 0.01 . 2 . . . . . . . . 4771 1 960 . 1 1 91 91 PHE HB3 H 1 2.54 0.01 . 2 . . . . . . . . 4771 1 961 . 1 1 91 91 PHE N N 15 115.88 0.10 . 1 . . . . . . . . 4771 1 962 . 1 1 92 92 LYS C C 13 177.13 0.10 . 1 . . . . . . . . 4771 1 963 . 1 1 92 92 LYS CA C 13 58.86 0.10 . 1 . . . . . . . . 4771 1 964 . 1 1 92 92 LYS CB C 13 31.39 0.10 . 1 . . . . . . . . 4771 1 965 . 1 1 92 92 LYS CD C 13 29.57 0.10 . 1 . . . . . . . . 4771 1 966 . 1 1 92 92 LYS CE C 13 41.97 0.10 . 1 . . . . . . . . 4771 1 967 . 1 1 92 92 LYS CG C 13 23.87 0.10 . 1 . . . . . . . . 4771 1 968 . 1 1 92 92 LYS H H 1 7.40 0.01 . 1 . . . . . . . . 4771 1 969 . 1 1 92 92 LYS HA H 1 4.08 0.01 . 1 . . . . . . . . 4771 1 970 . 1 1 92 92 LYS HB2 H 1 1.18 0.01 . 2 . . . . . . . . 4771 1 971 . 1 1 92 92 LYS HB3 H 1 1.52 0.01 . 2 . . . . . . . . 4771 1 972 . 1 1 92 92 LYS HD2 H 1 1.44 0.01 . 2 . . . . . . . . 4771 1 973 . 1 1 92 92 LYS HD3 H 1 1.33 0.01 . 2 . . . . . . . . 4771 1 974 . 1 1 92 92 LYS HE2 H 1 2.81 0.01 . 2 . . . . . . . . 4771 1 975 . 1 1 92 92 LYS HE3 H 1 2.88 0.01 . 2 . . . . . . . . 4771 1 976 . 1 1 92 92 LYS HG2 H 1 1.17 0.01 . 2 . . . . . . . . 4771 1 977 . 1 1 92 92 LYS HG3 H 1 0.98 0.01 . 2 . . . . . . . . 4771 1 978 . 1 1 92 92 LYS N N 15 117.66 0.10 . 1 . . . . . . . . 4771 1 979 . 1 1 93 93 ASN C C 13 173.98 0.10 . 1 . . . . . . . . 4771 1 980 . 1 1 93 93 ASN CA C 13 53.24 0.10 . 1 . . . . . . . . 4771 1 981 . 1 1 93 93 ASN CB C 13 37.99 0.10 . 1 . . . . . . . . 4771 1 982 . 1 1 93 93 ASN H H 1 7.20 0.01 . 1 . . . . . . . . 4771 1 983 . 1 1 93 93 ASN HA H 1 5.06 0.01 . 1 . . . . . . . . 4771 1 984 . 1 1 93 93 ASN HB2 H 1 2.76 0.01 . 2 . . . . . . . . 4771 1 985 . 1 1 93 93 ASN HB3 H 1 2.68 0.01 . 2 . . . . . . . . 4771 1 986 . 1 1 93 93 ASN N N 15 115.13 0.10 . 1 . . . . . . . . 4771 1 987 . 1 1 94 94 ALA CA C 13 50.06 0.10 . 1 . . . . . . . . 4771 1 988 . 1 1 94 94 ALA CB C 13 21.38 0.10 . 1 . . . . . . . . 4771 1 989 . 1 1 94 94 ALA H H 1 8.47 0.01 . 1 . . . . . . . . 4771 1 990 . 1 1 94 94 ALA HA H 1 4.78 0.01 . 1 . . . . . . . . 4771 1 991 . 1 1 94 94 ALA HB1 H 1 1.11 0.01 . 1 . . . . . . . . 4771 1 992 . 1 1 94 94 ALA HB2 H 1 1.11 0.01 . 1 . . . . . . . . 4771 1 993 . 1 1 94 94 ALA HB3 H 1 1.11 0.01 . 1 . . . . . . . . 4771 1 994 . 1 1 94 94 ALA N N 15 126.21 0.10 . 1 . . . . . . . . 4771 1 995 . 1 1 95 95 PRO C C 13 175.96 0.10 . 1 . . . . . . . . 4771 1 996 . 1 1 95 95 PRO CA C 13 61.06 0.10 . 1 . . . . . . . . 4771 1 997 . 1 1 95 95 PRO CB C 13 31.40 0.10 . 1 . . . . . . . . 4771 1 998 . 1 1 95 95 PRO CD C 13 49.69 0.10 . 1 . . . . . . . . 4771 1 999 . 1 1 95 95 PRO CG C 13 26.18 0.11 . 1 . . . . . . . . 4771 1 1000 . 1 1 95 95 PRO HA H 1 5.27 0.01 . 1 . . . . . . . . 4771 1 1001 . 1 1 95 95 PRO HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4771 1 1002 . 1 1 95 95 PRO HD2 H 1 3.58 0.02 . 2 . . . . . . . . 4771 1 1003 . 1 1 95 95 PRO HG2 H 1 2.05 0.01 . 2 . . . . . . . . 4771 1 1004 . 1 1 95 95 PRO HG3 H 1 1.94 0.01 . 2 . . . . . . . . 4771 1 1005 . 1 1 96 96 LEU C C 13 174.78 0.10 . 1 . . . . . . . . 4771 1 1006 . 1 1 96 96 LEU CA C 13 53.95 0.10 . 1 . . . . . . . . 4771 1 1007 . 1 1 96 96 LEU CB C 13 46.03 0.10 . 1 . . . . . . . . 4771 1 1008 . 1 1 96 96 LEU CD1 C 13 25.22 0.10 . 2 . . . . . . . . 4771 1 1009 . 1 1 96 96 LEU CD2 C 13 25.84 0.10 . 2 . . . . . . . . 4771 1 1010 . 1 1 96 96 LEU CG C 13 26.89 0.10 . 1 . . . . . . . . 4771 1 1011 . 1 1 96 96 LEU H H 1 9.07 0.01 . 1 . . . . . . . . 4771 1 1012 . 1 1 96 96 LEU HA H 1 4.48 0.01 . 1 . . . . . . . . 4771 1 1013 . 1 1 96 96 LEU HB2 H 1 1.61 0.01 . 2 . . . . . . . . 4771 1 1014 . 1 1 96 96 LEU HB3 H 1 1.40 0.01 . 2 . . . . . . . . 4771 1 1015 . 1 1 96 96 LEU HD11 H 1 0.91 0.01 . 2 . . . . . . . . 4771 1 1016 . 1 1 96 96 LEU HD12 H 1 0.91 0.01 . 2 . . . . . . . . 4771 1 1017 . 1 1 96 96 LEU HD13 H 1 0.91 0.01 . 2 . . . . . . . . 4771 1 1018 . 1 1 96 96 LEU HD21 H 1 0.78 0.01 . 2 . . . . . . . . 4771 1 1019 . 1 1 96 96 LEU HD22 H 1 0.78 0.01 . 2 . . . . . . . . 4771 1 1020 . 1 1 96 96 LEU HD23 H 1 0.78 0.01 . 2 . . . . . . . . 4771 1 1021 . 1 1 96 96 LEU HG H 1 1.49 0.01 . 2 . . . . . . . . 4771 1 1022 . 1 1 96 96 LEU N N 15 122.65 0.10 . 1 . . . . . . . . 4771 1 1023 . 1 1 97 97 ASP C C 13 174.40 0.10 . 1 . . . . . . . . 4771 1 1024 . 1 1 97 97 ASP CA C 13 53.94 0.10 . 1 . . . . . . . . 4771 1 1025 . 1 1 97 97 ASP CB C 13 40.69 0.10 . 1 . . . . . . . . 4771 1 1026 . 1 1 97 97 ASP H H 1 8.68 0.01 . 1 . . . . . . . . 4771 1 1027 . 1 1 97 97 ASP HA H 1 4.92 0.01 . 1 . . . . . . . . 4771 1 1028 . 1 1 97 97 ASP HB2 H 1 2.44 0.01 . 2 . . . . . . . . 4771 1 1029 . 1 1 97 97 ASP HB3 H 1 2.26 0.01 . 2 . . . . . . . . 4771 1 1030 . 1 1 97 97 ASP N N 15 125.91 0.10 . 1 . . . . . . . . 4771 1 1031 . 1 1 98 98 PHE C C 13 172.60 0.10 . 1 . . . . . . . . 4771 1 1032 . 1 1 98 98 PHE CA C 13 58.34 0.10 . 1 . . . . . . . . 4771 1 1033 . 1 1 98 98 PHE CB C 13 41.52 0.10 . 1 . . . . . . . . 4771 1 1034 . 1 1 98 98 PHE H H 1 9.08 0.01 . 1 . . . . . . . . 4771 1 1035 . 1 1 98 98 PHE HA H 1 4.36 0.01 . 1 . . . . . . . . 4771 1 1036 . 1 1 98 98 PHE HB2 H 1 3.04 0.01 . 2 . . . . . . . . 4771 1 1037 . 1 1 98 98 PHE HB3 H 1 2.52 0.01 . 2 . . . . . . . . 4771 1 1038 . 1 1 98 98 PHE N N 15 125.81 0.10 . 1 . . . . . . . . 4771 1 1039 . 1 1 99 99 LYS CA C 13 52.58 0.10 . 1 . . . . . . . . 4771 1 1040 . 1 1 99 99 LYS CB C 13 34.09 0.10 . 1 . . . . . . . . 4771 1 1041 . 1 1 99 99 LYS CD C 13 29.39 0.10 . 1 . . . . . . . . 4771 1 1042 . 1 1 99 99 LYS CE C 13 41.86 0.10 . 1 . . . . . . . . 4771 1 1043 . 1 1 99 99 LYS CG C 13 23.80 0.10 . 1 . . . . . . . . 4771 1 1044 . 1 1 99 99 LYS H H 1 7.56 0.01 . 1 . . . . . . . . 4771 1 1045 . 1 1 99 99 LYS HA H 1 4.77 0.01 . 1 . . . . . . . . 4771 1 1046 . 1 1 99 99 LYS HB2 H 1 1.49 0.01 . 2 . . . . . . . . 4771 1 1047 . 1 1 99 99 LYS HB3 H 1 1.39 0.01 . 2 . . . . . . . . 4771 1 1048 . 1 1 99 99 LYS HD2 H 1 1.38 0.01 . 2 . . . . . . . . 4771 1 1049 . 1 1 99 99 LYS HE2 H 1 2.70 0.01 . 2 . . . . . . . . 4771 1 1050 . 1 1 99 99 LYS HG2 H 1 1.10 0.01 . 2 . . . . . . . . 4771 1 1051 . 1 1 99 99 LYS N N 15 127.51 0.10 . 1 . . . . . . . . 4771 1 1052 . 1 1 100 100 PRO C C 13 175.96 0.10 . 1 . . . . . . . . 4771 1 1053 . 1 1 100 100 PRO CA C 13 62.48 0.10 . 1 . . . . . . . . 4771 1 1054 . 1 1 100 100 PRO CB C 13 31.92 0.10 . 1 . . . . . . . . 4771 1 1055 . 1 1 100 100 PRO CD C 13 50.07 0.10 . 1 . . . . . . . . 4771 1 1056 . 1 1 100 100 PRO CG C 13 27.24 0.10 . 1 . . . . . . . . 4771 1 1057 . 1 1 100 100 PRO HA H 1 3.90 0.01 . 1 . . . . . . . . 4771 1 1058 . 1 1 100 100 PRO HB2 H 1 1.59 0.01 . 2 . . . . . . . . 4771 1 1059 . 1 1 100 100 PRO HB3 H 1 1.52 0.01 . 2 . . . . . . . . 4771 1 1060 . 1 1 100 100 PRO HD2 H 1 3.70 0.01 . 2 . . . . . . . . 4771 1 1061 . 1 1 100 100 PRO HD3 H 1 2.90 0.01 . 2 . . . . . . . . 4771 1 1062 . 1 1 100 100 PRO HG2 H 1 1.74 0.01 . 2 . . . . . . . . 4771 1 1063 . 1 1 100 100 PRO HG3 H 1 1.39 0.01 . 2 . . . . . . . . 4771 1 1064 . 1 1 101 101 HIS C C 13 173.86 0.10 . 1 . . . . . . . . 4771 1 1065 . 1 1 101 101 HIS CA C 13 56.02 0.10 . 1 . . . . . . . . 4771 1 1066 . 1 1 101 101 HIS CB C 13 30.25 0.11 . 1 . . . . . . . . 4771 1 1067 . 1 1 101 101 HIS H H 1 8.95 0.01 . 1 . . . . . . . . 4771 1 1068 . 1 1 101 101 HIS HA H 1 4.36 0.01 . 1 . . . . . . . . 4771 1 1069 . 1 1 101 101 HIS HB2 H 1 3.01 0.01 . 2 . . . . . . . . 4771 1 1070 . 1 1 101 101 HIS HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4771 1 1071 . 1 1 101 101 HIS N N 15 120.61 0.10 . 1 . . . . . . . . 4771 1 1072 . 1 1 102 102 HIS CA C 13 57.22 0.10 . 1 . . . . . . . . 4771 1 1073 . 1 1 102 102 HIS CB C 13 30.21 0.10 . 1 . . . . . . . . 4771 1 1074 . 1 1 102 102 HIS H H 1 7.96 0.01 . 1 . . . . . . . . 4771 1 1075 . 1 1 102 102 HIS HA H 1 4.31 0.01 . 1 . . . . . . . . 4771 1 1076 . 1 1 102 102 HIS HB2 H 1 3.09 0.01 . 2 . . . . . . . . 4771 1 1077 . 1 1 102 102 HIS HB3 H 1 2.95 0.01 . 2 . . . . . . . . 4771 1 1078 . 1 1 102 102 HIS N N 15 125.48 0.10 . 1 . . . . . . . . 4771 1 stop_ save_