data_26027 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 26027 _Entry.Title ; Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2016-04-10 _Entry.Accession_date 2016-04-14 _Entry.Last_release_date 2016-10-14 _Entry.Original_release_date 2016-10-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1.1.99 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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.ORCID _Entry_author.Entry_ID 1 Matthias Wittwer . . . . 26027 2 Sonja Dames . A. . . 26027 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Technical University of Munich, Department of Chemistry, Biomolecular NMR' . 26027 2 . 'Institute of Structural Biology, Helmholtz Zentrum Munich' . 26027 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 26027 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 170 26027 '15N chemical shifts' 53 26027 '1H chemical shifts' 83 26027 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 . . 2016-10-14 . original BMRB . 26027 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 26028 ; Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain ; 26027 BMRB 26029 ; Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; 26027 BMRB 26030 ; Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; 26027 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 26027 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 27632081 _Citation.Full_citation . _Citation.Title ; Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biomol. NMR Assign.' _Citation.Journal_name_full . _Citation.Journal_volume 10 _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 401 _Citation.Page_last 406 _Citation.Year 2016 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Matthias Wittwer . . . . 26027 1 2 Sonja Dames . A. . . 26027 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Mycobacterium tuberculosis' 26027 1 'natively disordered protein' 26027 1 'protein kinase G' 26027 1 'redox-sensitive metal binding motif' 26027 1 rubredoxin 26027 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 26027 _Assembly.ID 1 _Assembly.Name 'Protein kinase G (PknG) 1-75 natively disordered region' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 2.7.11.1 _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 NORS 1 $His-PknG_1-75 A . yes native no no . 'Regulatory natively disordered N-terminal region of a ser/thr kinase' . 26027 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 2PZI . . X-ray 2.4 . 'Crystal structure of PknG 73-750 in complex with the inhibitor AX20017' 26027 1 yes PDB 4Y0X . . X-ray 1.74 . 'Crystal structure of PknG 64-405 in complex with ADP' 26027 1 yes PDB 4Y12 . . X-ray 1.9 . 'Crystal structure of PknG 64-405 in complex with AGS' 26027 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; The eukaryotic like serine /threonine protein kinase G promotes cellular survival of pathogenic mycobacteria by inhibiting phagosome-lysosome fusion within host macophages. ; 26027 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_His-PknG_1-75 _Entity.Sf_category entity _Entity.Sf_framecode His-PknG_1-75 _Entity.Entry_ID 26027 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name His-PknG_1-75 _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 ; MGSSHHHHHHSSGLVPRGSH MAKASETERSGPGTQPADAQ TATSATVRPLSTQAVFRPDF GDEDNFPHPTLGPDTEPQDR MATTSRVRPPVRRLG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq '21, M = the first aminoacid of the protein sequence' _Entity.Polymer_author_seq_details 'Residue 1-20 represents a non native poly histidine tag' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 95 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment 'His-PknG 1-75' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 10241.20 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'His-PknG 1-75 contains the natively disordered NORS (No Regulatory Secondary Structure) region of mycobacterial protein kinase G' _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Regulatory natively disordered N-terminal region of a ser/thr kinase' 26027 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 MET . 26027 1 2 2 GLY . 26027 1 3 3 SER . 26027 1 4 4 SER . 26027 1 5 5 HIS . 26027 1 6 6 HIS . 26027 1 7 7 HIS . 26027 1 8 8 HIS . 26027 1 9 9 HIS . 26027 1 10 10 HIS . 26027 1 11 11 SER . 26027 1 12 12 SER . 26027 1 13 13 GLY . 26027 1 14 14 LEU . 26027 1 15 15 VAL . 26027 1 16 16 PRO . 26027 1 17 17 ARG . 26027 1 18 18 GLY . 26027 1 19 19 SER . 26027 1 20 20 HIS . 26027 1 21 21 MET . 26027 1 22 22 ALA . 26027 1 23 23 LYS . 26027 1 24 24 ALA . 26027 1 25 25 SER . 26027 1 26 26 GLU . 26027 1 27 27 THR . 26027 1 28 28 GLU . 26027 1 29 29 ARG . 26027 1 30 30 SER . 26027 1 31 31 GLY . 26027 1 32 32 PRO . 26027 1 33 33 GLY . 26027 1 34 34 THR . 26027 1 35 35 GLN . 26027 1 36 36 PRO . 26027 1 37 37 ALA . 26027 1 38 38 ASP . 26027 1 39 39 ALA . 26027 1 40 40 GLN . 26027 1 41 41 THR . 26027 1 42 42 ALA . 26027 1 43 43 THR . 26027 1 44 44 SER . 26027 1 45 45 ALA . 26027 1 46 46 THR . 26027 1 47 47 VAL . 26027 1 48 48 ARG . 26027 1 49 49 PRO . 26027 1 50 50 LEU . 26027 1 51 51 SER . 26027 1 52 52 THR . 26027 1 53 53 GLN . 26027 1 54 54 ALA . 26027 1 55 55 VAL . 26027 1 56 56 PHE . 26027 1 57 57 ARG . 26027 1 58 58 PRO . 26027 1 59 59 ASP . 26027 1 60 60 PHE . 26027 1 61 61 GLY . 26027 1 62 62 ASP . 26027 1 63 63 GLU . 26027 1 64 64 ASP . 26027 1 65 65 ASN . 26027 1 66 66 PHE . 26027 1 67 67 PRO . 26027 1 68 68 HIS . 26027 1 69 69 PRO . 26027 1 70 70 THR . 26027 1 71 71 LEU . 26027 1 72 72 GLY . 26027 1 73 73 PRO . 26027 1 74 74 ASP . 26027 1 75 75 THR . 26027 1 76 76 GLU . 26027 1 77 77 PRO . 26027 1 78 78 GLN . 26027 1 79 79 ASP . 26027 1 80 80 ARG . 26027 1 81 81 MET . 26027 1 82 82 ALA . 26027 1 83 83 THR . 26027 1 84 84 THR . 26027 1 85 85 SER . 26027 1 86 86 ARG . 26027 1 87 87 VAL . 26027 1 88 88 ARG . 26027 1 89 89 PRO . 26027 1 90 90 PRO . 26027 1 91 91 VAL . 26027 1 92 92 ARG . 26027 1 93 93 ARG . 26027 1 94 94 LEU . 26027 1 95 95 GLY . 26027 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 . MET 1 1 26027 1 . GLY 2 2 26027 1 . SER 3 3 26027 1 . SER 4 4 26027 1 . HIS 5 5 26027 1 . HIS 6 6 26027 1 . HIS 7 7 26027 1 . HIS 8 8 26027 1 . HIS 9 9 26027 1 . HIS 10 10 26027 1 . SER 11 11 26027 1 . SER 12 12 26027 1 . GLY 13 13 26027 1 . LEU 14 14 26027 1 . VAL 15 15 26027 1 . PRO 16 16 26027 1 . ARG 17 17 26027 1 . GLY 18 18 26027 1 . SER 19 19 26027 1 . HIS 20 20 26027 1 . MET 21 21 26027 1 . ALA 22 22 26027 1 . LYS 23 23 26027 1 . ALA 24 24 26027 1 . SER 25 25 26027 1 . GLU 26 26 26027 1 . THR 27 27 26027 1 . GLU 28 28 26027 1 . ARG 29 29 26027 1 . SER 30 30 26027 1 . GLY 31 31 26027 1 . PRO 32 32 26027 1 . GLY 33 33 26027 1 . THR 34 34 26027 1 . GLN 35 35 26027 1 . PRO 36 36 26027 1 . ALA 37 37 26027 1 . ASP 38 38 26027 1 . ALA 39 39 26027 1 . GLN 40 40 26027 1 . THR 41 41 26027 1 . ALA 42 42 26027 1 . THR 43 43 26027 1 . SER 44 44 26027 1 . ALA 45 45 26027 1 . THR 46 46 26027 1 . VAL 47 47 26027 1 . ARG 48 48 26027 1 . PRO 49 49 26027 1 . LEU 50 50 26027 1 . SER 51 51 26027 1 . THR 52 52 26027 1 . GLN 53 53 26027 1 . ALA 54 54 26027 1 . VAL 55 55 26027 1 . PHE 56 56 26027 1 . ARG 57 57 26027 1 . PRO 58 58 26027 1 . ASP 59 59 26027 1 . PHE 60 60 26027 1 . GLY 61 61 26027 1 . ASP 62 62 26027 1 . GLU 63 63 26027 1 . ASP 64 64 26027 1 . ASN 65 65 26027 1 . PHE 66 66 26027 1 . PRO 67 67 26027 1 . HIS 68 68 26027 1 . PRO 69 69 26027 1 . THR 70 70 26027 1 . LEU 71 71 26027 1 . GLY 72 72 26027 1 . PRO 73 73 26027 1 . ASP 74 74 26027 1 . THR 75 75 26027 1 . GLU 76 76 26027 1 . PRO 77 77 26027 1 . GLN 78 78 26027 1 . ASP 79 79 26027 1 . ARG 80 80 26027 1 . MET 81 81 26027 1 . ALA 82 82 26027 1 . THR 83 83 26027 1 . THR 84 84 26027 1 . SER 85 85 26027 1 . ARG 86 86 26027 1 . VAL 87 87 26027 1 . ARG 88 88 26027 1 . PRO 89 89 26027 1 . PRO 90 90 26027 1 . VAL 91 91 26027 1 . ARG 92 92 26027 1 . ARG 93 93 26027 1 . LEU 94 94 26027 1 . GLY 95 95 26027 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 26027 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $His-PknG_1-75 . 83332 organism . 'Mycobacterium tuberculosis' 'Mycobacterium tuberculosis' . . Bacteria . Mycobacterium tuberculosis H37Rv . . . . . . . . . . 'pknG Rv0410c MTCY22G10.06c' . 26027 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 26027 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $His-PknG_1-75 . 'recombinant technology' 'Escherichia coli' . . 469008 Escherichia coli 'Bl21 (DE3)' . . . . . pET15b . . . 26027 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 26027 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _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 'PknG 1-75' '[U-13C; U-15N]' . . 1 $His-PknG_1-75 . protein . 0.4 0.8 mM . . . . 26027 1 2 TRIS-HCL 'natural abundance' . . . . . buffer 20 . . mM . . . . 26027 1 3 'sodium chloride' 'natural abundance' . . . . . salt 150 . . mM . . . . 26027 1 4 H2O 'natural abundance' . . . . . solvent 95 . . % . . . . 26027 1 5 D2O [U-2H] . . . . . solvent 5 . . % . . . . 26027 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 26027 _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 'ionic strength' 150 . mM 26027 1 pH 7.5 . pH 26027 1 pressure 1 . atm 26027 1 temperature 298 . K 26027 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 26027 _Software.ID 1 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, One Moon Scientific' . . 26027 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 26027 1 'peak picking' 26027 1 stop_ save_ save_NMRDraw _Software.Sf_category software _Software.Sf_framecode NMRDraw _Software.Entry_ID 26027 _Software.ID 2 _Software.Name NMRDraw _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 26027 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 26027 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 26027 _Software.ID 3 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 26027 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 26027 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 26027 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 26027 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 26027 _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 spectrometer_1 Bruker Avance . 500 . . . 26027 1 2 spectrometer_2 Bruker Avance . 600 . . . 26027 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 26027 _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 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 26027 1 2 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 26027 1 3 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 26027 1 4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 26027 1 5 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 26027 1 6 '3D HNHA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 26027 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 26027 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 water protons . . . . ppm 4.773 na indirect 0.251449530 . . . . . 26027 1 H 1 water protons . . . . ppm 4.773 internal direct 1.000000000 . . . . . 26027 1 N 15 water protons . . . . ppm 4.773 na indirect 0.101329118 . . . . . 26027 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 26027 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.02 _Assigned_chem_shift_list.Chem_shift_13C_err 0.15 _Assigned_chem_shift_list.Chem_shift_15N_err 0.1 _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 '2D 1H-15N HSQC' 1 $sample_1 isotropic 26027 1 2 '3D C(CO)NH' 1 $sample_1 isotropic 26027 1 3 '3D HNCO' 1 $sample_1 isotropic 26027 1 4 '3D HNCA' 1 $sample_1 isotropic 26027 1 5 '3D HNCACB' 1 $sample_1 isotropic 26027 1 6 '3D HNHA' 1 $sample_1 isotropic 26027 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $NMRView . . 26027 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 13 13 GLY CA C 13 45.262 0.15 . 1 . . . . 13 GLY CA . 26027 1 2 . 1 1 14 14 LEU H H 1 7.995 0.02 . 1 . . . . 14 LEU HN . 26027 1 3 . 1 1 14 14 LEU CA C 13 55.141 0.15 . 1 . . . . 14 LEU CA . 26027 1 4 . 1 1 14 14 LEU N N 15 121.344 0.1 . 1 . . . . 14 LEU N . 26027 1 5 . 1 1 15 15 VAL H H 1 8.051 0.02 . 1 . . . . 15 VAL HN . 26027 1 6 . 1 1 15 15 VAL CA C 13 59.775 0.15 . 1 . . . . 15 VAL CA . 26027 1 7 . 1 1 15 15 VAL N N 15 122.440 0.1 . 1 . . . . 15 VAL N . 26027 1 8 . 1 1 16 16 PRO CA C 13 63.127 0.15 . 1 . . . . 16 PRO CA . 26027 1 9 . 1 1 17 17 ARG H H 1 8.449 0.02 . 1 . . . . 17 ARG HN . 26027 1 10 . 1 1 17 17 ARG CA C 13 56.399 0.15 . 1 . . . . 17 ARG CA . 26027 1 11 . 1 1 17 17 ARG N N 15 121.848 0.1 . 1 . . . . 17 ARG N . 26027 1 12 . 1 1 26 26 GLU C C 13 177.023 0.15 . 1 . . . . 26 GLU C . 26027 1 13 . 1 1 26 26 GLU CA C 13 57.338 0.15 . 1 . . . . 26 GLU CA . 26027 1 14 . 1 1 26 26 GLU CG C 13 36.288 0.15 . 1 . . . . 26 GLU CG . 26027 1 15 . 1 1 27 27 THR H H 1 8.127 0.02 . 1 . . . . 27 THR HN . 26027 1 16 . 1 1 27 27 THR C C 13 174.847 0.15 . 1 . . . . 27 THR C . 26027 1 17 . 1 1 27 27 THR CA C 13 62.145 0.15 . 1 . . . . 27 THR CA . 26027 1 18 . 1 1 27 27 THR CB C 13 69.697 0.15 . 1 . . . . 27 THR CB . 26027 1 19 . 1 1 27 27 THR CG2 C 13 21.740 0.15 . 1 . . . . 27 THR CG2 . 26027 1 20 . 1 1 27 27 THR N N 15 113.777 0.1 . 1 . . . . 27 THR N . 26027 1 21 . 1 1 28 28 GLU H H 1 8.239 0.02 . 1 . . . . 28 GLU HN . 26027 1 22 . 1 1 28 28 GLU C C 13 176.867 0.15 . 1 . . . . 28 GLU C . 26027 1 23 . 1 1 28 28 GLU CA C 13 56.875 0.15 . 1 . . . . 28 GLU CA . 26027 1 24 . 1 1 28 28 GLU CB C 13 30.231 0.15 . 1 . . . . 28 GLU CB . 26027 1 25 . 1 1 28 28 GLU CG C 13 36.363 0.15 . 1 . . . . 28 GLU CG . 26027 1 26 . 1 1 28 28 GLU N N 15 123.192 0.1 . 1 . . . . 28 GLU N . 26027 1 27 . 1 1 29 29 ARG H H 1 8.319 0.02 . 1 . . . . 29 ARG HN . 26027 1 28 . 1 1 29 29 ARG HA H 1 4.378 0.02 . 1 . . . . 29 ARG HA . 26027 1 29 . 1 1 29 29 ARG C C 13 175.966 0.15 . 1 . . . . 29 ARG C . 26027 1 30 . 1 1 29 29 ARG CA C 13 56.196 0.15 . 1 . . . . 29 ARG CA . 26027 1 31 . 1 1 29 29 ARG CB C 13 30.653 0.15 . 1 . . . . 29 ARG CB . 26027 1 32 . 1 1 29 29 ARG CG C 13 27.179 0.15 . 1 . . . . 29 ARG CG . 26027 1 33 . 1 1 29 29 ARG N N 15 121.958 0.1 . 1 . . . . 29 ARG N . 26027 1 34 . 1 1 30 30 SER H H 1 8.320 0.02 . 1 . . . . 30 SER HN . 26027 1 35 . 1 1 30 30 SER HA H 1 4.502 0.02 . 1 . . . . 30 SER HA . 26027 1 36 . 1 1 30 30 SER C C 13 174.598 0.15 . 1 . . . . 30 SER C . 26027 1 37 . 1 1 30 30 SER CA C 13 58.279 0.15 . 1 . . . . 30 SER CA . 26027 1 38 . 1 1 30 30 SER CB C 13 64.181 0.15 . 1 . . . . 30 SER CB . 26027 1 39 . 1 1 30 30 SER N N 15 116.965 0.1 . 1 . . . . 30 SER N . 26027 1 40 . 1 1 31 31 GLY H H 1 8.252 0.02 . 1 . . . . 31 GLY HN . 26027 1 41 . 1 1 31 31 GLY CA C 13 44.728 0.15 . 1 . . . . 31 GLY CA . 26027 1 42 . 1 1 31 31 GLY N N 15 110.474 0.1 . 1 . . . . 31 GLY N . 26027 1 43 . 1 1 33 33 GLY C C 13 174.475 0.15 . 1 . . . . 33 GLY C . 26027 1 44 . 1 1 33 33 GLY CA C 13 45.217 0.15 . 1 . . . . 33 GLY CA . 26027 1 45 . 1 1 34 34 THR H H 1 7.950 0.02 . 1 . . . . 34 THR HN . 26027 1 46 . 1 1 34 34 THR C C 13 174.502 0.15 . 1 . . . . 34 THR C . 26027 1 47 . 1 1 34 34 THR CA C 13 61.814 0.15 . 1 . . . . 34 THR CA . 26027 1 48 . 1 1 34 34 THR CB C 13 70.047 0.15 . 1 . . . . 34 THR CB . 26027 1 49 . 1 1 34 34 THR CG2 C 13 21.676 0.15 . 1 . . . . 34 THR CG2 . 26027 1 50 . 1 1 34 34 THR N N 15 113.232 0.1 . 1 . . . . 34 THR N . 26027 1 51 . 1 1 35 35 GLN H H 1 8.452 0.02 . 1 . . . . 35 GLN HN . 26027 1 52 . 1 1 35 35 GLN HE21 H 1 7.544 0.02 . 2 . . . . 35 GLN HE21 . 26027 1 53 . 1 1 35 35 GLN HE22 H 1 6.843 0.02 . 2 . . . . 35 GLN HE22 . 26027 1 54 . 1 1 35 35 GLN CA C 13 53.614 0.15 . 1 . . . . 35 GLN CA . 26027 1 55 . 1 1 35 35 GLN CB C 13 29.039 0.15 . 1 . . . . 35 GLN CB . 26027 1 56 . 1 1 35 35 GLN N N 15 123.865 0.1 . 1 . . . . 35 GLN N . 26027 1 57 . 1 1 35 35 GLN NE2 N 15 112.566 0.1 . 1 . . . . 35 GLN NE2 . 26027 1 58 . 1 1 36 36 PRO CA C 13 63.302 0.15 . 1 . . . . 36 PRO CA . 26027 1 59 . 1 1 36 36 PRO CB C 13 31.996 0.15 . 1 . . . . 36 PRO CB . 26027 1 60 . 1 1 36 36 PRO CG C 13 27.282 0.15 . 1 . . . . 36 PRO CG . 26027 1 61 . 1 1 37 37 ALA H H 1 8.454 0.02 . 1 . . . . 37 ALA HN . 26027 1 62 . 1 1 37 37 ALA HA H 1 4.241 0.02 . 1 . . . . 37 ALA HA . 26027 1 63 . 1 1 37 37 ALA C C 13 175.830 0.15 . 1 . . . . 37 ALA C . 26027 1 64 . 1 1 37 37 ALA CA C 13 52.911 0.15 . 1 . . . . 37 ALA CA . 26027 1 65 . 1 1 37 37 ALA CB C 13 19.163 0.15 . 1 . . . . 37 ALA CB . 26027 1 66 . 1 1 37 37 ALA N N 15 123.945 0.1 . 1 . . . . 37 ALA N . 26027 1 67 . 1 1 38 38 ASP H H 1 8.225 0.02 . 1 . . . . 38 ASP HN . 26027 1 68 . 1 1 38 38 ASP HA H 1 4.514 0.02 . 1 . . . . 38 ASP HA . 26027 1 69 . 1 1 38 38 ASP CA C 13 54.266 0.15 . 1 . . . . 38 ASP CA . 26027 1 70 . 1 1 38 38 ASP CB C 13 41.223 0.15 . 1 . . . . 38 ASP CB . 26027 1 71 . 1 1 38 38 ASP N N 15 118.667 0.1 . 1 . . . . 38 ASP N . 26027 1 72 . 1 1 39 39 ALA H H 1 8.120 0.02 . 1 . . . . 39 ALA HN . 26027 1 73 . 1 1 39 39 ALA HA H 1 4.262 0.02 . 1 . . . . 39 ALA HA . 26027 1 74 . 1 1 39 39 ALA C C 13 176.263 0.15 . 1 . . . . 39 ALA C . 26027 1 75 . 1 1 39 39 ALA CA C 13 52.895 0.15 . 1 . . . . 39 ALA CA . 26027 1 76 . 1 1 39 39 ALA CB C 13 19.182 0.15 . 1 . . . . 39 ALA CB . 26027 1 77 . 1 1 39 39 ALA N N 15 123.793 0.1 . 1 . . . . 39 ALA N . 26027 1 78 . 1 1 40 40 GLN H H 1 8.342 0.02 . 1 . . . . 40 GLN HN . 26027 1 79 . 1 1 40 40 GLN HE21 H 1 7.524 0.02 . 2 . . . . 40 GLN HE21 . 26027 1 80 . 1 1 40 40 GLN HE22 H 1 6.839 0.02 . 2 . . . . 40 GLN HE22 . 26027 1 81 . 1 1 40 40 GLN C C 13 176.456 0.15 . 1 . . . . 40 GLN C . 26027 1 82 . 1 1 40 40 GLN CA C 13 56.162 0.15 . 1 . . . . 40 GLN CA . 26027 1 83 . 1 1 40 40 GLN CG C 13 34.044 0.15 . 1 . . . . 40 GLN CG . 26027 1 84 . 1 1 40 40 GLN N N 15 118.696 0.1 . 1 . . . . 40 GLN N . 26027 1 85 . 1 1 40 40 GLN NE2 N 15 112.783 0.1 . 1 . . . . 40 GLN NE2 . 26027 1 86 . 1 1 41 41 THR H H 1 8.074 0.02 . 1 . . . . 41 THR HN . 26027 1 87 . 1 1 41 41 THR CA C 13 62.007 0.15 . 1 . . . . 41 THR CA . 26027 1 88 . 1 1 41 41 THR CG2 C 13 21.668 0.15 . 1 . . . . 41 THR CG2 . 26027 1 89 . 1 1 41 41 THR N N 15 114.738 0.1 . 1 . . . . 41 THR N . 26027 1 90 . 1 1 42 42 ALA H H 1 8.306 0.02 . 1 . . . . 42 ALA HN . 26027 1 91 . 1 1 42 42 ALA CA C 13 52.860 0.15 . 1 . . . . 42 ALA CA . 26027 1 92 . 1 1 42 42 ALA N N 15 126.307 0.1 . 1 . . . . 42 ALA N . 26027 1 93 . 1 1 45 45 ALA C C 13 177.900 0.15 . 1 . . . . 45 ALA C . 26027 1 94 . 1 1 45 45 ALA CA C 13 52.638 0.15 . 1 . . . . 45 ALA CA . 26027 1 95 . 1 1 45 45 ALA CB C 13 19.280 0.15 . 1 . . . . 45 ALA CB . 26027 1 96 . 1 1 46 46 THR H H 1 8.077 0.02 . 1 . . . . 46 THR HN . 26027 1 97 . 1 1 46 46 THR HA H 1 4.267 0.02 . 1 . . . . 46 THR HA . 26027 1 98 . 1 1 46 46 THR C C 13 174.513 0.15 . 1 . . . . 46 THR C . 26027 1 99 . 1 1 46 46 THR CA C 13 62.172 0.15 . 1 . . . . 46 THR CA . 26027 1 100 . 1 1 46 46 THR CB C 13 69.874 0.15 . 1 . . . . 46 THR CB . 26027 1 101 . 1 1 46 46 THR CG2 C 13 21.656 0.15 . 1 . . . . 46 THR CG2 . 26027 1 102 . 1 1 46 46 THR N N 15 113.631 0.1 . 1 . . . . 46 THR N . 26027 1 103 . 1 1 47 47 VAL H H 1 8.095 0.02 . 1 . . . . 47 VAL HN . 26027 1 104 . 1 1 47 47 VAL C C 13 175.724 0.15 . 1 . . . . 47 VAL C . 26027 1 105 . 1 1 47 47 VAL CA C 13 62.205 0.15 . 1 . . . . 47 VAL CA . 26027 1 106 . 1 1 47 47 VAL CB C 13 32.713 0.15 . 1 . . . . 47 VAL CB . 26027 1 107 . 1 1 47 47 VAL CG1 C 13 20.822 0.15 . 2 . . . . 47 VAL CG1 . 26027 1 108 . 1 1 47 47 VAL N N 15 123.237 0.1 . 1 . . . . 47 VAL N . 26027 1 109 . 1 1 48 48 ARG H H 1 8.375 0.02 . 1 . . . . 48 ARG HN . 26027 1 110 . 1 1 48 48 ARG HA H 1 4.612 0.02 . 1 . . . . 48 ARG HA . 26027 1 111 . 1 1 48 48 ARG CA C 13 53.841 0.15 . 1 . . . . 48 ARG CA . 26027 1 112 . 1 1 48 48 ARG CB C 13 30.330 0.15 . 1 . . . . 48 ARG CB . 26027 1 113 . 1 1 48 48 ARG N N 15 126.313 0.1 . 1 . . . . 48 ARG N . 26027 1 114 . 1 1 49 49 PRO C C 13 176.891 0.15 . 1 . . . . 49 PRO C . 26027 1 115 . 1 1 49 49 PRO CA C 13 62.869 0.15 . 1 . . . . 49 PRO CA . 26027 1 116 . 1 1 49 49 PRO CB C 13 32.095 0.15 . 1 . . . . 49 PRO CB . 26027 1 117 . 1 1 49 49 PRO CD C 13 50.834 0.15 . 1 . . . . 49 PRO CD . 26027 1 118 . 1 1 49 49 PRO CG C 13 27.430 0.15 . 1 . . . . 49 PRO CG . 26027 1 119 . 1 1 50 50 LEU H H 1 8.381 0.02 . 1 . . . . 50 LEU HN . 26027 1 120 . 1 1 50 50 LEU HA H 1 4.302 0.02 . 1 . . . . 50 LEU HA . 26027 1 121 . 1 1 50 50 LEU CA C 13 55.497 0.15 . 1 . . . . 50 LEU CA . 26027 1 122 . 1 1 50 50 LEU CB C 13 42.341 0.15 . 1 . . . . 50 LEU CB . 26027 1 123 . 1 1 50 50 LEU N N 15 122.398 0.1 . 1 . . . . 50 LEU N . 26027 1 124 . 1 1 52 52 THR CA C 13 62.093 0.15 . 1 . . . . 52 THR CA . 26027 1 125 . 1 1 52 52 THR CG2 C 13 21.717 0.15 . 1 . . . . 52 THR CG2 . 26027 1 126 . 1 1 53 53 GLN H H 1 8.234 0.02 . 1 . . . . 53 GLN HN . 26027 1 127 . 1 1 53 53 GLN HE21 H 1 7.526 0.02 . 2 . . . . 53 GLN HE21 . 26027 1 128 . 1 1 53 53 GLN HE22 H 1 6.840 0.02 . 2 . . . . 53 GLN HE22 . 26027 1 129 . 1 1 53 53 GLN CA C 13 55.917 0.15 . 1 . . . . 53 GLN CA . 26027 1 130 . 1 1 53 53 GLN CG C 13 33.860 0.15 . 1 . . . . 53 GLN CG . 26027 1 131 . 1 1 53 53 GLN N N 15 122.050 0.1 . 1 . . . . 53 GLN N . 26027 1 132 . 1 1 53 53 GLN NE2 N 15 112.535 0.1 . 1 . . . . 53 GLN NE2 . 26027 1 133 . 1 1 54 54 ALA H H 1 8.260 0.02 . 1 . . . . 54 ALA HN . 26027 1 134 . 1 1 54 54 ALA C C 13 177.362 0.15 . 1 . . . . 54 ALA C . 26027 1 135 . 1 1 54 54 ALA CA C 13 52.570 0.15 . 1 . . . . 54 ALA CA . 26027 1 136 . 1 1 54 54 ALA CB C 13 19.170 0.15 . 1 . . . . 54 ALA CB . 26027 1 137 . 1 1 54 54 ALA N N 15 125.508 0.1 . 1 . . . . 54 ALA N . 26027 1 138 . 1 1 55 55 VAL H H 1 7.955 0.02 . 1 . . . . 55 VAL HN . 26027 1 139 . 1 1 55 55 VAL C C 13 175.671 0.15 . 1 . . . . 55 VAL C . 26027 1 140 . 1 1 55 55 VAL CA C 13 61.968 0.15 . 1 . . . . 55 VAL CA . 26027 1 141 . 1 1 55 55 VAL CB C 13 33.100 0.15 . 1 . . . . 55 VAL CB . 26027 1 142 . 1 1 55 55 VAL CG1 C 13 20.526 0.15 . 2 . . . . 55 VAL CG1 . 26027 1 143 . 1 1 55 55 VAL N N 15 119.011 0.1 . 1 . . . . 55 VAL N . 26027 1 144 . 1 1 56 56 PHE H H 1 8.332 0.02 . 1 . . . . 56 PHE HN . 26027 1 145 . 1 1 56 56 PHE CA C 13 57.598 0.15 . 1 . . . . 56 PHE CA . 26027 1 146 . 1 1 56 56 PHE CB C 13 39.797 0.15 . 1 . . . . 56 PHE CB . 26027 1 147 . 1 1 56 56 PHE N N 15 124.652 0.1 . 1 . . . . 56 PHE N . 26027 1 148 . 1 1 57 57 ARG H H 1 8.108 0.02 . 1 . . . . 57 ARG HN . 26027 1 149 . 1 1 57 57 ARG HA H 1 4.519 0.02 . 1 . . . . 57 ARG HA . 26027 1 150 . 1 1 57 57 ARG CA C 13 53.282 0.15 . 1 . . . . 57 ARG CA . 26027 1 151 . 1 1 57 57 ARG CB C 13 30.821 0.15 . 1 . . . . 57 ARG CB . 26027 1 152 . 1 1 57 57 ARG N N 15 125.237 0.1 . 1 . . . . 57 ARG N . 26027 1 153 . 1 1 58 58 PRO CA C 13 63.110 0.15 . 1 . . . . 58 PRO CA . 26027 1 154 . 1 1 58 58 PRO CB C 13 31.828 0.15 . 1 . . . . 58 PRO CB . 26027 1 155 . 1 1 58 58 PRO CD C 13 50.632 0.15 . 1 . . . . 58 PRO CD . 26027 1 156 . 1 1 58 58 PRO CG C 13 27.154 0.15 . 1 . . . . 58 PRO CG . 26027 1 157 . 1 1 59 59 ASP H H 1 8.306 0.02 . 1 . . . . 59 ASP HN . 26027 1 158 . 1 1 59 59 ASP HA H 1 4.467 0.02 . 1 . . . . 59 ASP HA . 26027 1 159 . 1 1 59 59 ASP C C 13 176.168 0.15 . 1 . . . . 59 ASP C . 26027 1 160 . 1 1 59 59 ASP CA C 13 54.144 0.15 . 1 . . . . 59 ASP CA . 26027 1 161 . 1 1 59 59 ASP CB C 13 40.870 0.15 . 1 . . . . 59 ASP CB . 26027 1 162 . 1 1 59 59 ASP N N 15 119.143 0.1 . 1 . . . . 59 ASP N . 26027 1 163 . 1 1 60 60 PHE H H 1 8.058 0.02 . 1 . . . . 60 PHE HN . 26027 1 164 . 1 1 60 60 PHE HA H 1 4.583 0.02 . 1 . . . . 60 PHE HA . 26027 1 165 . 1 1 60 60 PHE C C 13 176.274 0.15 . 1 . . . . 60 PHE C . 26027 1 166 . 1 1 60 60 PHE CA C 13 57.820 0.15 . 1 . . . . 60 PHE CA . 26027 1 167 . 1 1 60 60 PHE CB C 13 39.517 0.15 . 1 . . . . 60 PHE CB . 26027 1 168 . 1 1 60 60 PHE N N 15 120.024 0.1 . 1 . . . . 60 PHE N . 26027 1 169 . 1 1 61 61 GLY H H 1 8.385 0.02 . 1 . . . . 61 GLY HN . 26027 1 170 . 1 1 61 61 GLY HA2 H 1 3.901 0.02 . 2 . . . . 61 GLY HA . 26027 1 171 . 1 1 61 61 GLY HA3 H 1 3.901 0.02 . 2 . . . . 61 GLY HA . 26027 1 172 . 1 1 61 61 GLY C C 13 173.918 0.15 . 1 . . . . 61 GLY C . 26027 1 173 . 1 1 61 61 GLY CA C 13 45.401 0.15 . 1 . . . . 61 GLY CA . 26027 1 174 . 1 1 61 61 GLY N N 15 110.294 0.1 . 1 . . . . 61 GLY N . 26027 1 175 . 1 1 62 62 ASP H H 1 8.181 0.02 . 1 . . . . 62 ASP HN . 26027 1 176 . 1 1 62 62 ASP C C 13 176.605 0.15 . 1 . . . . 62 ASP C . 26027 1 177 . 1 1 62 62 ASP CA C 13 54.534 0.15 . 1 . . . . 62 ASP CA . 26027 1 178 . 1 1 62 62 ASP CB C 13 41.355 0.15 . 1 . . . . 62 ASP CB . 26027 1 179 . 1 1 62 62 ASP N N 15 120.484 0.1 . 1 . . . . 62 ASP N . 26027 1 180 . 1 1 63 63 GLU H H 1 8.465 0.02 . 1 . . . . 63 GLU HN . 26027 1 181 . 1 1 63 63 GLU HA H 1 4.159 0.02 . 1 . . . . 63 GLU HA . 26027 1 182 . 1 1 63 63 GLU C C 13 176.494 0.15 . 1 . . . . 63 GLU C . 26027 1 183 . 1 1 63 63 GLU CA C 13 57.106 0.15 . 1 . . . . 63 GLU CA . 26027 1 184 . 1 1 63 63 GLU CB C 13 30.175 0.15 . 1 . . . . 63 GLU CB . 26027 1 185 . 1 1 63 63 GLU CG C 13 36.440 0.15 . 1 . . . . 63 GLU CG . 26027 1 186 . 1 1 63 63 GLU N N 15 120.464 0.1 . 1 . . . . 63 GLU N . 26027 1 187 . 1 1 64 64 ASP H H 1 8.286 0.02 . 1 . . . . 64 ASP HN . 26027 1 188 . 1 1 64 64 ASP HA H 1 4.500 0.02 . 1 . . . . 64 ASP HA . 26027 1 189 . 1 1 64 64 ASP C C 13 175.953 0.15 . 1 . . . . 64 ASP C . 26027 1 190 . 1 1 64 64 ASP CA C 13 54.640 0.15 . 1 . . . . 64 ASP CA . 26027 1 191 . 1 1 64 64 ASP CB C 13 41.161 0.15 . 1 . . . . 64 ASP CB . 26027 1 192 . 1 1 64 64 ASP N N 15 120.272 0.1 . 1 . . . . 64 ASP N . 26027 1 193 . 1 1 65 65 ASN H H 1 8.115 0.02 . 1 . . . . 65 ASN HN . 26027 1 194 . 1 1 65 65 ASN HA H 1 4.613 0.02 . 1 . . . . 65 ASN HA . 26027 1 195 . 1 1 65 65 ASN HD21 H 1 7.547 0.02 . 2 . . . . 65 ASN HD21 . 26027 1 196 . 1 1 65 65 ASN HD22 H 1 6.840 0.02 . 2 . . . . 65 ASN HD22 . 26027 1 197 . 1 1 65 65 ASN C C 13 174.496 0.15 . 1 . . . . 65 ASN C . 26027 1 198 . 1 1 65 65 ASN CA C 13 53.113 0.15 . 1 . . . . 65 ASN CA . 26027 1 199 . 1 1 65 65 ASN CB C 13 39.101 0.15 . 1 . . . . 65 ASN CB . 26027 1 200 . 1 1 65 65 ASN N N 15 118.237 0.1 . 1 . . . . 65 ASN N . 26027 1 201 . 1 1 65 65 ASN ND2 N 15 113.006 0.1 . 1 . . . . 65 ASN ND2 . 26027 1 202 . 1 1 66 66 PHE H H 1 8.060 0.02 . 1 . . . . 66 PHE HN . 26027 1 203 . 1 1 66 66 PHE HA H 1 4.796 0.02 . 1 . . . . 66 PHE HA . 26027 1 204 . 1 1 66 66 PHE CA C 13 55.704 0.15 . 1 . . . . 66 PHE CA . 26027 1 205 . 1 1 66 66 PHE CB C 13 39.083 0.15 . 1 . . . . 66 PHE CB . 26027 1 206 . 1 1 66 66 PHE N N 15 121.419 0.1 . 1 . . . . 66 PHE N . 26027 1 207 . 1 1 67 67 PRO C C 13 176.480 0.15 . 1 . . . . 67 PRO C . 26027 1 208 . 1 1 67 67 PRO CA C 13 62.858 0.15 . 1 . . . . 67 PRO CA . 26027 1 209 . 1 1 67 67 PRO CB C 13 31.798 0.15 . 1 . . . . 67 PRO CB . 26027 1 210 . 1 1 67 67 PRO CD C 13 50.537 0.15 . 1 . . . . 67 PRO CD . 26027 1 211 . 1 1 67 67 PRO CG C 13 27.205 0.15 . 1 . . . . 67 PRO CG . 26027 1 212 . 1 1 68 68 HIS H H 1 8.278 0.02 . 1 . . . . 68 HIS HN . 26027 1 213 . 1 1 68 68 HIS CA C 13 54.366 0.15 . 1 . . . . 68 HIS CA . 26027 1 214 . 1 1 68 68 HIS CB C 13 30.100 0.15 . 1 . . . . 68 HIS CB . 26027 1 215 . 1 1 68 68 HIS N N 15 121.447 0.1 . 1 . . . . 68 HIS N . 26027 1 216 . 1 1 69 69 PRO C C 13 177.077 0.15 . 1 . . . . 69 PRO C . 26027 1 217 . 1 1 69 69 PRO CA C 13 63.357 0.15 . 1 . . . . 69 PRO CA . 26027 1 218 . 1 1 69 69 PRO CB C 13 32.192 0.15 . 1 . . . . 69 PRO CB . 26027 1 219 . 1 1 69 69 PRO CG C 13 27.425 0.15 . 1 . . . . 69 PRO CG . 26027 1 220 . 1 1 70 70 THR H H 1 8.414 0.02 . 1 . . . . 70 THR HN . 26027 1 221 . 1 1 70 70 THR HA H 1 4.315 0.02 . 1 . . . . 70 THR HA . 26027 1 222 . 1 1 70 70 THR C C 13 174.627 0.15 . 1 . . . . 70 THR C . 26027 1 223 . 1 1 70 70 THR CA C 13 62.002 0.15 . 1 . . . . 70 THR CA . 26027 1 224 . 1 1 70 70 THR CB C 13 69.907 0.15 . 1 . . . . 70 THR CB . 26027 1 225 . 1 1 70 70 THR CG2 C 13 21.749 0.15 . 1 . . . . 70 THR CG2 . 26027 1 226 . 1 1 70 70 THR N N 15 115.012 0.1 . 1 . . . . 70 THR N . 26027 1 227 . 1 1 71 71 LEU H H 1 8.359 0.02 . 1 . . . . 71 LEU HN . 26027 1 228 . 1 1 71 71 LEU C C 13 177.356 0.15 . 1 . . . . 71 LEU C . 26027 1 229 . 1 1 71 71 LEU CA C 13 55.081 0.15 . 1 . . . . 71 LEU CA . 26027 1 230 . 1 1 71 71 LEU CB C 13 42.609 0.15 . 1 . . . . 71 LEU CB . 26027 1 231 . 1 1 71 71 LEU CD1 C 13 25.033 0.15 . 2 . . . . 71 LEU CD1 . 26027 1 232 . 1 1 71 71 LEU CD2 C 13 23.411 0.15 . 2 . . . . 71 LEU CD2 . 26027 1 233 . 1 1 71 71 LEU CG C 13 26.971 0.15 . 1 . . . . 71 LEU CG . 26027 1 234 . 1 1 71 71 LEU N N 15 125.115 0.1 . 1 . . . . 71 LEU N . 26027 1 235 . 1 1 72 72 GLY H H 1 8.244 0.02 . 1 . . . . 72 GLY HN . 26027 1 236 . 1 1 72 72 GLY HA2 H 1 4.095 0.02 . 2 . . . . 72 GLY HA . 26027 1 237 . 1 1 72 72 GLY HA3 H 1 4.095 0.02 . 2 . . . . 72 GLY HA . 26027 1 238 . 1 1 72 72 GLY CA C 13 44.686 0.15 . 1 . . . . 72 GLY CA . 26027 1 239 . 1 1 72 72 GLY N N 15 109.909 0.1 . 1 . . . . 72 GLY N . 26027 1 240 . 1 1 73 73 PRO C C 13 176.964 0.15 . 1 . . . . 73 PRO C . 26027 1 241 . 1 1 73 73 PRO CA C 13 63.320 0.15 . 1 . . . . 73 PRO CA . 26027 1 242 . 1 1 73 73 PRO CB C 13 32.178 0.15 . 1 . . . . 73 PRO CB . 26027 1 243 . 1 1 73 73 PRO CD C 13 49.848 0.15 . 1 . . . . 73 PRO CD . 26027 1 244 . 1 1 73 73 PRO CG C 13 27.035 0.15 . 1 . . . . 73 PRO CG . 26027 1 245 . 1 1 74 74 ASP H H 1 8.467 0.02 . 1 . . . . 74 ASP HN . 26027 1 246 . 1 1 74 74 ASP HA H 1 4.610 0.02 . 1 . . . . 74 ASP HA . 26027 1 247 . 1 1 74 74 ASP C C 13 176.412 0.15 . 1 . . . . 74 ASP C . 26027 1 248 . 1 1 74 74 ASP CA C 13 54.578 0.15 . 1 . . . . 74 ASP CA . 26027 1 249 . 1 1 74 74 ASP CB C 13 40.885 0.15 . 1 . . . . 74 ASP CB . 26027 1 250 . 1 1 74 74 ASP N N 15 119.609 0.1 . 1 . . . . 74 ASP N . 26027 1 251 . 1 1 75 75 THR H H 1 7.936 0.02 . 1 . . . . 75 THR HN . 26027 1 252 . 1 1 75 75 THR HA H 1 4.271 0.02 . 1 . . . . 75 THR HA . 26027 1 253 . 1 1 75 75 THR C C 13 174.412 0.15 . 1 . . . . 75 THR C . 26027 1 254 . 1 1 75 75 THR CA C 13 61.850 0.15 . 1 . . . . 75 THR CA . 26027 1 255 . 1 1 75 75 THR CB C 13 70.098 0.15 . 1 . . . . 75 THR CB . 26027 1 256 . 1 1 75 75 THR CG2 C 13 21.696 0.15 . 1 . . . . 75 THR CG2 . 26027 1 257 . 1 1 75 75 THR N N 15 113.509 0.1 . 1 . . . . 75 THR N . 26027 1 258 . 1 1 76 76 GLU H H 1 8.330 0.02 . 1 . . . . 76 GLU HN . 26027 1 259 . 1 1 76 76 GLU CA C 13 54.531 0.15 . 1 . . . . 76 GLU CA . 26027 1 260 . 1 1 76 76 GLU CB C 13 29.738 0.15 . 1 . . . . 76 GLU CB . 26027 1 261 . 1 1 76 76 GLU N N 15 124.637 0.1 . 1 . . . . 76 GLU N . 26027 1 262 . 1 1 77 77 PRO CA C 13 63.531 0.15 . 1 . . . . 77 PRO CA . 26027 1 263 . 1 1 78 78 GLN H H 1 8.548 0.02 . 1 . . . . 78 GLN HN . 26027 1 264 . 1 1 78 78 GLN HA H 1 4.264 0.02 . 1 . . . . 78 GLN HA . 26027 1 265 . 1 1 78 78 GLN HE21 H 1 7.509 0.02 . 2 . . . . 78 GLN HE21 . 26027 1 266 . 1 1 78 78 GLN HE22 H 1 6.840 0.02 . 2 . . . . 78 GLN HE22 . 26027 1 267 . 1 1 78 78 GLN CA C 13 56.215 0.15 . 1 . . . . 78 GLN CA . 26027 1 268 . 1 1 78 78 GLN CG C 13 33.714 0.15 . 1 . . . . 78 GLN CG . 26027 1 269 . 1 1 78 78 GLN N N 15 120.041 0.1 . 1 . . . . 78 GLN N . 26027 1 270 . 1 1 78 78 GLN NE2 N 15 112.525 0.1 . 1 . . . . 78 GLN NE2 . 26027 1 271 . 1 1 79 79 ASP H H 1 8.326 0.02 . 1 . . . . 79 ASP HN . 26027 1 272 . 1 1 79 79 ASP CA C 13 55.326 0.15 . 1 . . . . 79 ASP CA . 26027 1 273 . 1 1 79 79 ASP N N 15 120.411 0.1 . 1 . . . . 79 ASP N . 26027 1 274 . 1 1 80 80 ARG H H 1 8.207 0.02 . 1 . . . . 80 ARG HN . 26027 1 275 . 1 1 80 80 ARG C C 13 176.274 0.15 . 1 . . . . 80 ARG C . 26027 1 276 . 1 1 80 80 ARG CA C 13 56.686 0.15 . 1 . . . . 80 ARG CA . 26027 1 277 . 1 1 80 80 ARG N N 15 121.099 0.1 . 1 . . . . 80 ARG N . 26027 1 278 . 1 1 81 81 MET H H 1 8.266 0.02 . 1 . . . . 81 MET HN . 26027 1 279 . 1 1 81 81 MET CA C 13 55.578 0.15 . 1 . . . . 81 MET CA . 26027 1 280 . 1 1 81 81 MET N N 15 119.759 0.1 . 1 . . . . 81 MET N . 26027 1 281 . 1 1 82 82 ALA H H 1 8.147 0.02 . 1 . . . . 82 ALA HN . 26027 1 282 . 1 1 82 82 ALA CA C 13 52.883 0.15 . 1 . . . . 82 ALA CA . 26027 1 283 . 1 1 82 82 ALA CB C 13 19.117 0.15 . 1 . . . . 82 ALA CB . 26027 1 284 . 1 1 82 82 ALA N N 15 124.402 0.1 . 1 . . . . 82 ALA N . 26027 1 285 . 1 1 83 83 THR H H 1 8.135 0.02 . 1 . . . . 83 THR HN . 26027 1 286 . 1 1 83 83 THR CA C 13 61.928 0.15 . 1 . . . . 83 THR CA . 26027 1 287 . 1 1 83 83 THR N N 15 112.880 0.1 . 1 . . . . 83 THR N . 26027 1 288 . 1 1 90 90 PRO C C 13 176.807 0.15 . 1 . . . . 90 PRO C . 26027 1 289 . 1 1 90 90 PRO CA C 13 62.884 0.15 . 1 . . . . 90 PRO CA . 26027 1 290 . 1 1 90 90 PRO CB C 13 32.040 0.15 . 1 . . . . 90 PRO CB . 26027 1 291 . 1 1 90 90 PRO CD C 13 50.386 0.15 . 1 . . . . 90 PRO CD . 26027 1 292 . 1 1 90 90 PRO CG C 13 27.315 0.15 . 1 . . . . 90 PRO CG . 26027 1 293 . 1 1 91 91 VAL H H 1 8.179 0.02 . 1 . . . . 91 VAL HN . 26027 1 294 . 1 1 91 91 VAL CA C 13 62.366 0.15 . 1 . . . . 91 VAL CA . 26027 1 295 . 1 1 91 91 VAL CB C 13 32.294 0.15 . 1 . . . . 91 VAL CB . 26027 1 296 . 1 1 91 91 VAL N N 15 120.484 0.1 . 1 . . . . 91 VAL N . 26027 1 297 . 1 1 94 94 LEU C C 13 175.277 0.15 . 1 . . . . 94 LEU C . 26027 1 298 . 1 1 94 94 LEU CB C 13 42.572 0.15 . 1 . . . . 94 LEU CB . 26027 1 299 . 1 1 94 94 LEU CD1 C 13 25.040 0.15 . 2 . . . . 94 LEU CD1 . 26027 1 300 . 1 1 94 94 LEU CD2 C 13 23.281 0.15 . 2 . . . . 94 LEU CD2 . 26027 1 301 . 1 1 94 94 LEU CG C 13 26.999 0.15 . 1 . . . . 94 LEU CG . 26027 1 302 . 1 1 95 95 GLY H H 1 7.923 0.02 . 1 . . . . 95 GLY HN . 26027 1 303 . 1 1 95 95 GLY HA2 H 1 3.709 0.02 . 2 . . . . 95 GLY HA . 26027 1 304 . 1 1 95 95 GLY HA3 H 1 3.709 0.02 . 2 . . . . 95 GLY HA . 26027 1 305 . 1 1 95 95 GLY CA C 13 46.103 0.15 . 1 . . . . 95 GLY CA . 26027 1 306 . 1 1 95 95 GLY N N 15 115.779 0.1 . 1 . . . . 95 GLY N . 26027 1 stop_ save_