data_18649 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18649 _Entry.Title ; Transmembrane domain of Amyloid precursor protein WT ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-08-07 _Entry.Accession_date 2012-08-07 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details ; HCCH-TOCSY H(CCCO)NH-H H(CCCO)NH-C ; _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 Wen Chen . . . 18649 2 Chunyu Wang . . . 18649 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Rensselaer Polytechnic Institute' . 18649 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18649 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 144 18649 '15N chemical shifts' 30 18649 '1H chemical shifts' 252 18649 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 3 . . 2014-02-19 2012-08-07 update BMRB 'update entry citation' 18649 2 . . 2013-12-10 2012-08-07 update author 'update entry citation' 18649 1 . . 2012-09-07 2012-08-07 original author 'original release' 18649 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18648 'Transmembrane domain of Amyloid precursor protein V44M' 18649 PDB 2LZ3 'BMRB Entry Tracking System' 18649 stop_ save_ ############### # Citations # ############### save_APPTM _Citation.Sf_category citations _Citation.Sf_framecode APPTM _Citation.Entry_ID 18649 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24390130 _Citation.Full_citation . _Citation.Title 'Familial Alzheimer's mutations within APPTM increase A42 production by enhancing accessibility of -cleavage site.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Commun.' _Citation.Journal_name_full 'Nature communications' _Citation.Journal_volume 5 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 3037 _Citation.Page_last 3037 _Citation.Year 2014 _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 Wen Chen . . . 18649 1 2 Eric Gamache . . . 18649 1 3 David Rosenman . J. . 18649 1 4 Jian Xie . . . 18649 1 5 Maria Lopez . M. . 18649 1 6 Yue-Ming Li . . . 18649 1 7 Chunyu Wang . . . 18649 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18649 _Assembly.ID 1 _Assembly.Name 'APPTM dimer' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _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 . _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 'wild type chain, 1' 1 $apptm_wt A . yes native no no . . . 18649 1 2 'wild type chain, 2' 1 $apptm_wt B . yes native no no . . . 18649 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_apptm_wt _Entity.Sf_category entity _Entity.Sf_framecode apptm_wt _Entity.Entry_ID 18649 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'wild type monomer' _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 ; GAMAKGAIIGLMVGGVVIAT VIVITLVMLKKK ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _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 32 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15775 . APP_C99 . . . . . 87.50 122 100.00 100.00 8.09e-07 . . . . 18649 1 2 no BMRB 18080 . entity . . . . . 87.50 43 100.00 100.00 3.73e-06 . . . . 18649 1 3 no PDB 2LLM . "Structure Of Amyloid Precursor Protein's Transmembrane Domain" . . . . . 87.50 43 100.00 100.00 3.73e-06 . . . . 18649 1 4 no PDB 2LOH . "Dimeric Structure Of Transmembrane Domain Of Amyloid Precursor Protein In Micellar Environment" . . . . . 87.50 43 100.00 100.00 3.73e-06 . . . . 18649 1 5 no PDB 2LP1 . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" . . . . . 87.50 122 100.00 100.00 8.09e-07 . . . . 18649 1 6 no PDB 2LZ3 . "Solution Nmr Structure Of Transmembrane Domain Of Amyloid Precursor Protein Wt" . . . . . 87.50 28 100.00 100.00 7.39e-06 . . . . 18649 1 7 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 8 no DBJ BAA24230 . "EL amyloid precursor protein 699 [Narke japonica]" . . . . . 87.50 699 100.00 100.00 3.69e-07 . . . . 18649 1 9 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 10 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 78.13 52 100.00 100.00 1.83e-04 . . . . 18649 1 11 no DBJ BAC34997 . "unnamed protein product [Mus musculus]" . . . . . 87.50 218 100.00 100.00 5.96e-08 . . . . 18649 1 12 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 87.50 751 100.00 100.00 3.82e-07 . . . . 18649 1 13 no EMBL CAA30488 . "unnamed protein product [Rattus rattus]" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 1 14 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 1 15 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 81.25 59 100.00 100.00 3.46e-05 . . . . 18649 1 16 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 78.13 58 100.00 100.00 1.96e-04 . . . . 18649 1 17 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 87.50 97 100.00 100.00 1.73e-06 . . . . 18649 1 18 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 1 19 no GB AAA37139 . "beta-amyloid protein [Mus musculus]" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 1 20 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 87.50 412 100.00 100.00 2.47e-07 . . . . 18649 1 21 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 87.50 264 100.00 100.00 1.10e-07 . . . . 18649 1 22 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 78.13 57 100.00 100.00 1.75e-04 . . . . 18649 1 23 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 78.13 57 100.00 100.00 1.75e-04 . . . . 18649 1 24 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 78.13 57 100.00 100.00 1.75e-04 . . . . 18649 1 25 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 78.13 57 100.00 100.00 1.75e-04 . . . . 18649 1 26 no PIR JH0773 . "Alzheimer's disease amyloid beta protein precursor - African clawed frog" . . . . . 87.50 747 100.00 100.00 3.81e-07 . . . . 18649 1 27 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 1 28 no PRF 1403400A . "amyloid protein A4" . . . . . 87.50 751 100.00 100.00 3.82e-07 . . . . 18649 1 29 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 87.50 412 100.00 100.00 2.47e-07 . . . . 18649 1 30 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 87.50 574 100.00 100.00 3.31e-07 . . . . 18649 1 31 no PRF 1507304C . "beta amyloid peptide precursor" . . . . . 87.50 165 100.00 100.00 4.03e-08 . . . . 18649 1 32 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 33 no REF NP_001005698 . "amyloid beta A4 protein precursor [Xenopus (Silurana) tropicalis]" . . . . . 87.50 750 100.00 100.00 3.82e-07 . . . . 18649 1 34 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 35 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 36 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 1 37 no SP P05067 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 38 no SP P08592 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 39 no SP P12023 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 40 no SP P53601 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 41 no SP P79307 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 87.50 770 100.00 100.00 3.86e-07 . . . . 18649 1 42 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 87.50 695 100.00 100.00 3.68e-07 . . . . 18649 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 . GLY . 18649 1 2 . ALA . 18649 1 3 . MET . 18649 1 4 . ALA . 18649 1 5 . LYS . 18649 1 6 . GLY . 18649 1 7 . ALA . 18649 1 8 . ILE . 18649 1 9 . ILE . 18649 1 10 . GLY . 18649 1 11 . LEU . 18649 1 12 . MET . 18649 1 13 . VAL . 18649 1 14 . GLY . 18649 1 15 . GLY . 18649 1 16 . VAL . 18649 1 17 . VAL . 18649 1 18 . ILE . 18649 1 19 . ALA . 18649 1 20 . THR . 18649 1 21 . VAL . 18649 1 22 . ILE . 18649 1 23 . VAL . 18649 1 24 . ILE . 18649 1 25 . THR . 18649 1 26 . LEU . 18649 1 27 . VAL . 18649 1 28 . MET . 18649 1 29 . LEU . 18649 1 30 . LYS . 18649 1 31 . LYS . 18649 1 32 . LYS . 18649 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 . GLY 1 1 18649 1 . ALA 2 2 18649 1 . MET 3 3 18649 1 . ALA 4 4 18649 1 . LYS 5 5 18649 1 . GLY 6 6 18649 1 . ALA 7 7 18649 1 . ILE 8 8 18649 1 . ILE 9 9 18649 1 . GLY 10 10 18649 1 . LEU 11 11 18649 1 . MET 12 12 18649 1 . VAL 13 13 18649 1 . GLY 14 14 18649 1 . GLY 15 15 18649 1 . VAL 16 16 18649 1 . VAL 17 17 18649 1 . ILE 18 18 18649 1 . ALA 19 19 18649 1 . THR 20 20 18649 1 . VAL 21 21 18649 1 . ILE 22 22 18649 1 . VAL 23 23 18649 1 . ILE 24 24 18649 1 . THR 25 25 18649 1 . LEU 26 26 18649 1 . VAL 27 27 18649 1 . MET 28 28 18649 1 . LEU 29 29 18649 1 . LYS 30 30 18649 1 . LYS 31 31 18649 1 . LYS 32 32 18649 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 18649 _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 $apptm_wt . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18649 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 18649 _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 $apptm_wt . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . PetM41 . . . . . . 18649 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_apptm_wt_sample _Sample.Sf_category sample _Sample.Sf_framecode apptm_wt_sample _Sample.Entry_ID 18649 _Sample.ID 1 _Sample.Type micelle _Sample.Sub_type . _Sample.Details '5% DPC' _Sample.Aggregate_sample_number 2 _Sample.Solvent_system '90% H2O/10% D2O, 5% DPC' _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 'APPTM dimer' '[U-100% 13C; U-100% 15N]' . . 1 $apptm_wt . . . . . mM . . . . 18649 1 2 'sodium phosphate' 'natural abundance' . . . . . . 0.5 . . mM . . . . 18649 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18649 1 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18649 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 18649 _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' 0 . M 18649 1 pH 7.2 . pH 18649 1 pressure 1 . atm 18649 1 temperature 313 . K 18649 1 stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18649 _Software.ID 1 _Software.Name SPARKY _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' . . 18649 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18649 1 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 18649 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 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 18649 _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 . 800 . . . 18649 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 18649 _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 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 3 '3D HNCACB' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 4 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 5 '3D HNCO' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 6 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 7 '3D HNHA' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 1 8 '3D H(CCO)NH' no . . . . . . . . . . 1 $apptm_wt_sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18649 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 18649 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 18649 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18649 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18649 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 18649 _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 . _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 '2D 1H-15N HSQC' . . . 18649 1 2 '2D 1H-13C HSQC' . . . 18649 1 3 '3D HNCACB' . . . 18649 1 4 '3D HBHA(CO)NH' . . . 18649 1 5 '3D HNCO' . . . 18649 1 6 '3D HCCH-TOCSY' . . . 18649 1 7 '3D HNHA' . . . 18649 1 8 '3D H(CCO)NH' . . . 18649 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 2 2 ALA HA H 1 4.345 0.007 . . . . . . 2 ALA HA . 18649 1 2 . 1 1 2 2 ALA HB1 H 1 1.425 0.003 . . . . . . 2 ALA QB . 18649 1 3 . 1 1 2 2 ALA HB2 H 1 1.425 0.003 . . . . . . 2 ALA QB . 18649 1 4 . 1 1 2 2 ALA HB3 H 1 1.425 0.003 . . . . . . 2 ALA QB . 18649 1 5 . 1 1 2 2 ALA C C 13 177.782 0.000 . . . . . . 2 ALA C . 18649 1 6 . 1 1 2 2 ALA CA C 13 52.753 0.057 . . . . . . 2 ALA CA . 18649 1 7 . 1 1 2 2 ALA CB C 13 19.428 0.158 . . . . . . 2 ALA CB . 18649 1 8 . 1 1 3 3 MET H H 1 8.576 0.004 . . . . . . 3 MET H . 18649 1 9 . 1 1 3 3 MET HA H 1 4.364 0.005 . . . . . . 3 MET HA . 18649 1 10 . 1 1 3 3 MET HB2 H 1 2.051 0.005 . . . . . . 3 MET QB . 18649 1 11 . 1 1 3 3 MET HB3 H 1 2.051 0.005 . . . . . . 3 MET QB . 18649 1 12 . 1 1 3 3 MET HG2 H 1 2.630 0.002 . . . . . . 3 MET HG2 . 18649 1 13 . 1 1 3 3 MET HG3 H 1 2.574 0.010 . . . . . . 3 MET HG3 . 18649 1 14 . 1 1 3 3 MET HE1 H 1 2.064 0.001 . . . . . . 3 MET QE . 18649 1 15 . 1 1 3 3 MET HE2 H 1 2.064 0.001 . . . . . . 3 MET QE . 18649 1 16 . 1 1 3 3 MET HE3 H 1 2.064 0.001 . . . . . . 3 MET QE . 18649 1 17 . 1 1 3 3 MET C C 13 175.698 0.000 . . . . . . 3 MET C . 18649 1 18 . 1 1 3 3 MET CA C 13 56.015 0.053 . . . . . . 3 MET CA . 18649 1 19 . 1 1 3 3 MET CB C 13 33.145 0.069 . . . . . . 3 MET CB . 18649 1 20 . 1 1 3 3 MET CG C 13 32.567 0.099 . . . . . . 3 MET CG . 18649 1 21 . 1 1 3 3 MET CE C 13 17.195 0.046 . . . . . . 3 MET CE . 18649 1 22 . 1 1 3 3 MET N N 15 121.531 0.054 . . . . . . 3 MET N . 18649 1 23 . 1 1 4 4 ALA H H 1 8.364 0.009 . . . . . . 4 ALA H . 18649 1 24 . 1 1 4 4 ALA HA H 1 4.309 0.006 . . . . . . 4 ALA HA . 18649 1 25 . 1 1 4 4 ALA HB1 H 1 1.521 0.010 . . . . . . 4 ALA QB . 18649 1 26 . 1 1 4 4 ALA HB2 H 1 1.521 0.010 . . . . . . 4 ALA QB . 18649 1 27 . 1 1 4 4 ALA HB3 H 1 1.521 0.010 . . . . . . 4 ALA QB . 18649 1 28 . 1 1 4 4 ALA C C 13 178.075 0.000 . . . . . . 4 ALA C . 18649 1 29 . 1 1 4 4 ALA CA C 13 52.423 0.110 . . . . . . 4 ALA CA . 18649 1 30 . 1 1 4 4 ALA CB C 13 19.176 0.147 . . . . . . 4 ALA CB . 18649 1 31 . 1 1 4 4 ALA N N 15 127.201 0.065 . . . . . . 4 ALA N . 18649 1 32 . 1 1 5 5 LYS H H 1 8.432 0.005 . . . . . . 5 LYS H . 18649 1 33 . 1 1 5 5 LYS HA H 1 4.039 0.003 . . . . . . 5 LYS HA . 18649 1 34 . 1 1 5 5 LYS HB2 H 1 1.862 0.004 . . . . . . 5 LYS QB . 18649 1 35 . 1 1 5 5 LYS HB3 H 1 1.862 0.004 . . . . . . 5 LYS QB . 18649 1 36 . 1 1 5 5 LYS HG2 H 1 1.536 0.005 . . . . . . 5 LYS HG2 . 18649 1 37 . 1 1 5 5 LYS HG3 H 1 1.455 0.010 . . . . . . 5 LYS HG3 . 18649 1 38 . 1 1 5 5 LYS HD2 H 1 1.714 0.002 . . . . . . 5 LYS QD . 18649 1 39 . 1 1 5 5 LYS HD3 H 1 1.714 0.002 . . . . . . 5 LYS QD . 18649 1 40 . 1 1 5 5 LYS HE2 H 1 2.977 0.009 . . . . . . 5 LYS QE . 18649 1 41 . 1 1 5 5 LYS HE3 H 1 2.977 0.009 . . . . . . 5 LYS QE . 18649 1 42 . 1 1 5 5 LYS C C 13 177.954 0.000 . . . . . . 5 LYS C . 18649 1 43 . 1 1 5 5 LYS CA C 13 59.110 0.083 . . . . . . 5 LYS CA . 18649 1 44 . 1 1 5 5 LYS CB C 13 32.523 0.069 . . . . . . 5 LYS CB . 18649 1 45 . 1 1 5 5 LYS CG C 13 25.296 0.051 . . . . . . 5 LYS CG . 18649 1 46 . 1 1 5 5 LYS CD C 13 28.758 0.087 . . . . . . 5 LYS CD . 18649 1 47 . 1 1 5 5 LYS CE C 13 41.803 0.159 . . . . . . 5 LYS CE . 18649 1 48 . 1 1 5 5 LYS N N 15 122.959 0.067 . . . . . . 5 LYS N . 18649 1 49 . 1 1 6 6 GLY H H 1 8.814 0.007 . . . . . . 6 GLY H . 18649 1 50 . 1 1 6 6 GLY HA2 H 1 3.892 0.006 . . . . . . 6 GLY HA2 . 18649 1 51 . 1 1 6 6 GLY HA3 H 1 3.749 0.003 . . . . . . 6 GLY HA3 . 18649 1 52 . 1 1 6 6 GLY C C 13 174.922 0.000 . . . . . . 6 GLY C . 18649 1 53 . 1 1 6 6 GLY CA C 13 47.025 0.110 . . . . . . 6 GLY CA . 18649 1 54 . 1 1 6 6 GLY N N 15 108.626 0.037 . . . . . . 6 GLY N . 18649 1 55 . 1 1 7 7 ALA H H 1 7.724 0.019 . . . . . . 7 ALA H . 18649 1 56 . 1 1 7 7 ALA HA H 1 4.136 0.006 . . . . . . 7 ALA HA . 18649 1 57 . 1 1 7 7 ALA HB1 H 1 1.524 0.022 . . . . . . 7 ALA QB . 18649 1 58 . 1 1 7 7 ALA HB2 H 1 1.524 0.022 . . . . . . 7 ALA QB . 18649 1 59 . 1 1 7 7 ALA HB3 H 1 1.524 0.022 . . . . . . 7 ALA QB . 18649 1 60 . 1 1 7 7 ALA C C 13 178.490 0.000 . . . . . . 7 ALA C . 18649 1 61 . 1 1 7 7 ALA CA C 13 54.643 0.126 . . . . . . 7 ALA CA . 18649 1 62 . 1 1 7 7 ALA CB C 13 18.743 0.098 . . . . . . 7 ALA CB . 18649 1 63 . 1 1 7 7 ALA N N 15 124.659 0.062 . . . . . . 7 ALA N . 18649 1 64 . 1 1 8 8 ILE H H 1 7.778 0.004 . . . . . . 8 ILE H . 18649 1 65 . 1 1 8 8 ILE HA H 1 3.756 0.006 . . . . . . 8 ILE HA . 18649 1 66 . 1 1 8 8 ILE HB H 1 2.062 0.009 . . . . . . 8 ILE HB . 18649 1 67 . 1 1 8 8 ILE HG12 H 1 1.733 0.005 . . . . . . 8 ILE HG12 . 18649 1 68 . 1 1 8 8 ILE HG13 H 1 1.192 0.008 . . . . . . 8 ILE HG13 . 18649 1 69 . 1 1 8 8 ILE HG21 H 1 0.971 0.010 . . . . . . 8 ILE QG2 . 18649 1 70 . 1 1 8 8 ILE HG22 H 1 0.971 0.010 . . . . . . 8 ILE QG2 . 18649 1 71 . 1 1 8 8 ILE HG23 H 1 0.971 0.010 . . . . . . 8 ILE QG2 . 18649 1 72 . 1 1 8 8 ILE HD11 H 1 0.898 0.004 . . . . . . 8 ILE QD1 . 18649 1 73 . 1 1 8 8 ILE HD12 H 1 0.898 0.004 . . . . . . 8 ILE QD1 . 18649 1 74 . 1 1 8 8 ILE HD13 H 1 0.898 0.004 . . . . . . 8 ILE QD1 . 18649 1 75 . 1 1 8 8 ILE C C 13 177.438 0.000 . . . . . . 8 ILE C . 18649 1 76 . 1 1 8 8 ILE CA C 13 64.505 0.115 . . . . . . 8 ILE CA . 18649 1 77 . 1 1 8 8 ILE CB C 13 37.502 0.065 . . . . . . 8 ILE CB . 18649 1 78 . 1 1 8 8 ILE CG1 C 13 29.109 0.151 . . . . . . 8 ILE CG1 . 18649 1 79 . 1 1 8 8 ILE CG2 C 13 17.756 0.122 . . . . . . 8 ILE CG2 . 18649 1 80 . 1 1 8 8 ILE CD1 C 13 12.990 0.112 . . . . . . 8 ILE CD1 . 18649 1 81 . 1 1 8 8 ILE N N 15 119.276 0.040 . . . . . . 8 ILE N . 18649 1 82 . 1 1 9 9 ILE H H 1 8.093 0.004 . . . . . . 9 ILE H . 18649 1 83 . 1 1 9 9 ILE HA H 1 3.731 0.009 . . . . . . 9 ILE HA . 18649 1 84 . 1 1 9 9 ILE HB H 1 1.990 0.009 . . . . . . 9 ILE HB . 18649 1 85 . 1 1 9 9 ILE HG12 H 1 1.811 0.006 . . . . . . 9 ILE HG12 . 18649 1 86 . 1 1 9 9 ILE HG13 H 1 1.171 0.005 . . . . . . 9 ILE HG13 . 18649 1 87 . 1 1 9 9 ILE HG21 H 1 0.916 0.012 . . . . . . 9 ILE QG2 . 18649 1 88 . 1 1 9 9 ILE HG22 H 1 0.916 0.012 . . . . . . 9 ILE QG2 . 18649 1 89 . 1 1 9 9 ILE HG23 H 1 0.916 0.012 . . . . . . 9 ILE QG2 . 18649 1 90 . 1 1 9 9 ILE HD11 H 1 0.874 0.006 . . . . . . 9 ILE QD1 . 18649 1 91 . 1 1 9 9 ILE HD12 H 1 0.874 0.006 . . . . . . 9 ILE QD1 . 18649 1 92 . 1 1 9 9 ILE HD13 H 1 0.874 0.006 . . . . . . 9 ILE QD1 . 18649 1 93 . 1 1 9 9 ILE C C 13 177.757 0.000 . . . . . . 9 ILE C . 18649 1 94 . 1 1 9 9 ILE CA C 13 64.941 0.103 . . . . . . 9 ILE CA . 18649 1 95 . 1 1 9 9 ILE CB C 13 37.331 0.091 . . . . . . 9 ILE CB . 18649 1 96 . 1 1 9 9 ILE CG1 C 13 29.238 0.033 . . . . . . 9 ILE CG1 . 18649 1 97 . 1 1 9 9 ILE CG2 C 13 17.709 0.101 . . . . . . 9 ILE CG2 . 18649 1 98 . 1 1 9 9 ILE CD1 C 13 13.127 0.092 . . . . . . 9 ILE CD1 . 18649 1 99 . 1 1 9 9 ILE N N 15 121.516 0.060 . . . . . . 9 ILE N . 18649 1 100 . 1 1 10 10 GLY H H 1 8.350 0.011 . . . . . . 10 GLY H . 18649 1 101 . 1 1 10 10 GLY HA2 H 1 3.656 0.005 . . . . . . 10 GLY QA . 18649 1 102 . 1 1 10 10 GLY HA3 H 1 3.656 0.005 . . . . . . 10 GLY QA . 18649 1 103 . 1 1 10 10 GLY C C 13 174.618 0.000 . . . . . . 10 GLY C . 18649 1 104 . 1 1 10 10 GLY CA C 13 47.744 0.074 . . . . . . 10 GLY CA . 18649 1 105 . 1 1 10 10 GLY N N 15 108.932 0.139 . . . . . . 10 GLY N . 18649 1 106 . 1 1 11 11 LEU H H 1 8.223 0.008 . . . . . . 11 LEU H . 18649 1 107 . 1 1 11 11 LEU HA H 1 4.044 0.005 . . . . . . 11 LEU HA . 18649 1 108 . 1 1 11 11 LEU HB2 H 1 1.964 0.007 . . . . . . 11 LEU HB2 . 18649 1 109 . 1 1 11 11 LEU HB3 H 1 1.575 0.002 . . . . . . 11 LEU HB3 . 18649 1 110 . 1 1 11 11 LEU HG H 1 1.884 0.008 . . . . . . 11 LEU HG . 18649 1 111 . 1 1 11 11 LEU HD11 H 1 0.918 0.008 . . . . . . 11 LEU QD1 . 18649 1 112 . 1 1 11 11 LEU HD12 H 1 0.918 0.008 . . . . . . 11 LEU QD1 . 18649 1 113 . 1 1 11 11 LEU HD13 H 1 0.918 0.008 . . . . . . 11 LEU QD1 . 18649 1 114 . 1 1 11 11 LEU HD21 H 1 0.882 0.013 . . . . . . 11 LEU QD2 . 18649 1 115 . 1 1 11 11 LEU HD22 H 1 0.882 0.013 . . . . . . 11 LEU QD2 . 18649 1 116 . 1 1 11 11 LEU HD23 H 1 0.882 0.013 . . . . . . 11 LEU QD2 . 18649 1 117 . 1 1 11 11 LEU C C 13 178.368 0.000 . . . . . . 11 LEU C . 18649 1 118 . 1 1 11 11 LEU CA C 13 58.186 0.123 . . . . . . 11 LEU CA . 18649 1 119 . 1 1 11 11 LEU CB C 13 41.985 0.125 . . . . . . 11 LEU CB . 18649 1 120 . 1 1 11 11 LEU CG C 13 26.887 0.121 . . . . . . 11 LEU CG . 18649 1 121 . 1 1 11 11 LEU CD1 C 13 25.252 0.205 . . . . . . 11 LEU CD1 . 18649 1 122 . 1 1 11 11 LEU CD2 C 13 24.413 0.165 . . . . . . 11 LEU CD2 . 18649 1 123 . 1 1 11 11 LEU N N 15 123.445 0.077 . . . . . . 11 LEU N . 18649 1 124 . 1 1 12 12 MET H H 1 8.147 0.005 . . . . . . 12 MET H . 18649 1 125 . 1 1 12 12 MET HA H 1 4.064 0.013 . . . . . . 12 MET HA . 18649 1 126 . 1 1 12 12 MET HB2 H 1 2.336 0.006 . . . . . . 12 MET HB2 . 18649 1 127 . 1 1 12 12 MET HB3 H 1 2.050 0.006 . . . . . . 12 MET HB3 . 18649 1 128 . 1 1 12 12 MET HG2 H 1 2.807 0.007 . . . . . . 12 MET HG2 . 18649 1 129 . 1 1 12 12 MET HG3 H 1 2.403 0.006 . . . . . . 12 MET HG3 . 18649 1 130 . 1 1 12 12 MET HE1 H 1 1.944 0.011 . . . . . . 12 MET QE . 18649 1 131 . 1 1 12 12 MET HE2 H 1 1.944 0.011 . . . . . . 12 MET QE . 18649 1 132 . 1 1 12 12 MET HE3 H 1 1.944 0.011 . . . . . . 12 MET QE . 18649 1 133 . 1 1 12 12 MET C C 13 177.568 0.000 . . . . . . 12 MET C . 18649 1 134 . 1 1 12 12 MET CA C 13 59.321 0.072 . . . . . . 12 MET CA . 18649 1 135 . 1 1 12 12 MET CB C 13 32.672 0.169 . . . . . . 12 MET CB . 18649 1 136 . 1 1 12 12 MET CG C 13 32.994 0.050 . . . . . . 12 MET CG . 18649 1 137 . 1 1 12 12 MET CE C 13 17.262 0.100 . . . . . . 12 MET CE . 18649 1 138 . 1 1 12 12 MET N N 15 119.782 0.158 . . . . . . 12 MET N . 18649 1 139 . 1 1 13 13 VAL H H 1 8.544 0.003 . . . . . . 13 VAL H . 18649 1 140 . 1 1 13 13 VAL HA H 1 3.484 0.007 . . . . . . 13 VAL HA . 18649 1 141 . 1 1 13 13 VAL HB H 1 2.192 0.008 . . . . . . 13 VAL HB . 18649 1 142 . 1 1 13 13 VAL HG11 H 1 0.867 0.005 . . . . . . 13 VAL QG1 . 18649 1 143 . 1 1 13 13 VAL HG12 H 1 0.867 0.005 . . . . . . 13 VAL QG1 . 18649 1 144 . 1 1 13 13 VAL HG13 H 1 0.867 0.005 . . . . . . 13 VAL QG1 . 18649 1 145 . 1 1 13 13 VAL HG21 H 1 1.048 0.012 . . . . . . 13 VAL QG2 . 18649 1 146 . 1 1 13 13 VAL HG22 H 1 1.048 0.012 . . . . . . 13 VAL QG2 . 18649 1 147 . 1 1 13 13 VAL HG23 H 1 1.048 0.012 . . . . . . 13 VAL QG2 . 18649 1 148 . 1 1 13 13 VAL C C 13 177.871 0.000 . . . . . . 13 VAL C . 18649 1 149 . 1 1 13 13 VAL CA C 13 67.099 0.135 . . . . . . 13 VAL CA . 18649 1 150 . 1 1 13 13 VAL CB C 13 31.312 0.091 . . . . . . 13 VAL CB . 18649 1 151 . 1 1 13 13 VAL CG1 C 13 21.292 0.116 . . . . . . 13 VAL CG1 . 18649 1 152 . 1 1 13 13 VAL CG2 C 13 23.171 0.079 . . . . . . 13 VAL CG2 . 18649 1 153 . 1 1 13 13 VAL N N 15 120.255 0.081 . . . . . . 13 VAL N . 18649 1 154 . 1 1 14 14 GLY H H 1 8.672 0.006 . . . . . . 14 GLY H . 18649 1 155 . 1 1 14 14 GLY HA2 H 1 3.560 0.007 . . . . . . 14 GLY QA . 18649 1 156 . 1 1 14 14 GLY HA3 H 1 3.560 0.007 . . . . . . 14 GLY QA . 18649 1 157 . 1 1 14 14 GLY C C 13 174.850 0.000 . . . . . . 14 GLY C . 18649 1 158 . 1 1 14 14 GLY CA C 13 47.434 0.087 . . . . . . 14 GLY CA . 18649 1 159 . 1 1 14 14 GLY N N 15 108.612 0.051 . . . . . . 14 GLY N . 18649 1 160 . 1 1 15 15 GLY H H 1 8.693 0.002 . . . . . . 15 GLY H . 18649 1 161 . 1 1 15 15 GLY HA2 H 1 3.647 0.009 . . . . . . 15 GLY HA2 . 18649 1 162 . 1 1 15 15 GLY HA3 H 1 3.591 0.003 . . . . . . 15 GLY HA3 . 18649 1 163 . 1 1 15 15 GLY C C 13 174.325 0.000 . . . . . . 15 GLY C . 18649 1 164 . 1 1 15 15 GLY CA C 13 47.400 0.069 . . . . . . 15 GLY CA . 18649 1 165 . 1 1 15 15 GLY N N 15 110.823 0.040 . . . . . . 15 GLY N . 18649 1 166 . 1 1 16 16 VAL H H 1 8.155 0.005 . . . . . . 16 VAL H . 18649 1 167 . 1 1 16 16 VAL HA H 1 3.592 0.009 . . . . . . 16 VAL HA . 18649 1 168 . 1 1 16 16 VAL HB H 1 2.282 0.003 . . . . . . 16 VAL HB . 18649 1 169 . 1 1 16 16 VAL HG11 H 1 0.876 0.006 . . . . . . 16 VAL QG1 . 18649 1 170 . 1 1 16 16 VAL HG12 H 1 0.876 0.006 . . . . . . 16 VAL QG1 . 18649 1 171 . 1 1 16 16 VAL HG13 H 1 0.876 0.006 . . . . . . 16 VAL QG1 . 18649 1 172 . 1 1 16 16 VAL HG21 H 1 1.057 0.012 . . . . . . 16 VAL QG2 . 18649 1 173 . 1 1 16 16 VAL HG22 H 1 1.057 0.012 . . . . . . 16 VAL QG2 . 18649 1 174 . 1 1 16 16 VAL HG23 H 1 1.057 0.012 . . . . . . 16 VAL QG2 . 18649 1 175 . 1 1 16 16 VAL C C 13 178.881 0.000 . . . . . . 16 VAL C . 18649 1 176 . 1 1 16 16 VAL CA C 13 66.989 0.113 . . . . . . 16 VAL CA . 18649 1 177 . 1 1 16 16 VAL CB C 13 31.209 0.069 . . . . . . 16 VAL CB . 18649 1 178 . 1 1 16 16 VAL CG1 C 13 21.126 0.131 . . . . . . 16 VAL CG1 . 18649 1 179 . 1 1 16 16 VAL CG2 C 13 23.383 0.144 . . . . . . 16 VAL CG2 . 18649 1 180 . 1 1 16 16 VAL N N 15 123.298 0.091 . . . . . . 16 VAL N . 18649 1 181 . 1 1 17 17 VAL H H 1 8.466 0.006 . . . . . . 17 VAL H . 18649 1 182 . 1 1 17 17 VAL HA H 1 3.463 0.009 . . . . . . 17 VAL HA . 18649 1 183 . 1 1 17 17 VAL HB H 1 2.272 0.003 . . . . . . 17 VAL HB . 18649 1 184 . 1 1 17 17 VAL HG11 H 1 0.829 0.014 . . . . . . 17 VAL QG1 . 18649 1 185 . 1 1 17 17 VAL HG12 H 1 0.829 0.014 . . . . . . 17 VAL QG1 . 18649 1 186 . 1 1 17 17 VAL HG13 H 1 0.829 0.014 . . . . . . 17 VAL QG1 . 18649 1 187 . 1 1 17 17 VAL HG21 H 1 0.999 0.012 . . . . . . 17 VAL QG2 . 18649 1 188 . 1 1 17 17 VAL HG22 H 1 0.999 0.012 . . . . . . 17 VAL QG2 . 18649 1 189 . 1 1 17 17 VAL HG23 H 1 0.999 0.012 . . . . . . 17 VAL QG2 . 18649 1 190 . 1 1 17 17 VAL C C 13 177.136 0.000 . . . . . . 17 VAL C . 18649 1 191 . 1 1 17 17 VAL CA C 13 67.737 0.123 . . . . . . 17 VAL CA . 18649 1 192 . 1 1 17 17 VAL CB C 13 30.990 0.159 . . . . . . 17 VAL CB . 18649 1 193 . 1 1 17 17 VAL CG1 C 13 21.146 0.109 . . . . . . 17 VAL CG1 . 18649 1 194 . 1 1 17 17 VAL CG2 C 13 23.009 0.152 . . . . . . 17 VAL CG2 . 18649 1 195 . 1 1 17 17 VAL N N 15 124.816 0.076 . . . . . . 17 VAL N . 18649 1 196 . 1 1 18 18 ILE H H 1 8.413 0.005 . . . . . . 18 ILE H . 18649 1 197 . 1 1 18 18 ILE HA H 1 3.553 0.004 . . . . . . 18 ILE HA . 18649 1 198 . 1 1 18 18 ILE HB H 1 1.942 0.005 . . . . . . 18 ILE HB . 18649 1 199 . 1 1 18 18 ILE HG12 H 1 1.749 0.006 . . . . . . 18 ILE HG12 . 18649 1 200 . 1 1 18 18 ILE HG13 H 1 1.081 0.008 . . . . . . 18 ILE HG13 . 18649 1 201 . 1 1 18 18 ILE HG21 H 1 0.845 0.009 . . . . . . 18 ILE QG2 . 18649 1 202 . 1 1 18 18 ILE HG22 H 1 0.845 0.009 . . . . . . 18 ILE QG2 . 18649 1 203 . 1 1 18 18 ILE HG23 H 1 0.845 0.009 . . . . . . 18 ILE QG2 . 18649 1 204 . 1 1 18 18 ILE HD11 H 1 0.744 0.008 . . . . . . 18 ILE QD1 . 18649 1 205 . 1 1 18 18 ILE HD12 H 1 0.744 0.008 . . . . . . 18 ILE QD1 . 18649 1 206 . 1 1 18 18 ILE HD13 H 1 0.744 0.008 . . . . . . 18 ILE QD1 . 18649 1 207 . 1 1 18 18 ILE C C 13 177.287 0.000 . . . . . . 18 ILE C . 18649 1 208 . 1 1 18 18 ILE CA C 13 65.346 0.111 . . . . . . 18 ILE CA . 18649 1 209 . 1 1 18 18 ILE CB C 13 37.535 0.113 . . . . . . 18 ILE CB . 18649 1 210 . 1 1 18 18 ILE CG1 C 13 29.262 0.121 . . . . . . 18 ILE CG1 . 18649 1 211 . 1 1 18 18 ILE CG2 C 13 17.228 0.136 . . . . . . 18 ILE CG2 . 18649 1 212 . 1 1 18 18 ILE CD1 C 13 12.464 0.129 . . . . . . 18 ILE CD1 . 18649 1 213 . 1 1 18 18 ILE N N 15 121.213 0.070 . . . . . . 18 ILE N . 18649 1 214 . 1 1 19 19 ALA H H 1 8.532 0.003 . . . . . . 19 ALA H . 18649 1 215 . 1 1 19 19 ALA HA H 1 3.870 0.013 . . . . . . 19 ALA HA . 18649 1 216 . 1 1 19 19 ALA HB1 H 1 1.416 0.013 . . . . . . 19 ALA QB . 18649 1 217 . 1 1 19 19 ALA HB2 H 1 1.416 0.013 . . . . . . 19 ALA QB . 18649 1 218 . 1 1 19 19 ALA HB3 H 1 1.416 0.013 . . . . . . 19 ALA QB . 18649 1 219 . 1 1 19 19 ALA C C 13 178.529 0.000 . . . . . . 19 ALA C . 18649 1 220 . 1 1 19 19 ALA CA C 13 55.756 0.132 . . . . . . 19 ALA CA . 18649 1 221 . 1 1 19 19 ALA CB C 13 17.990 0.192 . . . . . . 19 ALA CB . 18649 1 222 . 1 1 19 19 ALA N N 15 123.108 0.077 . . . . . . 19 ALA N . 18649 1 223 . 1 1 20 20 THR H H 1 8.117 0.009 . . . . . . 20 THR H . 18649 1 224 . 1 1 20 20 THR HA H 1 3.663 0.006 . . . . . . 20 THR HA . 18649 1 225 . 1 1 20 20 THR HB H 1 4.314 0.005 . . . . . . 20 THR HB . 18649 1 226 . 1 1 20 20 THR HG21 H 1 1.099 0.005 . . . . . . 20 THR QG2 . 18649 1 227 . 1 1 20 20 THR HG22 H 1 1.099 0.005 . . . . . . 20 THR QG2 . 18649 1 228 . 1 1 20 20 THR HG23 H 1 1.099 0.005 . . . . . . 20 THR QG2 . 18649 1 229 . 1 1 20 20 THR C C 13 176.162 0.000 . . . . . . 20 THR C . 18649 1 230 . 1 1 20 20 THR CA C 13 68.387 0.091 . . . . . . 20 THR CA . 18649 1 231 . 1 1 20 20 THR CB C 13 67.691 0.094 . . . . . . 20 THR CB . 18649 1 232 . 1 1 20 20 THR CG2 C 13 21.210 0.104 . . . . . . 20 THR CG2 . 18649 1 233 . 1 1 20 20 THR N N 15 116.561 0.079 . . . . . . 20 THR N . 18649 1 234 . 1 1 21 21 VAL H H 1 8.206 0.003 . . . . . . 21 VAL H . 18649 1 235 . 1 1 21 21 VAL HA H 1 3.517 0.007 . . . . . . 21 VAL HA . 18649 1 236 . 1 1 21 21 VAL HB H 1 2.275 0.003 . . . . . . 21 VAL HB . 18649 1 237 . 1 1 21 21 VAL HG11 H 1 0.867 0.003 . . . . . . 21 VAL QG1 . 18649 1 238 . 1 1 21 21 VAL HG12 H 1 0.867 0.003 . . . . . . 21 VAL QG1 . 18649 1 239 . 1 1 21 21 VAL HG13 H 1 0.867 0.003 . . . . . . 21 VAL QG1 . 18649 1 240 . 1 1 21 21 VAL HG21 H 1 1.023 0.012 . . . . . . 21 VAL QG2 . 18649 1 241 . 1 1 21 21 VAL HG22 H 1 1.023 0.012 . . . . . . 21 VAL QG2 . 18649 1 242 . 1 1 21 21 VAL HG23 H 1 1.023 0.012 . . . . . . 21 VAL QG2 . 18649 1 243 . 1 1 21 21 VAL C C 13 178.929 0.000 . . . . . . 21 VAL C . 18649 1 244 . 1 1 21 21 VAL CA C 13 67.390 0.182 . . . . . . 21 VAL CA . 18649 1 245 . 1 1 21 21 VAL CB C 13 31.145 0.086 . . . . . . 21 VAL CB . 18649 1 246 . 1 1 21 21 VAL CG1 C 13 21.338 0.155 . . . . . . 21 VAL CG1 . 18649 1 247 . 1 1 21 21 VAL CG2 C 13 22.977 0.142 . . . . . . 21 VAL CG2 . 18649 1 248 . 1 1 21 21 VAL N N 15 122.793 0.081 . . . . . . 21 VAL N . 18649 1 249 . 1 1 22 22 ILE H H 1 8.402 0.004 . . . . . . 22 ILE H . 18649 1 250 . 1 1 22 22 ILE HA H 1 3.548 0.008 . . . . . . 22 ILE HA . 18649 1 251 . 1 1 22 22 ILE HB H 1 2.099 0.004 . . . . . . 22 ILE HB . 18649 1 252 . 1 1 22 22 ILE HG12 H 1 1.919 0.006 . . . . . . 22 ILE HG12 . 18649 1 253 . 1 1 22 22 ILE HG13 H 1 0.972 0.005 . . . . . . 22 ILE HG13 . 18649 1 254 . 1 1 22 22 ILE HG21 H 1 0.857 0.008 . . . . . . 22 ILE QG2 . 18649 1 255 . 1 1 22 22 ILE HG22 H 1 0.857 0.008 . . . . . . 22 ILE QG2 . 18649 1 256 . 1 1 22 22 ILE HG23 H 1 0.857 0.008 . . . . . . 22 ILE QG2 . 18649 1 257 . 1 1 22 22 ILE HD11 H 1 0.775 0.006 . . . . . . 22 ILE QD1 . 18649 1 258 . 1 1 22 22 ILE HD12 H 1 0.775 0.006 . . . . . . 22 ILE QD1 . 18649 1 259 . 1 1 22 22 ILE HD13 H 1 0.775 0.006 . . . . . . 22 ILE QD1 . 18649 1 260 . 1 1 22 22 ILE C C 13 176.916 0.000 . . . . . . 22 ILE C . 18649 1 261 . 1 1 22 22 ILE CA C 13 66.387 0.125 . . . . . . 22 ILE CA . 18649 1 262 . 1 1 22 22 ILE CB C 13 37.297 0.066 . . . . . . 22 ILE CB . 18649 1 263 . 1 1 22 22 ILE CG1 C 13 29.301 0.074 . . . . . . 22 ILE CG1 . 18649 1 264 . 1 1 22 22 ILE CG2 C 13 17.095 0.057 . . . . . . 22 ILE CG2 . 18649 1 265 . 1 1 22 22 ILE CD1 C 13 13.607 0.103 . . . . . . 22 ILE CD1 . 18649 1 266 . 1 1 22 22 ILE N N 15 124.529 0.066 . . . . . . 22 ILE N . 18649 1 267 . 1 1 23 23 VAL H H 1 8.420 0.003 . . . . . . 23 VAL H . 18649 1 268 . 1 1 23 23 VAL HA H 1 3.539 0.009 . . . . . . 23 VAL HA . 18649 1 269 . 1 1 23 23 VAL HB H 1 2.261 0.007 . . . . . . 23 VAL HB . 18649 1 270 . 1 1 23 23 VAL HG11 H 1 0.937 0.009 . . . . . . 23 VAL QG1 . 18649 1 271 . 1 1 23 23 VAL HG12 H 1 0.937 0.009 . . . . . . 23 VAL QG1 . 18649 1 272 . 1 1 23 23 VAL HG13 H 1 0.937 0.009 . . . . . . 23 VAL QG1 . 18649 1 273 . 1 1 23 23 VAL HG21 H 1 1.088 0.009 . . . . . . 23 VAL QG2 . 18649 1 274 . 1 1 23 23 VAL HG22 H 1 1.088 0.009 . . . . . . 23 VAL QG2 . 18649 1 275 . 1 1 23 23 VAL HG23 H 1 1.088 0.009 . . . . . . 23 VAL QG2 . 18649 1 276 . 1 1 23 23 VAL C C 13 177.502 0.000 . . . . . . 23 VAL C . 18649 1 277 . 1 1 23 23 VAL CA C 13 68.050 0.103 . . . . . . 23 VAL CA . 18649 1 278 . 1 1 23 23 VAL CB C 13 31.248 0.047 . . . . . . 23 VAL CB . 18649 1 279 . 1 1 23 23 VAL CG1 C 13 21.708 0.108 . . . . . . 23 VAL CG1 . 18649 1 280 . 1 1 23 23 VAL CG2 C 13 23.427 0.099 . . . . . . 23 VAL CG2 . 18649 1 281 . 1 1 23 23 VAL N N 15 121.558 0.054 . . . . . . 23 VAL N . 18649 1 282 . 1 1 24 24 ILE H H 1 8.570 0.005 . . . . . . 24 ILE H . 18649 1 283 . 1 1 24 24 ILE HA H 1 3.572 0.004 . . . . . . 24 ILE HA . 18649 1 284 . 1 1 24 24 ILE HB H 1 1.927 0.002 . . . . . . 24 ILE HB . 18649 1 285 . 1 1 24 24 ILE HG12 H 1 1.927 0.006 . . . . . . 24 ILE HG12 . 18649 1 286 . 1 1 24 24 ILE HG13 H 1 1.102 0.005 . . . . . . 24 ILE HG13 . 18649 1 287 . 1 1 24 24 ILE HG21 H 1 0.916 0.015 . . . . . . 24 ILE QG2 . 18649 1 288 . 1 1 24 24 ILE HG22 H 1 0.916 0.015 . . . . . . 24 ILE QG2 . 18649 1 289 . 1 1 24 24 ILE HG23 H 1 0.916 0.015 . . . . . . 24 ILE QG2 . 18649 1 290 . 1 1 24 24 ILE HD11 H 1 0.815 0.005 . . . . . . 24 ILE QD1 . 18649 1 291 . 1 1 24 24 ILE HD12 H 1 0.815 0.005 . . . . . . 24 ILE QD1 . 18649 1 292 . 1 1 24 24 ILE HD13 H 1 0.815 0.005 . . . . . . 24 ILE QD1 . 18649 1 293 . 1 1 24 24 ILE C C 13 177.511 0.000 . . . . . . 24 ILE C . 18649 1 294 . 1 1 24 24 ILE CA C 13 65.830 0.100 . . . . . . 24 ILE CA . 18649 1 295 . 1 1 24 24 ILE CB C 13 37.270 0.057 . . . . . . 24 ILE CB . 18649 1 296 . 1 1 24 24 ILE CG1 C 13 29.288 0.138 . . . . . . 24 ILE CG1 . 18649 1 297 . 1 1 24 24 ILE CG2 C 13 17.495 0.165 . . . . . . 24 ILE CG2 . 18649 1 298 . 1 1 24 24 ILE CD1 C 13 13.677 0.101 . . . . . . 24 ILE CD1 . 18649 1 299 . 1 1 24 24 ILE N N 15 120.299 0.078 . . . . . . 24 ILE N . 18649 1 300 . 1 1 25 25 THR H H 1 8.137 0.004 . . . . . . 25 THR H . 18649 1 301 . 1 1 25 25 THR HA H 1 3.690 0.008 . . . . . . 25 THR HA . 18649 1 302 . 1 1 25 25 THR HB H 1 4.319 0.007 . . . . . . 25 THR HB . 18649 1 303 . 1 1 25 25 THR HG21 H 1 1.139 0.007 . . . . . . 25 THR QG2 . 18649 1 304 . 1 1 25 25 THR HG22 H 1 1.139 0.007 . . . . . . 25 THR QG2 . 18649 1 305 . 1 1 25 25 THR HG23 H 1 1.139 0.007 . . . . . . 25 THR QG2 . 18649 1 306 . 1 1 25 25 THR C C 13 176.067 0.000 . . . . . . 25 THR C . 18649 1 307 . 1 1 25 25 THR CA C 13 68.555 0.088 . . . . . . 25 THR CA . 18649 1 308 . 1 1 25 25 THR CB C 13 67.575 0.120 . . . . . . 25 THR CB . 18649 1 309 . 1 1 25 25 THR CG2 C 13 21.513 0.169 . . . . . . 25 THR CG2 . 18649 1 310 . 1 1 25 25 THR N N 15 119.146 0.071 . . . . . . 25 THR N . 18649 1 311 . 1 1 26 26 LEU H H 1 8.309 0.004 . . . . . . 26 LEU H . 18649 1 312 . 1 1 26 26 LEU HA H 1 4.012 0.006 . . . . . . 26 LEU HA . 18649 1 313 . 1 1 26 26 LEU HB2 H 1 2.035 0.005 . . . . . . 26 LEU HB2 . 18649 1 314 . 1 1 26 26 LEU HB3 H 1 1.503 0.008 . . . . . . 26 LEU HB3 . 18649 1 315 . 1 1 26 26 LEU HG H 1 1.963 0.005 . . . . . . 26 LEU HG . 18649 1 316 . 1 1 26 26 LEU HD11 H 1 0.886 0.010 . . . . . . 26 LEU QD1 . 18649 1 317 . 1 1 26 26 LEU HD12 H 1 0.886 0.010 . . . . . . 26 LEU QD1 . 18649 1 318 . 1 1 26 26 LEU HD13 H 1 0.886 0.010 . . . . . . 26 LEU QD1 . 18649 1 319 . 1 1 26 26 LEU HD21 H 1 0.859 0.004 . . . . . . 26 LEU QD2 . 18649 1 320 . 1 1 26 26 LEU HD22 H 1 0.859 0.004 . . . . . . 26 LEU QD2 . 18649 1 321 . 1 1 26 26 LEU HD23 H 1 0.859 0.004 . . . . . . 26 LEU QD2 . 18649 1 322 . 1 1 26 26 LEU C C 13 179.051 0.000 . . . . . . 26 LEU C . 18649 1 323 . 1 1 26 26 LEU CA C 13 58.242 0.064 . . . . . . 26 LEU CA . 18649 1 324 . 1 1 26 26 LEU CB C 13 41.834 0.121 . . . . . . 26 LEU CB . 18649 1 325 . 1 1 26 26 LEU CG C 13 26.862 0.164 . . . . . . 26 LEU CG . 18649 1 326 . 1 1 26 26 LEU CD1 C 13 25.426 0.145 . . . . . . 26 LEU CD1 . 18649 1 327 . 1 1 26 26 LEU CD2 C 13 23.459 0.099 . . . . . . 26 LEU CD2 . 18649 1 328 . 1 1 26 26 LEU N N 15 122.563 0.062 . . . . . . 26 LEU N . 18649 1 329 . 1 1 27 27 VAL H H 1 8.330 0.003 . . . . . . 27 VAL H . 18649 1 330 . 1 1 27 27 VAL HA H 1 3.627 0.010 . . . . . . 27 VAL HA . 18649 1 331 . 1 1 27 27 VAL HB H 1 2.305 0.004 . . . . . . 27 VAL HB . 18649 1 332 . 1 1 27 27 VAL HG11 H 1 0.951 0.009 . . . . . . 27 VAL QG1 . 18649 1 333 . 1 1 27 27 VAL HG12 H 1 0.951 0.009 . . . . . . 27 VAL QG1 . 18649 1 334 . 1 1 27 27 VAL HG13 H 1 0.951 0.009 . . . . . . 27 VAL QG1 . 18649 1 335 . 1 1 27 27 VAL HG21 H 1 1.091 0.004 . . . . . . 27 VAL QG2 . 18649 1 336 . 1 1 27 27 VAL HG22 H 1 1.091 0.004 . . . . . . 27 VAL QG2 . 18649 1 337 . 1 1 27 27 VAL HG23 H 1 1.091 0.004 . . . . . . 27 VAL QG2 . 18649 1 338 . 1 1 27 27 VAL C C 13 178.222 0.000 . . . . . . 27 VAL C . 18649 1 339 . 1 1 27 27 VAL CA C 13 66.517 0.099 . . . . . . 27 VAL CA . 18649 1 340 . 1 1 27 27 VAL CB C 13 31.432 0.121 . . . . . . 27 VAL CB . 18649 1 341 . 1 1 27 27 VAL CG1 C 13 21.595 0.066 . . . . . . 27 VAL CG1 . 18649 1 342 . 1 1 27 27 VAL CG2 C 13 23.130 0.098 . . . . . . 27 VAL CG2 . 18649 1 343 . 1 1 27 27 VAL N N 15 120.127 0.108 . . . . . . 27 VAL N . 18649 1 344 . 1 1 28 28 MET H H 1 8.345 0.003 . . . . . . 28 MET H . 18649 1 345 . 1 1 28 28 MET HA H 1 4.273 0.006 . . . . . . 28 MET HA . 18649 1 346 . 1 1 28 28 MET HB2 H 1 2.329 0.008 . . . . . . 28 MET HB2 . 18649 1 347 . 1 1 28 28 MET HB3 H 1 2.071 0.008 . . . . . . 28 MET HB3 . 18649 1 348 . 1 1 28 28 MET HG2 H 1 2.711 0.005 . . . . . . 28 MET QG . 18649 1 349 . 1 1 28 28 MET HG3 H 1 2.711 0.005 . . . . . . 28 MET QG . 18649 1 350 . 1 1 28 28 MET HE1 H 1 2.087 0.009 . . . . . . 28 MET QE . 18649 1 351 . 1 1 28 28 MET HE2 H 1 2.087 0.009 . . . . . . 28 MET QE . 18649 1 352 . 1 1 28 28 MET HE3 H 1 2.087 0.009 . . . . . . 28 MET QE . 18649 1 353 . 1 1 28 28 MET C C 13 178.449 0.000 . . . . . . 28 MET C . 18649 1 354 . 1 1 28 28 MET CA C 13 57.703 0.110 . . . . . . 28 MET CA . 18649 1 355 . 1 1 28 28 MET CB C 13 32.033 0.088 . . . . . . 28 MET CB . 18649 1 356 . 1 1 28 28 MET CG C 13 32.993 0.054 . . . . . . 28 MET CG . 18649 1 357 . 1 1 28 28 MET CE C 13 17.274 0.203 . . . . . . 28 MET CE . 18649 1 358 . 1 1 28 28 MET N N 15 119.574 0.069 . . . . . . 28 MET N . 18649 1 359 . 1 1 29 29 LEU H H 1 8.187 0.004 . . . . . . 29 LEU H . 18649 1 360 . 1 1 29 29 LEU HA H 1 4.263 0.004 . . . . . . 29 LEU HA . 18649 1 361 . 1 1 29 29 LEU HB2 H 1 1.936 0.004 . . . . . . 29 LEU HB2 . 18649 1 362 . 1 1 29 29 LEU HB3 H 1 1.592 0.002 . . . . . . 29 LEU HB3 . 18649 1 363 . 1 1 29 29 LEU HG H 1 1.962 0.004 . . . . . . 29 LEU HG . 18649 1 364 . 1 1 29 29 LEU HD11 H 1 0.901 0.009 . . . . . . 29 LEU QD1 . 18649 1 365 . 1 1 29 29 LEU HD12 H 1 0.901 0.009 . . . . . . 29 LEU QD1 . 18649 1 366 . 1 1 29 29 LEU HD13 H 1 0.901 0.009 . . . . . . 29 LEU QD1 . 18649 1 367 . 1 1 29 29 LEU HD21 H 1 0.898 0.005 . . . . . . 29 LEU QD2 . 18649 1 368 . 1 1 29 29 LEU HD22 H 1 0.898 0.005 . . . . . . 29 LEU QD2 . 18649 1 369 . 1 1 29 29 LEU HD23 H 1 0.898 0.005 . . . . . . 29 LEU QD2 . 18649 1 370 . 1 1 29 29 LEU C C 13 178.103 0.000 . . . . . . 29 LEU C . 18649 1 371 . 1 1 29 29 LEU CA C 13 56.359 0.140 . . . . . . 29 LEU CA . 18649 1 372 . 1 1 29 29 LEU CB C 13 42.366 0.161 . . . . . . 29 LEU CB . 18649 1 373 . 1 1 29 29 LEU CG C 13 26.696 0.137 . . . . . . 29 LEU CG . 18649 1 374 . 1 1 29 29 LEU CD1 C 13 25.870 0.094 . . . . . . 29 LEU CD1 . 18649 1 375 . 1 1 29 29 LEU CD2 C 13 23.318 0.030 . . . . . . 29 LEU CD2 . 18649 1 376 . 1 1 29 29 LEU N N 15 120.131 0.064 . . . . . . 29 LEU N . 18649 1 377 . 1 1 30 30 LYS H H 1 7.760 0.004 . . . . . . 30 LYS H . 18649 1 378 . 1 1 30 30 LYS HA H 1 4.314 0.004 . . . . . . 30 LYS HA . 18649 1 379 . 1 1 30 30 LYS HB2 H 1 1.952 0.003 . . . . . . 30 LYS QB . 18649 1 380 . 1 1 30 30 LYS HB3 H 1 1.952 0.003 . . . . . . 30 LYS QB . 18649 1 381 . 1 1 30 30 LYS HG2 H 1 1.541 0.004 . . . . . . 30 LYS QG . 18649 1 382 . 1 1 30 30 LYS HG3 H 1 1.541 0.004 . . . . . . 30 LYS QG . 18649 1 383 . 1 1 30 30 LYS HD2 H 1 1.719 0.003 . . . . . . 30 LYS QD . 18649 1 384 . 1 1 30 30 LYS HD3 H 1 1.719 0.003 . . . . . . 30 LYS QD . 18649 1 385 . 1 1 30 30 LYS HE2 H 1 2.997 0.003 . . . . . . 30 LYS QE . 18649 1 386 . 1 1 30 30 LYS HE3 H 1 2.997 0.003 . . . . . . 30 LYS QE . 18649 1 387 . 1 1 30 30 LYS C C 13 176.630 0.000 . . . . . . 30 LYS C . 18649 1 388 . 1 1 30 30 LYS CA C 13 56.261 0.063 . . . . . . 30 LYS CA . 18649 1 389 . 1 1 30 30 LYS CB C 13 32.581 0.064 . . . . . . 30 LYS CB . 18649 1 390 . 1 1 30 30 LYS CG C 13 24.591 0.092 . . . . . . 30 LYS CG . 18649 1 391 . 1 1 30 30 LYS CD C 13 28.666 0.103 . . . . . . 30 LYS CD . 18649 1 392 . 1 1 30 30 LYS CE C 13 41.890 0.130 . . . . . . 30 LYS CE . 18649 1 393 . 1 1 30 30 LYS N N 15 120.359 0.082 . . . . . . 30 LYS N . 18649 1 394 . 1 1 31 31 LYS H H 1 7.916 0.005 . . . . . . 31 LYS H . 18649 1 395 . 1 1 31 31 LYS HA H 1 4.314 0.005 . . . . . . 31 LYS HA . 18649 1 396 . 1 1 31 31 LYS HB2 H 1 1.954 0.003 . . . . . . 31 LYS QB . 18649 1 397 . 1 1 31 31 LYS HB3 H 1 1.954 0.003 . . . . . . 31 LYS QB . 18649 1 398 . 1 1 31 31 LYS HG2 H 1 1.709 0.004 . . . . . . 31 LYS HG2 . 18649 1 399 . 1 1 31 31 LYS HG3 H 1 1.537 0.004 . . . . . . 31 LYS HG3 . 18649 1 400 . 1 1 31 31 LYS HD2 H 1 1.857 0.009 . . . . . . 31 LYS QD . 18649 1 401 . 1 1 31 31 LYS HD3 H 1 1.857 0.009 . . . . . . 31 LYS QD . 18649 1 402 . 1 1 31 31 LYS HE2 H 1 2.984 0.008 . . . . . . 31 LYS QE . 18649 1 403 . 1 1 31 31 LYS HE3 H 1 2.984 0.008 . . . . . . 31 LYS QE . 18649 1 404 . 1 1 31 31 LYS C C 13 175.436 0.000 . . . . . . 31 LYS C . 18649 1 405 . 1 1 31 31 LYS CA C 13 56.486 0.123 . . . . . . 31 LYS CA . 18649 1 406 . 1 1 31 31 LYS CB C 13 32.701 0.077 . . . . . . 31 LYS CB . 18649 1 407 . 1 1 31 31 LYS CG C 13 24.624 0.144 . . . . . . 31 LYS CG . 18649 1 408 . 1 1 31 31 LYS CD C 13 29.017 0.178 . . . . . . 31 LYS CD . 18649 1 409 . 1 1 31 31 LYS CE C 13 41.881 0.151 . . . . . . 31 LYS CE . 18649 1 410 . 1 1 31 31 LYS N N 15 123.768 0.093 . . . . . . 31 LYS N . 18649 1 411 . 1 1 32 32 LYS H H 1 7.762 0.016 . . . . . . 32 LYS H . 18649 1 412 . 1 1 32 32 LYS HA H 1 4.138 0.004 . . . . . . 32 LYS HA . 18649 1 413 . 1 1 32 32 LYS HB2 H 1 1.843 0.003 . . . . . . 32 LYS HB2 . 18649 1 414 . 1 1 32 32 LYS HB3 H 1 1.758 0.004 . . . . . . 32 LYS HB3 . 18649 1 415 . 1 1 32 32 LYS HG2 H 1 1.463 0.004 . . . . . . 32 LYS QG . 18649 1 416 . 1 1 32 32 LYS HG3 H 1 1.463 0.004 . . . . . . 32 LYS QG . 18649 1 417 . 1 1 32 32 LYS HD2 H 1 1.709 0.004 . . . . . . 32 LYS QD . 18649 1 418 . 1 1 32 32 LYS HD3 H 1 1.709 0.004 . . . . . . 32 LYS QD . 18649 1 419 . 1 1 32 32 LYS HE2 H 1 3.016 0.003 . . . . . . 32 LYS QE . 18649 1 420 . 1 1 32 32 LYS HE3 H 1 3.016 0.003 . . . . . . 32 LYS QE . 18649 1 421 . 1 1 32 32 LYS CA C 13 57.704 0.102 . . . . . . 32 LYS CA . 18649 1 422 . 1 1 32 32 LYS CB C 13 33.554 0.097 . . . . . . 32 LYS CB . 18649 1 423 . 1 1 32 32 LYS CG C 13 24.688 0.055 . . . . . . 32 LYS CG . 18649 1 424 . 1 1 32 32 LYS CD C 13 28.864 0.089 . . . . . . 32 LYS CD . 18649 1 425 . 1 1 32 32 LYS CE C 13 42.109 0.086 . . . . . . 32 LYS CE . 18649 1 426 . 1 1 32 32 LYS N N 15 129.909 0.069 . . . . . . 32 LYS N . 18649 1 stop_ save_