data_11027 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 11027 _Entry.Title ; SPECTRIN SH3 CHIMERA WITH A LIGAND LINKED TO BE BOUND IN ORIENTATION II ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-01-17 _Entry.Accession_date 2008-01-17 _Entry.Last_release_date 2009-05-21 _Entry.Original_release_date 2009-05-21 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.100 _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.Entry_ID 1 Victor Kutyshenko N. P. . 11027 2 Dmitry Prokhorov . A. . 11027 3 Maria Timchenko . A. . 11027 4 Yuri Kudrevatykh . A. . 11027 5 Daria Fedyukina . V. . 11027 6 Lyubov Gushchina . V. . 11027 7 Vladimir Khristoforov . S. . 11027 8 Vladimir Filimonov . V. . 11027 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID alpha-spectrin . 11027 'chimeric protein' . 11027 'circular permutant' . 11027 SH3 . 11027 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 11027 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 319 11027 '15N chemical shifts' 69 11027 '1H chemical shifts' 501 11027 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 . . 2009-05-21 2008-01-17 original author . 11027 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 11027 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8836105 _Citation.Full_citation . _Citation.Title 'Different folding transition states may result in the same native structure.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 3 _Citation.Journal_issue 10 _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 874 _Citation.Page_last 880 _Citation.Year 1996 _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 A. Viguera N. R. . 11027 1 2 L. Serrano . . . 11027 1 3 M. Wilmanns . . . 11027 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 11027 _Assembly.ID 1 _Assembly.Name 'SH3-F2 (single chain polypeptide)' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 . _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 'alpha-spectrin SH3-F2' 1 $entity_1 A . yes native no no . . . 11027 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 11027 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'alpha-spectrin SH3-F2' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MGAPPLPPYSAGGREVTMKK GDILTLLNSTNKDWWKVEVN DRQGFVPAAYVKKLDSGTGK ELVLALYDYQEKS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details ; This is chimeric protein with the ligand-linker-SH3 topology where ligand is a sequence MGAPPLPPYSA; linker is GG and SH3 is a s19-p20 circular permutant of the WT alpha-spectrin SH3(PDB ID 1tuc) ; _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 73 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'Chicken Alpha-Spectrin Sh3 Domain' _Entity.Mutation ; The sequence, involving poliproline ligand MGAPPLPPYSA and GG linker, was conjugated with the N-terminal of circular permutant S19P20 (PDB ID 1tuc) instead of the first amino acids GP ; _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8068.312 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2014-05-12 loop_ _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 no BMRB 17089 . SH3-F2 . . . . . 100.00 73 100.00 100.00 5.26e-45 . . . . 11027 1 no PDB 1BK2 . "A-Spectrin Sh3 Domain D48g Mutant" . . . . . 57.53 57 97.62 97.62 6.24e-20 . . . . 11027 1 no PDB 1TUC . "Alpha-Spectrin Src Homology 3 Domain, Circular Permutant, Cut At S19-P20" . . . . . 84.93 63 98.39 98.39 1.09e-34 . . . . 11027 1 no PDB 2KXD . "The Structure Of Sh3-F2" . . . . . 100.00 73 100.00 100.00 5.26e-45 . . . . 11027 1 no PDB 3M0S . "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 7" . . . . . 56.16 57 100.00 100.00 3.84e-20 . . . . 11027 1 no REF XP_006119095 . "PREDICTED: LOW QUALITY PROTEIN: spectrin alpha chain, non-erythrocytic 1 [Pelodiscus sinensis]" . . . . . 57.53 2479 100.00 100.00 3.26e-19 . . . . 11027 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 . MET . 11027 1 2 . GLY . 11027 1 3 . ALA . 11027 1 4 . PRO . 11027 1 5 . PRO . 11027 1 6 . LEU . 11027 1 7 . PRO . 11027 1 8 . PRO . 11027 1 9 . TYR . 11027 1 10 . SER . 11027 1 11 . ALA . 11027 1 12 . GLY . 11027 1 13 . GLY . 11027 1 14 . ARG . 11027 1 15 . GLU . 11027 1 16 . VAL . 11027 1 17 . THR . 11027 1 18 . MET . 11027 1 19 . LYS . 11027 1 20 . LYS . 11027 1 21 . GLY . 11027 1 22 . ASP . 11027 1 23 . ILE . 11027 1 24 . LEU . 11027 1 25 . THR . 11027 1 26 . LEU . 11027 1 27 . LEU . 11027 1 28 . ASN . 11027 1 29 . SER . 11027 1 30 . THR . 11027 1 31 . ASN . 11027 1 32 . LYS . 11027 1 33 . ASP . 11027 1 34 . TRP . 11027 1 35 . TRP . 11027 1 36 . LYS . 11027 1 37 . VAL . 11027 1 38 . GLU . 11027 1 39 . VAL . 11027 1 40 . ASN . 11027 1 41 . ASP . 11027 1 42 . ARG . 11027 1 43 . GLN . 11027 1 44 . GLY . 11027 1 45 . PHE . 11027 1 46 . VAL . 11027 1 47 . PRO . 11027 1 48 . ALA . 11027 1 49 . ALA . 11027 1 50 . TYR . 11027 1 51 . VAL . 11027 1 52 . LYS . 11027 1 53 . LYS . 11027 1 54 . LEU . 11027 1 55 . ASP . 11027 1 56 . SER . 11027 1 57 . GLY . 11027 1 58 . THR . 11027 1 59 . GLY . 11027 1 60 . LYS . 11027 1 61 . GLU . 11027 1 62 . LEU . 11027 1 63 . VAL . 11027 1 64 . LEU . 11027 1 65 . ALA . 11027 1 66 . LEU . 11027 1 67 . TYR . 11027 1 68 . ASP . 11027 1 69 . TYR . 11027 1 70 . GLN . 11027 1 71 . GLU . 11027 1 72 . LYS . 11027 1 73 . SER . 11027 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 11027 1 . GLY 2 2 11027 1 . ALA 3 3 11027 1 . PRO 4 4 11027 1 . PRO 5 5 11027 1 . LEU 6 6 11027 1 . PRO 7 7 11027 1 . PRO 8 8 11027 1 . TYR 9 9 11027 1 . SER 10 10 11027 1 . ALA 11 11 11027 1 . GLY 12 12 11027 1 . GLY 13 13 11027 1 . ARG 14 14 11027 1 . GLU 15 15 11027 1 . VAL 16 16 11027 1 . THR 17 17 11027 1 . MET 18 18 11027 1 . LYS 19 19 11027 1 . LYS 20 20 11027 1 . GLY 21 21 11027 1 . ASP 22 22 11027 1 . ILE 23 23 11027 1 . LEU 24 24 11027 1 . THR 25 25 11027 1 . LEU 26 26 11027 1 . LEU 27 27 11027 1 . ASN 28 28 11027 1 . SER 29 29 11027 1 . THR 30 30 11027 1 . ASN 31 31 11027 1 . LYS 32 32 11027 1 . ASP 33 33 11027 1 . TRP 34 34 11027 1 . TRP 35 35 11027 1 . LYS 36 36 11027 1 . VAL 37 37 11027 1 . GLU 38 38 11027 1 . VAL 39 39 11027 1 . ASN 40 40 11027 1 . ASP 41 41 11027 1 . ARG 42 42 11027 1 . GLN 43 43 11027 1 . GLY 44 44 11027 1 . PHE 45 45 11027 1 . VAL 46 46 11027 1 . PRO 47 47 11027 1 . ALA 48 48 11027 1 . ALA 49 49 11027 1 . TYR 50 50 11027 1 . VAL 51 51 11027 1 . LYS 52 52 11027 1 . LYS 53 53 11027 1 . LEU 54 54 11027 1 . ASP 55 55 11027 1 . SER 56 56 11027 1 . GLY 57 57 11027 1 . THR 58 58 11027 1 . GLY 59 59 11027 1 . LYS 60 60 11027 1 . GLU 61 61 11027 1 . LEU 62 62 11027 1 . VAL 63 63 11027 1 . LEU 64 64 11027 1 . ALA 65 65 11027 1 . LEU 66 66 11027 1 . TYR 67 67 11027 1 . ASP 68 68 11027 1 . TYR 69 69 11027 1 . GLN 70 70 11027 1 . GLU 71 71 11027 1 . LYS 72 72 11027 1 . SER 73 73 11027 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 11027 _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 $entity_1 . 9031 . . 'Gallus gallus' Chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 11027 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 11027 _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 $entity_1 . 'recombinant technology' 'Escherichia coli' . . 469008 Escherichia coli BL21(DE3) . . . . . . . . . . . . plasmid . . pBAT-4 . . . . . . 11027 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 11027 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 'alpha-spectrin SH3-F2' '[U-98% 13C; U-98% 15N]' . . 1 $entity_1 . protein 2.5 . . mM . . . . 11027 1 2 'sodium acetate' '[U-99% 2H]' . . . . . buffer 25 . . mM . . . . 11027 1 3 'sodium azide' 'natural abundance' . . . . . 'antimicrobial agent' 0.03 . . % . . . . 11027 1 4 H2O 'natural abundance' . . . . . solvent 90 . . % . . . . 11027 1 5 D2O '[U-99% 2H]' . . . . . solvent 10 . . % . . . . 11027 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 11027 _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' 25 . mM 11027 1 pH 4 . pH 11027 1 pressure 744 . mmHg 11027 1 temperature 298 . K 11027 1 stop_ save_ ############################ # Computer software used # ############################ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 11027 _Software.ID 1 _Software.Name CARA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Rochus Keller and Kurt Wuthrich' ; Institute of Molecular Biology and Biophysics, ETH Honggerberg, CH-8093 Zurich ; rkeller@nmr.ch 11027 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 11027 1 'data collection' 11027 1 processing 11027 1 stop_ save_ save_TALOS _Software.Sf_category software _Software.Sf_framecode TALOS _Software.Entry_ID 11027 _Software.ID 2 _Software.Name TALOS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' ; Laboratory of Chemical Physics National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health Bethesda, Maryland 20892-0520 ; http://spin.niddk.nih.gov/NMRPipe/talos/ 11027 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'dihedral angles calculation' 11027 2 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 11027 _Software.ID 3 _Software.Name CYANA _Software.Version 2.1 _Software.Details ; The structure was determined using dihedral angles PHI and PSI predicted by program TALOS. H-bonds were determined on the basis of temperature dependence of NH chemical shifts. ; loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' 'L.A.SYSTEMS Inc. Masanobu Otsuka' http://www.las.jp/prod/cyana/eg/ 11027 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 11027 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 11027 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details ; AVANCE Bruker spectrometer equipped of triple resonance TXI probehead and pulsed field gradient. ; _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 11027 _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 . 600 ; AVANCE Bruker spectrometer equipped of triple resonance TXI probehead and pulsed field gradient. ; . . 11027 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 11027 _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 . . . . . . . . . . . . . . . . 11027 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 3 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 4 '3D HCCH-TOCSY-ali' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 5 '3D HCCH-TOCSY-aro' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 6 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 8 '3D 1H-13C NOESY-ali' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 9 '3D 1H-13C NOESY-aro' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 1 10 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11027 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 11027 _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 . indirect 0.251449530 . . . . . . . . . 11027 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 11027 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 11027 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 11027 _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' 1 $sample_1 isotropic 11027 1 2 '3D HNCACB' 1 $sample_1 isotropic 11027 1 3 '3D C(CO)NH' 1 $sample_1 isotropic 11027 1 4 '3D HCCH-TOCSY-ali' 1 $sample_1 isotropic 11027 1 5 '3D HCCH-TOCSY-aro' 1 $sample_1 isotropic 11027 1 6 '3D 1H-15N TOCSY' 1 $sample_1 isotropic 11027 1 8 '3D 1H-13C NOESY-ali' 1 $sample_1 isotropic 11027 1 10 '3D HNCO' 1 $sample_1 isotropic 11027 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET CA C 13 58.630 0.400 . 1 . . . . 1 MET CA . 11027 1 2 . 1 1 1 1 MET CB C 13 26.897 0.400 . 1 . . . . 1 MET CB . 11027 1 3 . 1 1 2 2 GLY N N 15 115.627 0.400 . 1 . . . . 2 GLY N . 11027 1 4 . 1 1 2 2 GLY H H 1 7.187 0.020 . 1 . . . . 2 GLY H . 11027 1 5 . 1 1 2 2 GLY CA C 13 42.837 0.400 . 1 . . . . 2 GLY CA . 11027 1 6 . 1 1 2 2 GLY HA2 H 1 3.801 0.020 . 2 . . . . 2 GLY HA2 . 11027 1 7 . 1 1 2 2 GLY HA3 H 1 3.801 0.020 . 2 . . . . 2 GLY HA3 . 11027 1 8 . 1 1 2 2 GLY C C 13 168.722 0.400 . 1 . . . . 2 GLY C . 11027 1 9 . 1 1 3 3 ALA N N 15 124.583 0.400 . 1 . . . . 3 ALA N . 11027 1 10 . 1 1 3 3 ALA H H 1 8.373 0.020 . 1 . . . . 3 ALA H . 11027 1 11 . 1 1 3 3 ALA CA C 13 50.904 0.400 . 1 . . . . 3 ALA CA . 11027 1 12 . 1 1 3 3 ALA HA H 1 3.550 0.020 . 1 . . . . 3 ALA HA . 11027 1 13 . 1 1 3 3 ALA HB1 H 1 0.892 0.020 . 1 . . . . 3 ALA HB . 11027 1 14 . 1 1 3 3 ALA HB2 H 1 0.892 0.020 . 1 . . . . 3 ALA HB . 11027 1 15 . 1 1 3 3 ALA HB3 H 1 0.892 0.020 . 1 . . . . 3 ALA HB . 11027 1 16 . 1 1 3 3 ALA CB C 13 17.001 0.400 . 1 . . . . 3 ALA CB . 11027 1 17 . 1 1 4 4 PRO CD C 13 49.738 0.400 . 1 . . . . 4 PRO CD . 11027 1 18 . 1 1 4 4 PRO CA C 13 61.753 0.400 . 1 . . . . 4 PRO CA . 11027 1 19 . 1 1 4 4 PRO HA H 1 4.524 0.020 . 1 . . . . 4 PRO HA . 11027 1 20 . 1 1 4 4 PRO CB C 13 29.578 0.400 . 1 . . . . 4 PRO CB . 11027 1 21 . 1 1 4 4 PRO HB2 H 1 2.246 0.020 . 2 . . . . 4 PRO HB2 . 11027 1 22 . 1 1 4 4 PRO HB3 H 1 2.246 0.020 . 2 . . . . 4 PRO HB3 . 11027 1 23 . 1 1 4 4 PRO CG C 13 26.463 0.400 . 1 . . . . 4 PRO CG . 11027 1 24 . 1 1 4 4 PRO HG2 H 1 1.545 0.020 . 2 . . . . 4 PRO HG2 . 11027 1 25 . 1 1 4 4 PRO HG3 H 1 1.655 0.020 . 2 . . . . 4 PRO HG3 . 11027 1 26 . 1 1 4 4 PRO HD2 H 1 2.634 0.020 . 2 . . . . 4 PRO HD2 . 11027 1 27 . 1 1 4 4 PRO HD3 H 1 2.145 0.020 . 2 . . . . 4 PRO HD3 . 11027 1 28 . 1 1 5 5 PRO CD C 13 50.210 0.400 . 1 . . . . 5 PRO CD . 11027 1 29 . 1 1 5 5 PRO CA C 13 62.967 0.400 . 1 . . . . 5 PRO CA . 11027 1 30 . 1 1 5 5 PRO HA H 1 4.348 0.020 . 1 . . . . 5 PRO HA . 11027 1 31 . 1 1 5 5 PRO CB C 13 31.137 0.400 . 1 . . . . 5 PRO CB . 11027 1 32 . 1 1 5 5 PRO HB2 H 1 2.237 0.020 . 2 . . . . 5 PRO HB2 . 11027 1 33 . 1 1 5 5 PRO HB3 H 1 1.774 0.020 . 2 . . . . 5 PRO HB3 . 11027 1 34 . 1 1 5 5 PRO CG C 13 27.134 0.400 . 1 . . . . 5 PRO CG . 11027 1 35 . 1 1 5 5 PRO HG2 H 1 1.943 0.020 . 2 . . . . 5 PRO HG2 . 11027 1 36 . 1 1 5 5 PRO HG3 H 1 1.943 0.020 . 2 . . . . 5 PRO HG3 . 11027 1 37 . 1 1 5 5 PRO HD2 H 1 3.682 0.020 . 2 . . . . 5 PRO HD2 . 11027 1 38 . 1 1 5 5 PRO HD3 H 1 3.465 0.020 . 2 . . . . 5 PRO HD3 . 11027 1 39 . 1 1 5 5 PRO C C 13 176.185 0.400 . 1 . . . . 5 PRO C . 11027 1 40 . 1 1 6 6 LEU N N 15 122.369 0.400 . 1 . . . . 6 LEU N . 11027 1 41 . 1 1 6 6 LEU H H 1 8.284 0.020 . 1 . . . . 6 LEU H . 11027 1 42 . 1 1 6 6 LEU CA C 13 52.516 0.400 . 1 . . . . 6 LEU CA . 11027 1 43 . 1 1 6 6 LEU HA H 1 4.296 0.020 . 1 . . . . 6 LEU HA . 11027 1 44 . 1 1 6 6 LEU CB C 13 41.309 0.400 . 1 . . . . 6 LEU CB . 11027 1 45 . 1 1 6 6 LEU HB2 H 1 1.382 0.020 . 2 . . . . 6 LEU HB2 . 11027 1 46 . 1 1 6 6 LEU HB3 H 1 1.592 0.020 . 2 . . . . 6 LEU HB3 . 11027 1 47 . 1 1 6 6 LEU CG C 13 27.036 0.400 . 1 . . . . 6 LEU CG . 11027 1 48 . 1 1 6 6 LEU HG H 1 1.810 0.020 . 1 . . . . 6 LEU HG . 11027 1 49 . 1 1 6 6 LEU HD11 H 1 1.059 0.020 . 2 . . . . 6 LEU HD1 . 11027 1 50 . 1 1 6 6 LEU HD12 H 1 1.059 0.020 . 2 . . . . 6 LEU HD1 . 11027 1 51 . 1 1 6 6 LEU HD13 H 1 1.059 0.020 . 2 . . . . 6 LEU HD1 . 11027 1 52 . 1 1 6 6 LEU HD21 H 1 0.743 0.020 . 2 . . . . 6 LEU HD2 . 11027 1 53 . 1 1 6 6 LEU HD22 H 1 0.743 0.020 . 2 . . . . 6 LEU HD2 . 11027 1 54 . 1 1 6 6 LEU HD23 H 1 0.743 0.020 . 2 . . . . 6 LEU HD2 . 11027 1 55 . 1 1 6 6 LEU CD1 C 13 25.157 0.400 . 1 . . . . 6 LEU CD1 . 11027 1 56 . 1 1 6 6 LEU CD2 C 13 24.788 0.400 . 1 . . . . 6 LEU CD2 . 11027 1 57 . 1 1 7 7 PRO CD C 13 49.926 0.400 . 1 . . . . 7 PRO CD . 11027 1 58 . 1 1 7 7 PRO CA C 13 61.165 0.400 . 1 . . . . 7 PRO CA . 11027 1 59 . 1 1 7 7 PRO HA H 1 4.517 0.020 . 1 . . . . 7 PRO HA . 11027 1 60 . 1 1 7 7 PRO CB C 13 30.373 0.400 . 1 . . . . 7 PRO CB . 11027 1 61 . 1 1 7 7 PRO HB2 H 1 1.866 0.020 . 2 . . . . 7 PRO HB2 . 11027 1 62 . 1 1 7 7 PRO HB3 H 1 1.655 0.020 . 2 . . . . 7 PRO HB3 . 11027 1 63 . 1 1 7 7 PRO CG C 13 26.565 0.400 . 1 . . . . 7 PRO CG . 11027 1 64 . 1 1 7 7 PRO HG2 H 1 1.298 0.020 . 2 . . . . 7 PRO HG2 . 11027 1 65 . 1 1 7 7 PRO HG3 H 1 0.540 0.020 . 2 . . . . 7 PRO HG3 . 11027 1 66 . 1 1 7 7 PRO HD2 H 1 3.324 0.020 . 2 . . . . 7 PRO HD2 . 11027 1 67 . 1 1 7 7 PRO HD3 H 1 2.880 0.020 . 2 . . . . 7 PRO HD3 . 11027 1 68 . 1 1 8 8 PRO CD C 13 50.350 0.400 . 1 . . . . 8 PRO CD . 11027 1 69 . 1 1 8 8 PRO CA C 13 63.232 0.400 . 1 . . . . 8 PRO CA . 11027 1 70 . 1 1 8 8 PRO HA H 1 4.454 0.020 . 1 . . . . 8 PRO HA . 11027 1 71 . 1 1 8 8 PRO CB C 13 30.239 0.400 . 1 . . . . 8 PRO CB . 11027 1 72 . 1 1 8 8 PRO HB2 H 1 2.047 0.020 . 2 . . . . 8 PRO HB2 . 11027 1 73 . 1 1 8 8 PRO HB3 H 1 2.153 0.020 . 2 . . . . 8 PRO HB3 . 11027 1 74 . 1 1 8 8 PRO CG C 13 27.001 0.400 . 1 . . . . 8 PRO CG . 11027 1 75 . 1 1 8 8 PRO HG2 H 1 1.956 0.020 . 2 . . . . 8 PRO HG2 . 11027 1 76 . 1 1 8 8 PRO HG3 H 1 1.956 0.020 . 2 . . . . 8 PRO HG3 . 11027 1 77 . 1 1 8 8 PRO HD2 H 1 3.500 0.020 . 2 . . . . 8 PRO HD2 . 11027 1 78 . 1 1 8 8 PRO HD3 H 1 3.696 0.020 . 2 . . . . 8 PRO HD3 . 11027 1 79 . 1 1 8 8 PRO C C 13 175.451 0.400 . 1 . . . . 8 PRO C . 11027 1 80 . 1 1 9 9 TYR N N 15 118.183 0.400 . 1 . . . . 9 TYR N . 11027 1 81 . 1 1 9 9 TYR H H 1 7.485 0.020 . 1 . . . . 9 TYR H . 11027 1 82 . 1 1 9 9 TYR CA C 13 56.082 0.400 . 1 . . . . 9 TYR CA . 11027 1 83 . 1 1 9 9 TYR HA H 1 4.655 0.020 . 1 . . . . 9 TYR HA . 11027 1 84 . 1 1 9 9 TYR CB C 13 39.416 0.400 . 1 . . . . 9 TYR CB . 11027 1 85 . 1 1 9 9 TYR HB2 H 1 2.949 0.020 . 2 . . . . 9 TYR HB2 . 11027 1 86 . 1 1 9 9 TYR HB3 H 1 2.988 0.020 . 2 . . . . 9 TYR HB3 . 11027 1 87 . 1 1 9 9 TYR CD1 C 13 133.465 0.400 . 1 . . . . 9 TYR CD1 . 11027 1 88 . 1 1 9 9 TYR HD1 H 1 6.893 0.020 . 1 . . . . 9 TYR HD1 . 11027 1 89 . 1 1 9 9 TYR CE1 C 13 117.959 0.400 . 1 . . . . 9 TYR CE1 . 11027 1 90 . 1 1 9 9 TYR HE1 H 1 6.761 0.020 . 1 . . . . 9 TYR HE1 . 11027 1 91 . 1 1 9 9 TYR CE2 C 13 117.959 0.400 . 1 . . . . 9 TYR CE2 . 11027 1 92 . 1 1 9 9 TYR HE2 H 1 6.761 0.020 . 1 . . . . 9 TYR HE2 . 11027 1 93 . 1 1 9 9 TYR CD2 C 13 133.435 0.400 . 1 . . . . 9 TYR CD2 . 11027 1 94 . 1 1 9 9 TYR HD2 H 1 6.893 0.020 . 1 . . . . 9 TYR HD2 . 11027 1 95 . 1 1 9 9 TYR C C 13 174.699 0.400 . 1 . . . . 9 TYR C . 11027 1 96 . 1 1 10 10 SER N N 15 116.751 0.400 . 1 . . . . 10 SER N . 11027 1 97 . 1 1 10 10 SER H H 1 8.120 0.020 . 1 . . . . 10 SER H . 11027 1 98 . 1 1 10 10 SER CA C 13 57.758 0.400 . 1 . . . . 10 SER CA . 11027 1 99 . 1 1 10 10 SER HA H 1 4.240 0.020 . 1 . . . . 10 SER HA . 11027 1 100 . 1 1 10 10 SER CB C 13 64.015 0.400 . 1 . . . . 10 SER CB . 11027 1 101 . 1 1 10 10 SER HB2 H 1 3.781 0.020 . 2 . . . . 10 SER HB2 . 11027 1 102 . 1 1 10 10 SER HB3 H 1 3.677 0.020 . 2 . . . . 10 SER HB3 . 11027 1 103 . 1 1 10 10 SER C C 13 173.693 0.400 . 1 . . . . 10 SER C . 11027 1 104 . 1 1 11 11 ALA N N 15 123.966 0.400 . 1 . . . . 11 ALA N . 11027 1 105 . 1 1 11 11 ALA H H 1 6.808 0.020 . 1 . . . . 11 ALA H . 11027 1 106 . 1 1 11 11 ALA CA C 13 52.080 0.400 . 1 . . . . 11 ALA CA . 11027 1 107 . 1 1 11 11 ALA HA H 1 2.994 0.020 . 1 . . . . 11 ALA HA . 11027 1 108 . 1 1 11 11 ALA HB1 H 1 -0.044 0.020 . 1 . . . . 11 ALA HB . 11027 1 109 . 1 1 11 11 ALA HB2 H 1 -0.044 0.020 . 1 . . . . 11 ALA HB . 11027 1 110 . 1 1 11 11 ALA HB3 H 1 -0.044 0.020 . 1 . . . . 11 ALA HB . 11027 1 111 . 1 1 11 11 ALA CB C 13 18.165 0.400 . 1 . . . . 11 ALA CB . 11027 1 112 . 1 1 11 11 ALA C C 13 177.520 0.400 . 1 . . . . 11 ALA C . 11027 1 113 . 1 1 12 12 GLY N N 15 105.312 0.400 . 1 . . . . 12 GLY N . 11027 1 114 . 1 1 12 12 GLY H H 1 7.803 0.020 . 1 . . . . 12 GLY H . 11027 1 115 . 1 1 12 12 GLY CA C 13 45.020 0.400 . 1 . . . . 12 GLY CA . 11027 1 116 . 1 1 12 12 GLY HA2 H 1 3.700 0.020 . 2 . . . . 12 GLY HA2 . 11027 1 117 . 1 1 12 12 GLY HA3 H 1 3.629 0.020 . 2 . . . . 12 GLY HA3 . 11027 1 118 . 1 1 12 12 GLY C C 13 173.871 0.400 . 1 . . . . 12 GLY C . 11027 1 119 . 1 1 13 13 GLY N N 15 106.157 0.400 . 1 . . . . 13 GLY N . 11027 1 120 . 1 1 13 13 GLY H H 1 7.132 0.020 . 1 . . . . 13 GLY H . 11027 1 121 . 1 1 13 13 GLY CA C 13 44.438 0.400 . 1 . . . . 13 GLY CA . 11027 1 122 . 1 1 13 13 GLY HA2 H 1 4.115 0.020 . 2 . . . . 13 GLY HA2 . 11027 1 123 . 1 1 13 13 GLY HA3 H 1 3.970 0.020 . 2 . . . . 13 GLY HA3 . 11027 1 124 . 1 1 13 13 GLY C C 13 172.291 0.400 . 1 . . . . 13 GLY C . 11027 1 125 . 1 1 14 14 ARG N N 15 120.715 0.400 . 1 . . . . 14 ARG N . 11027 1 126 . 1 1 14 14 ARG H H 1 8.534 0.020 . 1 . . . . 14 ARG H . 11027 1 127 . 1 1 14 14 ARG CA C 13 56.301 0.400 . 1 . . . . 14 ARG CA . 11027 1 128 . 1 1 14 14 ARG HA H 1 4.347 0.020 . 1 . . . . 14 ARG HA . 11027 1 129 . 1 1 14 14 ARG CB C 13 30.773 0.400 . 1 . . . . 14 ARG CB . 11027 1 130 . 1 1 14 14 ARG HB2 H 1 1.913 0.020 . 2 . . . . 14 ARG HB2 . 11027 1 131 . 1 1 14 14 ARG HB3 H 1 1.948 0.020 . 2 . . . . 14 ARG HB3 . 11027 1 132 . 1 1 14 14 ARG CG C 13 27.826 0.400 . 1 . . . . 14 ARG CG . 11027 1 133 . 1 1 14 14 ARG HG2 H 1 1.641 0.020 . 2 . . . . 14 ARG HG2 . 11027 1 134 . 1 1 14 14 ARG HG3 H 1 1.711 0.020 . 2 . . . . 14 ARG HG3 . 11027 1 135 . 1 1 14 14 ARG CD C 13 43.072 0.400 . 1 . . . . 14 ARG CD . 11027 1 136 . 1 1 14 14 ARG HD2 H 1 3.268 0.020 . 2 . . . . 14 ARG HD2 . 11027 1 137 . 1 1 14 14 ARG HD3 H 1 3.268 0.020 . 2 . . . . 14 ARG HD3 . 11027 1 138 . 1 1 14 14 ARG C C 13 176.185 0.400 . 1 . . . . 14 ARG C . 11027 1 139 . 1 1 15 15 GLU N N 15 122.761 0.400 . 1 . . . . 15 GLU N . 11027 1 140 . 1 1 15 15 GLU H H 1 8.633 0.020 . 1 . . . . 15 GLU H . 11027 1 141 . 1 1 15 15 GLU CA C 13 55.791 0.400 . 1 . . . . 15 GLU CA . 11027 1 142 . 1 1 15 15 GLU HA H 1 5.145 0.020 . 1 . . . . 15 GLU HA . 11027 1 143 . 1 1 15 15 GLU CB C 13 30.865 0.400 . 1 . . . . 15 GLU CB . 11027 1 144 . 1 1 15 15 GLU HB2 H 1 2.075 0.020 . 2 . . . . 15 GLU HB2 . 11027 1 145 . 1 1 15 15 GLU HB3 H 1 2.417 0.020 . 2 . . . . 15 GLU HB3 . 11027 1 146 . 1 1 15 15 GLU CG C 13 34.393 0.400 . 1 . . . . 15 GLU CG . 11027 1 147 . 1 1 15 15 GLU HG2 H 1 2.322 0.020 . 2 . . . . 15 GLU HG2 . 11027 1 148 . 1 1 15 15 GLU HG3 H 1 2.322 0.020 . 2 . . . . 15 GLU HG3 . 11027 1 149 . 1 1 15 15 GLU C C 13 175.918 0.400 . 1 . . . . 15 GLU C . 11027 1 150 . 1 1 16 16 VAL N N 15 118.566 0.400 . 1 . . . . 16 VAL N . 11027 1 151 . 1 1 16 16 VAL H H 1 7.880 0.020 . 1 . . . . 16 VAL H . 11027 1 152 . 1 1 16 16 VAL CA C 13 60.734 0.400 . 1 . . . . 16 VAL CA . 11027 1 153 . 1 1 16 16 VAL HA H 1 4.385 0.020 . 1 . . . . 16 VAL HA . 11027 1 154 . 1 1 16 16 VAL CB C 13 34.538 0.400 . 1 . . . . 16 VAL CB . 11027 1 155 . 1 1 16 16 VAL HB H 1 1.779 0.020 . 1 . . . . 16 VAL HB . 11027 1 156 . 1 1 16 16 VAL HG11 H 1 0.659 0.020 . 2 . . . . 16 VAL HG1 . 11027 1 157 . 1 1 16 16 VAL HG12 H 1 0.659 0.020 . 2 . . . . 16 VAL HG1 . 11027 1 158 . 1 1 16 16 VAL HG13 H 1 0.659 0.020 . 2 . . . . 16 VAL HG1 . 11027 1 159 . 1 1 16 16 VAL HG21 H 1 0.659 0.020 . 2 . . . . 16 VAL HG2 . 11027 1 160 . 1 1 16 16 VAL HG22 H 1 0.659 0.020 . 2 . . . . 16 VAL HG2 . 11027 1 161 . 1 1 16 16 VAL HG23 H 1 0.659 0.020 . 2 . . . . 16 VAL HG2 . 11027 1 162 . 1 1 16 16 VAL CG1 C 13 20.385 0.400 . 1 . . . . 16 VAL CG1 . 11027 1 163 . 1 1 16 16 VAL C C 13 172.825 0.400 . 1 . . . . 16 VAL C . 11027 1 164 . 1 1 17 17 THR N N 15 116.529 0.400 . 1 . . . . 17 THR N . 11027 1 165 . 1 1 17 17 THR H H 1 7.527 0.020 . 1 . . . . 17 THR H . 11027 1 166 . 1 1 17 17 THR CA C 13 61.251 0.400 . 1 . . . . 17 THR CA . 11027 1 167 . 1 1 17 17 THR HA H 1 4.849 0.020 . 1 . . . . 17 THR HA . 11027 1 168 . 1 1 17 17 THR CB C 13 70.639 0.400 . 1 . . . . 17 THR CB . 11027 1 169 . 1 1 17 17 THR HB H 1 4.102 0.020 . 1 . . . . 17 THR HB . 11027 1 170 . 1 1 17 17 THR HG21 H 1 1.251 0.020 . 1 . . . . 17 THR HG2 . 11027 1 171 . 1 1 17 17 THR HG22 H 1 1.251 0.020 . 1 . . . . 17 THR HG2 . 11027 1 172 . 1 1 17 17 THR HG23 H 1 1.251 0.020 . 1 . . . . 17 THR HG2 . 11027 1 173 . 1 1 17 17 THR CG2 C 13 21.946 0.400 . 1 . . . . 17 THR CG2 . 11027 1 174 . 1 1 17 17 THR C C 13 174.004 0.400 . 1 . . . . 17 THR C . 11027 1 175 . 1 1 18 18 MET N N 15 119.983 0.400 . 1 . . . . 18 MET N . 11027 1 176 . 1 1 18 18 MET H H 1 9.283 0.020 . 1 . . . . 18 MET H . 11027 1 177 . 1 1 18 18 MET CA C 13 54.626 0.400 . 1 . . . . 18 MET CA . 11027 1 178 . 1 1 18 18 MET HA H 1 4.861 0.020 . 1 . . . . 18 MET HA . 11027 1 179 . 1 1 18 18 MET CB C 13 36.248 0.400 . 1 . . . . 18 MET CB . 11027 1 180 . 1 1 18 18 MET HB2 H 1 2.180 0.020 . 2 . . . . 18 MET HB2 . 11027 1 181 . 1 1 18 18 MET HB3 H 1 1.957 0.020 . 2 . . . . 18 MET HB3 . 11027 1 182 . 1 1 18 18 MET CG C 13 31.244 0.400 . 1 . . . . 18 MET CG . 11027 1 183 . 1 1 18 18 MET HG2 H 1 2.557 0.020 . 2 . . . . 18 MET HG2 . 11027 1 184 . 1 1 18 18 MET HG3 H 1 2.728 0.020 . 2 . . . . 18 MET HG3 . 11027 1 185 . 1 1 18 18 MET HE1 H 1 1.964 0.020 . 1 . . . . 18 MET HE . 11027 1 186 . 1 1 18 18 MET HE2 H 1 1.964 0.020 . 1 . . . . 18 MET HE . 11027 1 187 . 1 1 18 18 MET HE3 H 1 1.964 0.020 . 1 . . . . 18 MET HE . 11027 1 188 . 1 1 18 18 MET C C 13 173.693 0.400 . 1 . . . . 18 MET C . 11027 1 189 . 1 1 19 19 LYS N N 15 124.615 0.400 . 1 . . . . 19 LYS N . 11027 1 190 . 1 1 19 19 LYS H H 1 8.896 0.020 . 1 . . . . 19 LYS H . 11027 1 191 . 1 1 19 19 LYS CA C 13 53.535 0.400 . 1 . . . . 19 LYS CA . 11027 1 192 . 1 1 19 19 LYS HA H 1 4.895 0.020 . 1 . . . . 19 LYS HA . 11027 1 193 . 1 1 19 19 LYS CB C 13 34.233 0.400 . 1 . . . . 19 LYS CB . 11027 1 194 . 1 1 19 19 LYS HB2 H 1 1.681 0.020 . 2 . . . . 19 LYS HB2 . 11027 1 195 . 1 1 19 19 LYS HB3 H 1 1.681 0.020 . 2 . . . . 19 LYS HB3 . 11027 1 196 . 1 1 19 19 LYS CG C 13 23.792 0.400 . 1 . . . . 19 LYS CG . 11027 1 197 . 1 1 19 19 LYS HG2 H 1 1.419 0.020 . 2 . . . . 19 LYS HG2 . 11027 1 198 . 1 1 19 19 LYS HG3 H 1 1.419 0.020 . 2 . . . . 19 LYS HG3 . 11027 1 199 . 1 1 19 19 LYS CD C 13 28.334 0.400 . 1 . . . . 19 LYS CD . 11027 1 200 . 1 1 19 19 LYS HD2 H 1 1.681 0.020 . 2 . . . . 19 LYS HD2 . 11027 1 201 . 1 1 19 19 LYS HD3 H 1 1.681 0.020 . 2 . . . . 19 LYS HD3 . 11027 1 202 . 1 1 19 19 LYS CE C 13 41.820 0.400 . 1 . . . . 19 LYS CE . 11027 1 203 . 1 1 19 19 LYS HE2 H 1 2.988 0.020 . 2 . . . . 19 LYS HE2 . 11027 1 204 . 1 1 19 19 LYS HE3 H 1 2.988 0.020 . 2 . . . . 19 LYS HE3 . 11027 1 205 . 1 1 19 19 LYS C C 13 175.095 0.400 . 1 . . . . 19 LYS C . 11027 1 206 . 1 1 20 20 LYS N N 15 122.217 0.400 . 1 . . . . 20 LYS N . 11027 1 207 . 1 1 20 20 LYS H H 1 8.941 0.020 . 1 . . . . 20 LYS H . 11027 1 208 . 1 1 20 20 LYS CA C 13 58.630 0.400 . 1 . . . . 20 LYS CA . 11027 1 209 . 1 1 20 20 LYS HA H 1 4.561 0.020 . 1 . . . . 20 LYS HA . 11027 1 210 . 1 1 20 20 LYS CB C 13 32.284 0.400 . 1 . . . . 20 LYS CB . 11027 1 211 . 1 1 20 20 LYS HB2 H 1 1.831 0.020 . 2 . . . . 20 LYS HB2 . 11027 1 212 . 1 1 20 20 LYS HB3 H 1 1.831 0.020 . 2 . . . . 20 LYS HB3 . 11027 1 213 . 1 1 20 20 LYS CG C 13 24.005 0.400 . 1 . . . . 20 LYS CG . 11027 1 214 . 1 1 20 20 LYS HG2 H 1 1.446 0.020 . 2 . . . . 20 LYS HG2 . 11027 1 215 . 1 1 20 20 LYS HG3 H 1 1.446 0.020 . 2 . . . . 20 LYS HG3 . 11027 1 216 . 1 1 20 20 LYS CD C 13 29.250 0.400 . 1 . . . . 20 LYS CD . 11027 1 217 . 1 1 20 20 LYS HD2 H 1 1.648 0.020 . 2 . . . . 20 LYS HD2 . 11027 1 218 . 1 1 20 20 LYS HD3 H 1 1.718 0.020 . 2 . . . . 20 LYS HD3 . 11027 1 219 . 1 1 20 20 LYS CE C 13 42.064 0.400 . 1 . . . . 20 LYS CE . 11027 1 220 . 1 1 20 20 LYS HE2 H 1 2.834 0.020 . 2 . . . . 20 LYS HE2 . 11027 1 221 . 1 1 20 20 LYS HE3 H 1 2.834 0.020 . 2 . . . . 20 LYS HE3 . 11027 1 222 . 1 1 20 20 LYS C C 13 177.142 0.400 . 1 . . . . 20 LYS C . 11027 1 223 . 1 1 21 21 GLY N N 15 115.664 0.400 . 1 . . . . 21 GLY N . 11027 1 224 . 1 1 21 21 GLY H H 1 8.865 0.020 . 1 . . . . 21 GLY H . 11027 1 225 . 1 1 21 21 GLY CA C 13 44.657 0.400 . 1 . . . . 21 GLY CA . 11027 1 226 . 1 1 21 21 GLY HA2 H 1 4.482 0.020 . 2 . . . . 21 GLY HA2 . 11027 1 227 . 1 1 21 21 GLY HA3 H 1 3.503 0.020 . 2 . . . . 21 GLY HA3 . 11027 1 228 . 1 1 21 21 GLY C C 13 174.004 0.400 . 1 . . . . 21 GLY C . 11027 1 229 . 1 1 22 22 ASP N N 15 122.284 0.400 . 1 . . . . 22 ASP N . 11027 1 230 . 1 1 22 22 ASP H H 1 8.527 0.020 . 1 . . . . 22 ASP H . 11027 1 231 . 1 1 22 22 ASP CA C 13 55.646 0.400 . 1 . . . . 22 ASP CA . 11027 1 232 . 1 1 22 22 ASP HA H 1 4.501 0.020 . 1 . . . . 22 ASP HA . 11027 1 233 . 1 1 22 22 ASP CB C 13 41.236 0.400 . 1 . . . . 22 ASP CB . 11027 1 234 . 1 1 22 22 ASP HB2 H 1 2.801 0.020 . 2 . . . . 22 ASP HB2 . 11027 1 235 . 1 1 22 22 ASP HB3 H 1 2.553 0.020 . 2 . . . . 22 ASP HB3 . 11027 1 236 . 1 1 22 22 ASP C C 13 174.249 0.400 . 1 . . . . 22 ASP C . 11027 1 237 . 1 1 23 23 ILE N N 15 120.167 0.400 . 1 . . . . 23 ILE N . 11027 1 238 . 1 1 23 23 ILE H H 1 8.105 0.020 . 1 . . . . 23 ILE H . 11027 1 239 . 1 1 23 23 ILE CA C 13 60.085 0.400 . 1 . . . . 23 ILE CA . 11027 1 240 . 1 1 23 23 ILE HA H 1 5.054 0.020 . 1 . . . . 23 ILE HA . 11027 1 241 . 1 1 23 23 ILE CB C 13 38.616 0.400 . 1 . . . . 23 ILE CB . 11027 1 242 . 1 1 23 23 ILE HB H 1 1.754 0.020 . 1 . . . . 23 ILE HB . 11027 1 243 . 1 1 23 23 ILE HG21 H 1 0.856 0.020 . 1 . . . . 23 ILE HG2 . 11027 1 244 . 1 1 23 23 ILE HG22 H 1 0.856 0.020 . 1 . . . . 23 ILE HG2 . 11027 1 245 . 1 1 23 23 ILE HG23 H 1 0.856 0.020 . 1 . . . . 23 ILE HG2 . 11027 1 246 . 1 1 23 23 ILE CG2 C 13 18.292 0.400 . 1 . . . . 23 ILE CG2 . 11027 1 247 . 1 1 23 23 ILE CG1 C 13 27.411 0.400 . 1 . . . . 23 ILE CG1 . 11027 1 248 . 1 1 23 23 ILE HG12 H 1 1.092 0.020 . 2 . . . . 23 ILE HG12 . 11027 1 249 . 1 1 23 23 ILE HG13 H 1 1.679 0.020 . 2 . . . . 23 ILE HG13 . 11027 1 250 . 1 1 23 23 ILE HD11 H 1 0.890 0.020 . 1 . . . . 23 ILE HD1 . 11027 1 251 . 1 1 23 23 ILE HD12 H 1 0.890 0.020 . 1 . . . . 23 ILE HD1 . 11027 1 252 . 1 1 23 23 ILE HD13 H 1 0.890 0.020 . 1 . . . . 23 ILE HD1 . 11027 1 253 . 1 1 23 23 ILE C C 13 176.296 0.400 . 1 . . . . 23 ILE C . 11027 1 254 . 1 1 24 24 LEU N N 15 127.196 0.400 . 1 . . . . 24 LEU N . 11027 1 255 . 1 1 24 24 LEU H H 1 9.282 0.020 . 1 . . . . 24 LEU H . 11027 1 256 . 1 1 24 24 LEU CA C 13 53.902 0.400 . 1 . . . . 24 LEU CA . 11027 1 257 . 1 1 24 24 LEU HA H 1 4.974 0.020 . 1 . . . . 24 LEU HA . 11027 1 258 . 1 1 24 24 LEU CB C 13 43.929 0.400 . 1 . . . . 24 LEU CB . 11027 1 259 . 1 1 24 24 LEU HB2 H 1 1.566 0.020 . 2 . . . . 24 LEU HB2 . 11027 1 260 . 1 1 24 24 LEU HB3 H 1 1.411 0.020 . 2 . . . . 24 LEU HB3 . 11027 1 261 . 1 1 24 24 LEU CG C 13 27.269 0.400 . 1 . . . . 24 LEU CG . 11027 1 262 . 1 1 24 24 LEU HD11 H 1 0.898 0.020 . 2 . . . . 24 LEU HD1 . 11027 1 263 . 1 1 24 24 LEU HD12 H 1 0.898 0.020 . 2 . . . . 24 LEU HD1 . 11027 1 264 . 1 1 24 24 LEU HD13 H 1 0.898 0.020 . 2 . . . . 24 LEU HD1 . 11027 1 265 . 1 1 24 24 LEU HD21 H 1 0.842 0.020 . 2 . . . . 24 LEU HD2 . 11027 1 266 . 1 1 24 24 LEU HD22 H 1 0.842 0.020 . 2 . . . . 24 LEU HD2 . 11027 1 267 . 1 1 24 24 LEU HD23 H 1 0.842 0.020 . 2 . . . . 24 LEU HD2 . 11027 1 268 . 1 1 24 24 LEU CD1 C 13 26.715 0.400 . 1 . . . . 24 LEU CD1 . 11027 1 269 . 1 1 24 24 LEU CD2 C 13 27.312 0.400 . 1 . . . . 24 LEU CD2 . 11027 1 270 . 1 1 24 24 LEU C C 13 175.562 0.400 . 1 . . . . 24 LEU C . 11027 1 271 . 1 1 25 25 THR N N 15 117.801 0.400 . 1 . . . . 25 THR N . 11027 1 272 . 1 1 25 25 THR H H 1 8.515 0.020 . 1 . . . . 25 THR H . 11027 1 273 . 1 1 25 25 THR CA C 13 63.361 0.400 . 1 . . . . 25 THR CA . 11027 1 274 . 1 1 25 25 THR HA H 1 4.565 0.020 . 1 . . . . 25 THR HA . 11027 1 275 . 1 1 25 25 THR CB C 13 69.690 0.400 . 1 . . . . 25 THR CB . 11027 1 276 . 1 1 25 25 THR HB H 1 4.127 0.020 . 1 . . . . 25 THR HB . 11027 1 277 . 1 1 25 25 THR HG21 H 1 1.140 0.020 . 1 . . . . 25 THR HG2 . 11027 1 278 . 1 1 25 25 THR HG22 H 1 1.140 0.020 . 1 . . . . 25 THR HG2 . 11027 1 279 . 1 1 25 25 THR HG23 H 1 1.140 0.020 . 1 . . . . 25 THR HG2 . 11027 1 280 . 1 1 25 25 THR CG2 C 13 21.662 0.400 . 1 . . . . 25 THR CG2 . 11027 1 281 . 1 1 25 25 THR C C 13 173.671 0.400 . 1 . . . . 25 THR C . 11027 1 282 . 1 1 26 26 LEU N N 15 129.213 0.400 . 1 . . . . 26 LEU N . 11027 1 283 . 1 1 26 26 LEU H H 1 8.848 0.020 . 1 . . . . 26 LEU H . 11027 1 284 . 1 1 26 26 LEU CA C 13 54.772 0.400 . 1 . . . . 26 LEU CA . 11027 1 285 . 1 1 26 26 LEU HA H 1 4.393 0.020 . 1 . . . . 26 LEU HA . 11027 1 286 . 1 1 26 26 LEU CB C 13 43.201 0.400 . 1 . . . . 26 LEU CB . 11027 1 287 . 1 1 26 26 LEU HB2 H 1 1.777 0.020 . 2 . . . . 26 LEU HB2 . 11027 1 288 . 1 1 26 26 LEU HB3 H 1 1.777 0.020 . 2 . . . . 26 LEU HB3 . 11027 1 289 . 1 1 26 26 LEU CG C 13 26.341 0.400 . 1 . . . . 26 LEU CG . 11027 1 290 . 1 1 26 26 LEU HG H 1 1.132 0.020 . 1 . . . . 26 LEU HG . 11027 1 291 . 1 1 26 26 LEU HD11 H 1 0.680 0.020 . 2 . . . . 26 LEU HD1 . 11027 1 292 . 1 1 26 26 LEU HD12 H 1 0.680 0.020 . 2 . . . . 26 LEU HD1 . 11027 1 293 . 1 1 26 26 LEU HD13 H 1 0.680 0.020 . 2 . . . . 26 LEU HD1 . 11027 1 294 . 1 1 26 26 LEU HD21 H 1 0.393 0.020 . 2 . . . . 26 LEU HD2 . 11027 1 295 . 1 1 26 26 LEU HD22 H 1 0.393 0.020 . 2 . . . . 26 LEU HD2 . 11027 1 296 . 1 1 26 26 LEU HD23 H 1 0.393 0.020 . 2 . . . . 26 LEU HD2 . 11027 1 297 . 1 1 26 26 LEU CD1 C 13 23.131 0.400 . 1 . . . . 26 LEU CD1 . 11027 1 298 . 1 1 26 26 LEU CD2 C 13 24.910 0.400 . 1 . . . . 26 LEU CD2 . 11027 1 299 . 1 1 26 26 LEU C C 13 174.561 0.400 . 1 . . . . 26 LEU C . 11027 1 300 . 1 1 27 27 LEU N N 15 126.293 0.400 . 1 . . . . 27 LEU N . 11027 1 301 . 1 1 27 27 LEU H H 1 9.099 0.020 . 1 . . . . 27 LEU H . 11027 1 302 . 1 1 27 27 LEU CA C 13 55.131 0.400 . 1 . . . . 27 LEU CA . 11027 1 303 . 1 1 27 27 LEU HA H 1 4.523 0.020 . 1 . . . . 27 LEU HA . 11027 1 304 . 1 1 27 27 LEU CB C 13 43.360 0.400 . 1 . . . . 27 LEU CB . 11027 1 305 . 1 1 27 27 LEU HB2 H 1 1.391 0.020 . 2 . . . . 27 LEU HB2 . 11027 1 306 . 1 1 27 27 LEU HB3 H 1 1.167 0.020 . 2 . . . . 27 LEU HB3 . 11027 1 307 . 1 1 27 27 LEU CG C 13 26.469 0.400 . 1 . . . . 27 LEU CG . 11027 1 308 . 1 1 27 27 LEU HG H 1 1.391 0.020 . 1 . . . . 27 LEU HG . 11027 1 309 . 1 1 27 27 LEU HD11 H 1 0.680 0.020 . 2 . . . . 27 LEU HD1 . 11027 1 310 . 1 1 27 27 LEU HD12 H 1 0.680 0.020 . 2 . . . . 27 LEU HD1 . 11027 1 311 . 1 1 27 27 LEU HD13 H 1 0.680 0.020 . 2 . . . . 27 LEU HD1 . 11027 1 312 . 1 1 27 27 LEU HD21 H 1 0.729 0.020 . 2 . . . . 27 LEU HD2 . 11027 1 313 . 1 1 27 27 LEU HD22 H 1 0.729 0.020 . 2 . . . . 27 LEU HD2 . 11027 1 314 . 1 1 27 27 LEU HD23 H 1 0.729 0.020 . 2 . . . . 27 LEU HD2 . 11027 1 315 . 1 1 27 27 LEU CD1 C 13 21.454 0.400 . 1 . . . . 27 LEU CD1 . 11027 1 316 . 1 1 27 27 LEU CD2 C 13 22.254 0.400 . 1 . . . . 27 LEU CD2 . 11027 1 317 . 1 1 27 27 LEU C C 13 177.476 0.400 . 1 . . . . 27 LEU C . 11027 1 318 . 1 1 28 28 ASN N N 15 113.997 0.400 . 1 . . . . 28 ASN N . 11027 1 319 . 1 1 28 28 ASN H H 1 7.655 0.020 . 1 . . . . 28 ASN H . 11027 1 320 . 1 1 28 28 ASN CA C 13 54.479 0.400 . 1 . . . . 28 ASN CA . 11027 1 321 . 1 1 28 28 ASN HA H 1 4.707 0.020 . 1 . . . . 28 ASN HA . 11027 1 322 . 1 1 28 28 ASN CB C 13 41.016 0.400 . 1 . . . . 28 ASN CB . 11027 1 323 . 1 1 28 28 ASN HB2 H 1 2.763 0.020 . 2 . . . . 28 ASN HB2 . 11027 1 324 . 1 1 28 28 ASN HB3 H 1 2.660 0.020 . 2 . . . . 28 ASN HB3 . 11027 1 325 . 1 1 28 28 ASN C C 13 174.316 0.400 . 1 . . . . 28 ASN C . 11027 1 326 . 1 1 29 29 SER N N 15 123.485 0.400 . 1 . . . . 29 SER N . 11027 1 327 . 1 1 29 29 SER H H 1 9.126 0.020 . 1 . . . . 29 SER H . 11027 1 328 . 1 1 29 29 SER CA C 13 56.952 0.400 . 1 . . . . 29 SER CA . 11027 1 329 . 1 1 29 29 SER HA H 1 3.920 0.020 . 1 . . . . 29 SER HA . 11027 1 330 . 1 1 29 29 SER CB C 13 62.219 0.400 . 1 . . . . 29 SER CB . 11027 1 331 . 1 1 29 29 SER HB2 H 1 2.041 0.020 . 2 . . . . 29 SER HB2 . 11027 1 332 . 1 1 29 29 SER HB3 H 1 2.892 0.020 . 2 . . . . 29 SER HB3 . 11027 1 333 . 1 1 29 29 SER C C 13 173.381 0.400 . 1 . . . . 29 SER C . 11027 1 334 . 1 1 30 30 THR N N 15 115.195 0.400 . 1 . . . . 30 THR N . 11027 1 335 . 1 1 30 30 THR H H 1 8.217 0.020 . 1 . . . . 30 THR H . 11027 1 336 . 1 1 30 30 THR CA C 13 65.326 0.400 . 1 . . . . 30 THR CA . 11027 1 337 . 1 1 30 30 THR HA H 1 3.984 0.020 . 1 . . . . 30 THR HA . 11027 1 338 . 1 1 30 30 THR CB C 13 69.544 0.400 . 1 . . . . 30 THR CB . 11027 1 339 . 1 1 30 30 THR HB H 1 4.269 0.020 . 1 . . . . 30 THR HB . 11027 1 340 . 1 1 30 30 THR HG21 H 1 1.308 0.020 . 1 . . . . 30 THR HG2 . 11027 1 341 . 1 1 30 30 THR HG22 H 1 1.308 0.020 . 1 . . . . 30 THR HG2 . 11027 1 342 . 1 1 30 30 THR HG23 H 1 1.308 0.020 . 1 . . . . 30 THR HG2 . 11027 1 343 . 1 1 30 30 THR CG2 C 13 21.662 0.400 . 1 . . . . 30 THR CG2 . 11027 1 344 . 1 1 30 30 THR C C 13 175.317 0.400 . 1 . . . . 30 THR C . 11027 1 345 . 1 1 31 31 ASN N N 15 122.788 0.400 . 1 . . . . 31 ASN N . 11027 1 346 . 1 1 31 31 ASN H H 1 8.667 0.020 . 1 . . . . 31 ASN H . 11027 1 347 . 1 1 31 31 ASN CA C 13 53.535 0.400 . 1 . . . . 31 ASN CA . 11027 1 348 . 1 1 31 31 ASN HA H 1 4.861 0.020 . 1 . . . . 31 ASN HA . 11027 1 349 . 1 1 31 31 ASN CB C 13 40.290 0.400 . 1 . . . . 31 ASN CB . 11027 1 350 . 1 1 31 31 ASN HB2 H 1 3.775 0.020 . 2 . . . . 31 ASN HB2 . 11027 1 351 . 1 1 31 31 ASN HB3 H 1 2.892 0.020 . 2 . . . . 31 ASN HB3 . 11027 1 352 . 1 1 31 31 ASN C C 13 174.472 0.400 . 1 . . . . 31 ASN C . 11027 1 353 . 1 1 32 32 LYS N N 15 120.948 0.400 . 1 . . . . 32 LYS N . 11027 1 354 . 1 1 32 32 LYS H H 1 8.502 0.020 . 1 . . . . 32 LYS H . 11027 1 355 . 1 1 32 32 LYS CA C 13 58.193 0.400 . 1 . . . . 32 LYS CA . 11027 1 356 . 1 1 32 32 LYS HA H 1 4.269 0.020 . 1 . . . . 32 LYS HA . 11027 1 357 . 1 1 32 32 LYS CB C 13 32.575 0.400 . 1 . . . . 32 LYS CB . 11027 1 358 . 1 1 32 32 LYS HB2 H 1 1.848 0.020 . 2 . . . . 32 LYS HB2 . 11027 1 359 . 1 1 32 32 LYS HB3 H 1 1.778 0.020 . 2 . . . . 32 LYS HB3 . 11027 1 360 . 1 1 32 32 LYS CG C 13 23.721 0.400 . 1 . . . . 32 LYS CG . 11027 1 361 . 1 1 32 32 LYS HG2 H 1 1.438 0.020 . 2 . . . . 32 LYS HG2 . 11027 1 362 . 1 1 32 32 LYS HG3 H 1 1.438 0.020 . 2 . . . . 32 LYS HG3 . 11027 1 363 . 1 1 32 32 LYS CD C 13 28.973 0.400 . 1 . . . . 32 LYS CD . 11027 1 364 . 1 1 32 32 LYS HD2 H 1 1.697 0.020 . 2 . . . . 32 LYS HD2 . 11027 1 365 . 1 1 32 32 LYS HD3 H 1 1.697 0.020 . 2 . . . . 32 LYS HD3 . 11027 1 366 . 1 1 32 32 LYS CE C 13 42.246 0.400 . 1 . . . . 32 LYS CE . 11027 1 367 . 1 1 32 32 LYS HE2 H 1 2.981 0.020 . 2 . . . . 32 LYS HE2 . 11027 1 368 . 1 1 32 32 LYS HE3 H 1 2.981 0.020 . 2 . . . . 32 LYS HE3 . 11027 1 369 . 1 1 32 32 LYS C C 13 176.207 0.400 . 1 . . . . 32 LYS C . 11027 1 370 . 1 1 33 33 ASP N N 15 115.183 0.400 . 1 . . . . 33 ASP N . 11027 1 371 . 1 1 33 33 ASP H H 1 8.323 0.020 . 1 . . . . 33 ASP H . 11027 1 372 . 1 1 33 33 ASP CA C 13 55.644 0.400 . 1 . . . . 33 ASP CA . 11027 1 373 . 1 1 33 33 ASP HA H 1 4.539 0.020 . 1 . . . . 33 ASP HA . 11027 1 374 . 1 1 33 33 ASP CB C 13 43.199 0.400 . 1 . . . . 33 ASP CB . 11027 1 375 . 1 1 33 33 ASP HB2 H 1 2.750 0.020 . 2 . . . . 33 ASP HB2 . 11027 1 376 . 1 1 33 33 ASP HB3 H 1 1.964 0.020 . 2 . . . . 33 ASP HB3 . 11027 1 377 . 1 1 33 33 ASP C C 13 176.630 0.400 . 1 . . . . 33 ASP C . 11027 1 378 . 1 1 34 34 TRP N N 15 122.165 0.400 . 1 . . . . 34 TRP N . 11027 1 379 . 1 1 34 34 TRP H H 1 8.356 0.020 . 1 . . . . 34 TRP H . 11027 1 380 . 1 1 34 34 TRP CA C 13 55.791 0.400 . 1 . . . . 34 TRP CA . 11027 1 381 . 1 1 34 34 TRP HA H 1 5.145 0.020 . 1 . . . . 34 TRP HA . 11027 1 382 . 1 1 34 34 TRP CB C 13 32.648 0.400 . 1 . . . . 34 TRP CB . 11027 1 383 . 1 1 34 34 TRP HB2 H 1 2.925 0.020 . 2 . . . . 34 TRP HB2 . 11027 1 384 . 1 1 34 34 TRP HB3 H 1 2.852 0.020 . 2 . . . . 34 TRP HB3 . 11027 1 385 . 1 1 34 34 TRP CD1 C 13 127.468 0.400 . 1 . . . . 34 TRP CD1 . 11027 1 386 . 1 1 34 34 TRP CE3 C 13 119.448 0.400 . 1 . . . . 34 TRP CE3 . 11027 1 387 . 1 1 34 34 TRP NE1 N 15 127.314 0.400 . 1 . . . . 34 TRP NE1 . 11027 1 388 . 1 1 34 34 TRP HD1 H 1 6.972 0.020 . 1 . . . . 34 TRP HD1 . 11027 1 389 . 1 1 34 34 TRP HE3 H 1 7.076 0.020 . 1 . . . . 34 TRP HE3 . 11027 1 390 . 1 1 34 34 TRP CZ3 C 13 120.887 0.400 . 1 . . . . 34 TRP CZ3 . 11027 1 391 . 1 1 34 34 TRP CZ2 C 13 114.450 0.400 . 1 . . . . 34 TRP CZ2 . 11027 1 392 . 1 1 34 34 TRP HE1 H 1 9.144 0.020 . 1 . . . . 34 TRP HE1 . 11027 1 393 . 1 1 34 34 TRP HZ3 H 1 6.622 0.020 . 1 . . . . 34 TRP HZ3 . 11027 1 394 . 1 1 34 34 TRP CH2 C 13 124.256 0.400 . 1 . . . . 34 TRP CH2 . 11027 1 395 . 1 1 34 34 TRP HZ2 H 1 7.491 0.020 . 1 . . . . 34 TRP HZ2 . 11027 1 396 . 1 1 34 34 TRP HH2 H 1 7.208 0.020 . 1 . . . . 34 TRP HH2 . 11027 1 397 . 1 1 34 34 TRP C C 13 174.182 0.400 . 1 . . . . 34 TRP C . 11027 1 398 . 1 1 35 35 TRP N N 15 124.706 0.400 . 1 . . . . 35 TRP N . 11027 1 399 . 1 1 35 35 TRP H H 1 9.498 0.020 . 1 . . . . 35 TRP H . 11027 1 400 . 1 1 35 35 TRP CA C 13 53.899 0.400 . 1 . . . . 35 TRP CA . 11027 1 401 . 1 1 35 35 TRP HA H 1 5.531 0.020 . 1 . . . . 35 TRP HA . 11027 1 402 . 1 1 35 35 TRP CB C 13 31.483 0.400 . 1 . . . . 35 TRP CB . 11027 1 403 . 1 1 35 35 TRP HB2 H 1 2.983 0.020 . 2 . . . . 35 TRP HB2 . 11027 1 404 . 1 1 35 35 TRP HB3 H 1 2.828 0.020 . 2 . . . . 35 TRP HB3 . 11027 1 405 . 1 1 35 35 TRP CD1 C 13 125.239 0.400 . 1 . . . . 35 TRP CD1 . 11027 1 406 . 1 1 35 35 TRP CE3 C 13 121.683 0.400 . 1 . . . . 35 TRP CE3 . 11027 1 407 . 1 1 35 35 TRP NE1 N 15 129.359 0.400 . 1 . . . . 35 TRP NE1 . 11027 1 408 . 1 1 35 35 TRP HD1 H 1 7.582 0.020 . 1 . . . . 35 TRP HD1 . 11027 1 409 . 1 1 35 35 TRP HE3 H 1 7.082 0.020 . 1 . . . . 35 TRP HE3 . 11027 1 410 . 1 1 35 35 TRP CZ3 C 13 120.335 0.400 . 1 . . . . 35 TRP CZ3 . 11027 1 411 . 1 1 35 35 TRP CZ2 C 13 114.480 0.400 . 1 . . . . 35 TRP CZ2 . 11027 1 412 . 1 1 35 35 TRP HE1 H 1 9.291 0.020 . 1 . . . . 35 TRP HE1 . 11027 1 413 . 1 1 35 35 TRP HZ3 H 1 6.707 0.020 . 1 . . . . 35 TRP HZ3 . 11027 1 414 . 1 1 35 35 TRP CH2 C 13 124.734 0.400 . 1 . . . . 35 TRP CH2 . 11027 1 415 . 1 1 35 35 TRP HZ2 H 1 7.552 0.020 . 1 . . . . 35 TRP HZ2 . 11027 1 416 . 1 1 35 35 TRP HH2 H 1 7.217 0.020 . 1 . . . . 35 TRP HH2 . 11027 1 417 . 1 1 35 35 TRP C C 13 174.160 0.400 . 1 . . . . 35 TRP C . 11027 1 418 . 1 1 36 36 LYS N N 15 124.398 0.400 . 1 . . . . 36 LYS N . 11027 1 419 . 1 1 36 36 LYS H H 1 8.852 0.020 . 1 . . . . 36 LYS H . 11027 1 420 . 1 1 36 36 LYS CA C 13 55.500 0.400 . 1 . . . . 36 LYS CA . 11027 1 421 . 1 1 36 36 LYS HA H 1 4.361 0.020 . 1 . . . . 36 LYS HA . 11027 1 422 . 1 1 36 36 LYS CB C 13 34.322 0.400 . 1 . . . . 36 LYS CB . 11027 1 423 . 1 1 36 36 LYS HB2 H 1 1.655 0.020 . 2 . . . . 36 LYS HB2 . 11027 1 424 . 1 1 36 36 LYS HB3 H 1 1.655 0.020 . 2 . . . . 36 LYS HB3 . 11027 1 425 . 1 1 36 36 LYS CG C 13 25.140 0.400 . 1 . . . . 36 LYS CG . 11027 1 426 . 1 1 36 36 LYS HG2 H 1 1.434 0.020 . 2 . . . . 36 LYS HG2 . 11027 1 427 . 1 1 36 36 LYS HG3 H 1 1.340 0.020 . 2 . . . . 36 LYS HG3 . 11027 1 428 . 1 1 36 36 LYS CD C 13 28.689 0.400 . 1 . . . . 36 LYS CD . 11027 1 429 . 1 1 36 36 LYS CE C 13 41.749 0.400 . 1 . . . . 36 LYS CE . 11027 1 430 . 1 1 36 36 LYS HE2 H 1 2.974 0.020 . 2 . . . . 36 LYS HE2 . 11027 1 431 . 1 1 36 36 LYS HE3 H 1 2.974 0.020 . 2 . . . . 36 LYS HE3 . 11027 1 432 . 1 1 36 36 LYS C C 13 175.429 0.400 . 1 . . . . 36 LYS C . 11027 1 433 . 1 1 37 37 VAL N N 15 122.097 0.400 . 1 . . . . 37 VAL N . 11027 1 434 . 1 1 37 37 VAL H H 1 9.433 0.020 . 1 . . . . 37 VAL H . 11027 1 435 . 1 1 37 37 VAL CA C 13 59.207 0.400 . 1 . . . . 37 VAL CA . 11027 1 436 . 1 1 37 37 VAL HA H 1 5.363 0.020 . 1 . . . . 37 VAL HA . 11027 1 437 . 1 1 37 37 VAL CB C 13 36.794 0.400 . 1 . . . . 37 VAL CB . 11027 1 438 . 1 1 37 37 VAL HB H 1 2.125 0.020 . 1 . . . . 37 VAL HB . 11027 1 439 . 1 1 37 37 VAL HG11 H 1 0.835 0.020 . 2 . . . . 37 VAL HG1 . 11027 1 440 . 1 1 37 37 VAL HG12 H 1 0.835 0.020 . 2 . . . . 37 VAL HG1 . 11027 1 441 . 1 1 37 37 VAL HG13 H 1 0.835 0.020 . 2 . . . . 37 VAL HG1 . 11027 1 442 . 1 1 37 37 VAL HG21 H 1 0.750 0.020 . 2 . . . . 37 VAL HG2 . 11027 1 443 . 1 1 37 37 VAL HG22 H 1 0.750 0.020 . 2 . . . . 37 VAL HG2 . 11027 1 444 . 1 1 37 37 VAL HG23 H 1 0.750 0.020 . 2 . . . . 37 VAL HG2 . 11027 1 445 . 1 1 37 37 VAL CG1 C 13 21.307 0.400 . 1 . . . . 37 VAL CG1 . 11027 1 446 . 1 1 37 37 VAL CG2 C 13 18.539 0.400 . 1 . . . . 37 VAL CG2 . 11027 1 447 . 1 1 37 37 VAL C C 13 173.381 0.400 . 1 . . . . 37 VAL C . 11027 1 448 . 1 1 38 38 GLU N N 15 118.261 0.400 . 1 . . . . 38 GLU N . 11027 1 449 . 1 1 38 38 GLU H H 1 8.711 0.020 . 1 . . . . 38 GLU H . 11027 1 450 . 1 1 38 38 GLU CA C 13 54.046 0.400 . 1 . . . . 38 GLU CA . 11027 1 451 . 1 1 38 38 GLU HA H 1 5.383 0.020 . 1 . . . . 38 GLU HA . 11027 1 452 . 1 1 38 38 GLU CB C 13 32.357 0.400 . 1 . . . . 38 GLU CB . 11027 1 453 . 1 1 38 38 GLU HB2 H 1 1.867 0.020 . 2 . . . . 38 GLU HB2 . 11027 1 454 . 1 1 38 38 GLU HB3 H 1 1.867 0.020 . 2 . . . . 38 GLU HB3 . 11027 1 455 . 1 1 38 38 GLU CG C 13 33.661 0.400 . 1 . . . . 38 GLU CG . 11027 1 456 . 1 1 38 38 GLU HG2 H 1 2.196 0.020 . 2 . . . . 38 GLU HG2 . 11027 1 457 . 1 1 38 38 GLU HG3 H 1 2.196 0.020 . 2 . . . . 38 GLU HG3 . 11027 1 458 . 1 1 38 38 GLU C C 13 174.561 0.400 . 1 . . . . 38 GLU C . 11027 1 459 . 1 1 39 39 VAL N N 15 124.388 0.400 . 1 . . . . 39 VAL N . 11027 1 460 . 1 1 39 39 VAL H H 1 8.793 0.020 . 1 . . . . 39 VAL H . 11027 1 461 . 1 1 39 39 VAL CA C 13 60.959 0.400 . 1 . . . . 39 VAL CA . 11027 1 462 . 1 1 39 39 VAL HA H 1 4.476 0.020 . 1 . . . . 39 VAL HA . 11027 1 463 . 1 1 39 39 VAL CB C 13 33.521 0.400 . 1 . . . . 39 VAL CB . 11027 1 464 . 1 1 39 39 VAL HB H 1 2.106 0.020 . 1 . . . . 39 VAL HB . 11027 1 465 . 1 1 39 39 VAL HG11 H 1 1.037 0.020 . 2 . . . . 39 VAL HG1 . 11027 1 466 . 1 1 39 39 VAL HG12 H 1 1.037 0.020 . 2 . . . . 39 VAL HG1 . 11027 1 467 . 1 1 39 39 VAL HG13 H 1 1.037 0.020 . 2 . . . . 39 VAL HG1 . 11027 1 468 . 1 1 39 39 VAL HG21 H 1 0.960 0.020 . 2 . . . . 39 VAL HG2 . 11027 1 469 . 1 1 39 39 VAL HG22 H 1 0.960 0.020 . 2 . . . . 39 VAL HG2 . 11027 1 470 . 1 1 39 39 VAL HG23 H 1 0.960 0.020 . 2 . . . . 39 VAL HG2 . 11027 1 471 . 1 1 39 39 VAL CG1 C 13 20.810 0.400 . 1 . . . . 39 VAL CG1 . 11027 1 472 . 1 1 39 39 VAL CG2 C 13 18.823 0.400 . 1 . . . . 39 VAL CG2 . 11027 1 473 . 1 1 39 39 VAL C C 13 174.449 0.400 . 1 . . . . 39 VAL C . 11027 1 474 . 1 1 40 40 ASN N N 15 126.491 0.400 . 1 . . . . 40 ASN N . 11027 1 475 . 1 1 40 40 ASN H H 1 9.452 0.020 . 1 . . . . 40 ASN H . 11027 1 476 . 1 1 40 40 ASN CA C 13 55.355 0.400 . 1 . . . . 40 ASN CA . 11027 1 477 . 1 1 40 40 ASN HA H 1 4.295 0.020 . 1 . . . . 40 ASN HA . 11027 1 478 . 1 1 40 40 ASN CB C 13 37.306 0.400 . 1 . . . . 40 ASN CB . 11027 1 479 . 1 1 40 40 ASN HB2 H 1 3.020 0.020 . 2 . . . . 40 ASN HB2 . 11027 1 480 . 1 1 40 40 ASN HB3 H 1 2.853 0.020 . 2 . . . . 40 ASN HB3 . 11027 1 481 . 1 1 40 40 ASN C C 13 174.004 0.400 . 1 . . . . 40 ASN C . 11027 1 482 . 1 1 41 41 ASP N N 15 112.534 0.400 . 1 . . . . 41 ASP N . 11027 1 483 . 1 1 41 41 ASP H H 1 8.741 0.020 . 1 . . . . 41 ASP H . 11027 1 484 . 1 1 41 41 ASP CA C 13 54.986 0.400 . 1 . . . . 41 ASP CA . 11027 1 485 . 1 1 41 41 ASP HA H 1 4.411 0.020 . 1 . . . . 41 ASP HA . 11027 1 486 . 1 1 41 41 ASP CB C 13 38.688 0.400 . 1 . . . . 41 ASP CB . 11027 1 487 . 1 1 41 41 ASP HB2 H 1 2.950 0.020 . 2 . . . . 41 ASP HB2 . 11027 1 488 . 1 1 41 41 ASP HB3 H 1 2.950 0.020 . 2 . . . . 41 ASP HB3 . 11027 1 489 . 1 1 41 41 ASP C C 13 174.538 0.400 . 1 . . . . 41 ASP C . 11027 1 490 . 1 1 42 42 ARG N N 15 120.189 0.400 . 1 . . . . 42 ARG N . 11027 1 491 . 1 1 42 42 ARG H H 1 8.177 0.020 . 1 . . . . 42 ARG H . 11027 1 492 . 1 1 42 42 ARG CA C 13 55.282 0.400 . 1 . . . . 42 ARG CA . 11027 1 493 . 1 1 42 42 ARG HA H 1 4.630 0.020 . 1 . . . . 42 ARG HA . 11027 1 494 . 1 1 42 42 ARG CB C 13 32.211 0.400 . 1 . . . . 42 ARG CB . 11027 1 495 . 1 1 42 42 ARG HB2 H 1 1.926 0.020 . 2 . . . . 42 ARG HB2 . 11027 1 496 . 1 1 42 42 ARG HB3 H 1 1.784 0.020 . 2 . . . . 42 ARG HB3 . 11027 1 497 . 1 1 42 42 ARG CG C 13 26.702 0.400 . 1 . . . . 42 ARG CG . 11027 1 498 . 1 1 42 42 ARG HG2 H 1 1.655 0.020 . 2 . . . . 42 ARG HG2 . 11027 1 499 . 1 1 42 42 ARG HG3 H 1 1.655 0.020 . 2 . . . . 42 ARG HG3 . 11027 1 500 . 1 1 42 42 ARG CD C 13 43.240 0.400 . 1 . . . . 42 ARG CD . 11027 1 501 . 1 1 42 42 ARG HD2 H 1 3.265 0.020 . 2 . . . . 42 ARG HD2 . 11027 1 502 . 1 1 42 42 ARG HD3 H 1 3.265 0.020 . 2 . . . . 42 ARG HD3 . 11027 1 503 . 1 1 42 42 ARG C C 13 174.338 0.400 . 1 . . . . 42 ARG C . 11027 1 504 . 1 1 43 43 GLN N N 15 118.640 0.400 . 1 . . . . 43 GLN N . 11027 1 505 . 1 1 43 43 GLN H H 1 8.367 0.020 . 1 . . . . 43 GLN H . 11027 1 506 . 1 1 43 43 GLN CA C 13 53.751 0.400 . 1 . . . . 43 GLN CA . 11027 1 507 . 1 1 43 43 GLN HA H 1 5.454 0.020 . 1 . . . . 43 GLN HA . 11027 1 508 . 1 1 43 43 GLN CB C 13 31.701 0.400 . 1 . . . . 43 GLN CB . 11027 1 509 . 1 1 43 43 GLN HB2 H 1 1.835 0.020 . 2 . . . . 43 GLN HB2 . 11027 1 510 . 1 1 43 43 GLN HB3 H 1 1.694 0.020 . 2 . . . . 43 GLN HB3 . 11027 1 511 . 1 1 43 43 GLN CG C 13 33.720 0.400 . 1 . . . . 43 GLN CG . 11027 1 512 . 1 1 43 43 GLN HG2 H 1 2.273 0.020 . 2 . . . . 43 GLN HG2 . 11027 1 513 . 1 1 43 43 GLN HG3 H 1 2.080 0.020 . 2 . . . . 43 GLN HG3 . 11027 1 514 . 1 1 43 43 GLN C C 13 176.141 0.400 . 1 . . . . 43 GLN C . 11027 1 515 . 1 1 44 44 GLY N N 15 108.501 0.400 . 1 . . . . 44 GLY N . 11027 1 516 . 1 1 44 44 GLY H H 1 8.608 0.020 . 1 . . . . 44 GLY H . 11027 1 517 . 1 1 44 44 GLY CA C 13 45.238 0.400 . 1 . . . . 44 GLY CA . 11027 1 518 . 1 1 44 44 GLY HA2 H 1 3.999 0.020 . 2 . . . . 44 GLY HA2 . 11027 1 519 . 1 1 44 44 GLY HA3 H 1 3.870 0.020 . 2 . . . . 44 GLY HA3 . 11027 1 520 . 1 1 44 44 GLY C C 13 170.244 0.400 . 1 . . . . 44 GLY C . 11027 1 521 . 1 1 45 45 PHE N N 15 119.029 0.400 . 1 . . . . 45 PHE N . 11027 1 522 . 1 1 45 45 PHE H H 1 9.303 0.020 . 1 . . . . 45 PHE H . 11027 1 523 . 1 1 45 45 PHE CA C 13 58.553 0.400 . 1 . . . . 45 PHE CA . 11027 1 524 . 1 1 45 45 PHE HA H 1 5.634 0.020 . 1 . . . . 45 PHE HA . 11027 1 525 . 1 1 45 45 PHE CB C 13 42.835 0.400 . 1 . . . . 45 PHE CB . 11027 1 526 . 1 1 45 45 PHE HB2 H 1 2.994 0.020 . 2 . . . . 45 PHE HB2 . 11027 1 527 . 1 1 45 45 PHE HB3 H 1 2.557 0.020 . 2 . . . . 45 PHE HB3 . 11027 1 528 . 1 1 45 45 PHE CD1 C 13 131.510 0.400 . 1 . . . . 45 PHE CD1 . 11027 1 529 . 1 1 45 45 PHE HD1 H 1 7.020 0.020 . 1 . . . . 45 PHE HD1 . 11027 1 530 . 1 1 45 45 PHE CE1 C 13 129.577 0.400 . 1 . . . . 45 PHE CE1 . 11027 1 531 . 1 1 45 45 PHE HE1 H 1 7.323 0.020 . 1 . . . . 45 PHE HE1 . 11027 1 532 . 1 1 45 45 PHE CZ C 13 131.544 0.400 . 1 . . . . 45 PHE CZ . 11027 1 533 . 1 1 45 45 PHE HZ H 1 7.322 0.020 . 1 . . . . 45 PHE HZ . 11027 1 534 . 1 1 45 45 PHE CE2 C 13 129.577 0.400 . 1 . . . . 45 PHE CE2 . 11027 1 535 . 1 1 45 45 PHE HE2 H 1 7.323 0.020 . 1 . . . . 45 PHE HE2 . 11027 1 536 . 1 1 45 45 PHE CD2 C 13 131.510 0.400 . 1 . . . . 45 PHE CD2 . 11027 1 537 . 1 1 45 45 PHE HD2 H 1 7.020 0.020 . 1 . . . . 45 PHE HD2 . 11027 1 538 . 1 1 45 45 PHE C C 13 175.584 0.400 . 1 . . . . 45 PHE C . 11027 1 539 . 1 1 46 46 VAL N N 15 111.131 0.400 . 1 . . . . 46 VAL N . 11027 1 540 . 1 1 46 46 VAL H H 1 9.143 0.020 . 1 . . . . 46 VAL H . 11027 1 541 . 1 1 46 46 VAL CA C 13 57.829 0.400 . 1 . . . . 46 VAL CA . 11027 1 542 . 1 1 46 46 VAL HA H 1 4.844 0.020 . 1 . . . . 46 VAL HA . 11027 1 543 . 1 1 46 46 VAL CB C 13 33.376 0.400 . 1 . . . . 46 VAL CB . 11027 1 544 . 1 1 46 46 VAL HB H 1 1.817 0.020 . 1 . . . . 46 VAL HB . 11027 1 545 . 1 1 46 46 VAL HG11 H 1 0.698 0.020 . 2 . . . . 46 VAL HG1 . 11027 1 546 . 1 1 46 46 VAL HG12 H 1 0.698 0.020 . 2 . . . . 46 VAL HG1 . 11027 1 547 . 1 1 46 46 VAL HG13 H 1 0.698 0.020 . 2 . . . . 46 VAL HG1 . 11027 1 548 . 1 1 46 46 VAL HG21 H 1 1.094 0.020 . 2 . . . . 46 VAL HG2 . 11027 1 549 . 1 1 46 46 VAL HG22 H 1 1.094 0.020 . 2 . . . . 46 VAL HG2 . 11027 1 550 . 1 1 46 46 VAL HG23 H 1 1.094 0.020 . 2 . . . . 46 VAL HG2 . 11027 1 551 . 1 1 46 46 VAL CG1 C 13 17.123 0.400 . 1 . . . . 46 VAL CG1 . 11027 1 552 . 1 1 46 46 VAL CG2 C 13 22.105 0.400 . 1 . . . . 46 VAL CG2 . 11027 1 553 . 1 1 47 47 PRO CD C 13 49.846 0.400 . 1 . . . . 47 PRO CD . 11027 1 554 . 1 1 47 47 PRO CA C 13 61.541 0.400 . 1 . . . . 47 PRO CA . 11027 1 555 . 1 1 47 47 PRO HA H 1 3.851 0.020 . 1 . . . . 47 PRO HA . 11027 1 556 . 1 1 47 47 PRO CB C 13 29.418 0.400 . 1 . . . . 47 PRO CB . 11027 1 557 . 1 1 47 47 PRO HB2 H 1 1.143 0.020 . 2 . . . . 47 PRO HB2 . 11027 1 558 . 1 1 47 47 PRO HB3 H 1 1.080 0.020 . 2 . . . . 47 PRO HB3 . 11027 1 559 . 1 1 47 47 PRO CG C 13 27.213 0.400 . 1 . . . . 47 PRO CG . 11027 1 560 . 1 1 47 47 PRO HG2 H 1 0.379 0.020 . 2 . . . . 47 PRO HG2 . 11027 1 561 . 1 1 47 47 PRO HG3 H 1 0.624 0.020 . 2 . . . . 47 PRO HG3 . 11027 1 562 . 1 1 47 47 PRO HD2 H 1 2.458 0.020 . 2 . . . . 47 PRO HD2 . 11027 1 563 . 1 1 47 47 PRO HD3 H 1 2.286 0.020 . 2 . . . . 47 PRO HD3 . 11027 1 564 . 1 1 47 47 PRO C C 13 177.654 0.400 . 1 . . . . 47 PRO C . 11027 1 565 . 1 1 48 48 ALA N N 15 130.207 0.400 . 1 . . . . 48 ALA N . 11027 1 566 . 1 1 48 48 ALA H H 1 7.631 0.020 . 1 . . . . 48 ALA H . 11027 1 567 . 1 1 48 48 ALA CA C 13 54.554 0.400 . 1 . . . . 48 ALA CA . 11027 1 568 . 1 1 48 48 ALA HA H 1 2.643 0.020 . 1 . . . . 48 ALA HA . 11027 1 569 . 1 1 48 48 ALA HB1 H 1 -0.099 0.020 . 1 . . . . 48 ALA HB . 11027 1 570 . 1 1 48 48 ALA HB2 H 1 -0.099 0.020 . 1 . . . . 48 ALA HB . 11027 1 571 . 1 1 48 48 ALA HB3 H 1 -0.099 0.020 . 1 . . . . 48 ALA HB . 11027 1 572 . 1 1 48 48 ALA CB C 13 15.256 0.400 . 1 . . . . 48 ALA CB . 11027 1 573 . 1 1 48 48 ALA C C 13 178.744 0.400 . 1 . . . . 48 ALA C . 11027 1 574 . 1 1 49 49 ALA N N 15 113.960 0.400 . 1 . . . . 49 ALA N . 11027 1 575 . 1 1 49 49 ALA H H 1 8.389 0.020 . 1 . . . . 49 ALA H . 11027 1 576 . 1 1 49 49 ALA CA C 13 52.805 0.400 . 1 . . . . 49 ALA CA . 11027 1 577 . 1 1 49 49 ALA HA H 1 4.063 0.020 . 1 . . . . 49 ALA HA . 11027 1 578 . 1 1 49 49 ALA HB1 H 1 1.243 0.020 . 1 . . . . 49 ALA HB . 11027 1 579 . 1 1 49 49 ALA HB2 H 1 1.243 0.020 . 1 . . . . 49 ALA HB . 11027 1 580 . 1 1 49 49 ALA HB3 H 1 1.243 0.020 . 1 . . . . 49 ALA HB . 11027 1 581 . 1 1 49 49 ALA CB C 13 17.727 0.400 . 1 . . . . 49 ALA CB . 11027 1 582 . 1 1 49 49 ALA C C 13 177.342 0.400 . 1 . . . . 49 ALA C . 11027 1 583 . 1 1 50 50 TYR N N 15 116.306 0.400 . 1 . . . . 50 TYR N . 11027 1 584 . 1 1 50 50 TYR H H 1 7.830 0.020 . 1 . . . . 50 TYR H . 11027 1 585 . 1 1 50 50 TYR CA C 13 57.462 0.400 . 1 . . . . 50 TYR CA . 11027 1 586 . 1 1 50 50 TYR HA H 1 4.681 0.020 . 1 . . . . 50 TYR HA . 11027 1 587 . 1 1 50 50 TYR CB C 13 37.390 0.400 . 1 . . . . 50 TYR CB . 11027 1 588 . 1 1 50 50 TYR HB2 H 1 3.330 0.020 . 2 . . . . 50 TYR HB2 . 11027 1 589 . 1 1 50 50 TYR HB3 H 1 3.086 0.020 . 2 . . . . 50 TYR HB3 . 11027 1 590 . 1 1 50 50 TYR CD1 C 13 130.736 0.400 . 1 . . . . 50 TYR CD1 . 11027 1 591 . 1 1 50 50 TYR HD1 H 1 6.828 0.020 . 1 . . . . 50 TYR HD1 . 11027 1 592 . 1 1 50 50 TYR CE1 C 13 118.560 0.400 . 1 . . . . 50 TYR CE1 . 11027 1 593 . 1 1 50 50 TYR HE1 H 1 6.782 0.020 . 1 . . . . 50 TYR HE1 . 11027 1 594 . 1 1 50 50 TYR CE2 C 13 118.560 0.400 . 1 . . . . 50 TYR CE2 . 11027 1 595 . 1 1 50 50 TYR HE2 H 1 6.782 0.020 . 1 . . . . 50 TYR HE2 . 11027 1 596 . 1 1 50 50 TYR CD2 C 13 130.736 0.400 . 1 . . . . 50 TYR CD2 . 11027 1 597 . 1 1 50 50 TYR HD2 H 1 6.828 0.020 . 1 . . . . 50 TYR HD2 . 11027 1 598 . 1 1 50 50 TYR C C 13 174.538 0.400 . 1 . . . . 50 TYR C . 11027 1 599 . 1 1 51 51 VAL N N 15 110.732 0.400 . 1 . . . . 51 VAL N . 11027 1 600 . 1 1 51 51 VAL H H 1 7.472 0.020 . 1 . . . . 51 VAL H . 11027 1 601 . 1 1 51 51 VAL CA C 13 58.118 0.400 . 1 . . . . 51 VAL CA . 11027 1 602 . 1 1 51 51 VAL HA H 1 5.531 0.020 . 1 . . . . 51 VAL HA . 11027 1 603 . 1 1 51 51 VAL CB C 13 36.377 0.400 . 1 . . . . 51 VAL CB . 11027 1 604 . 1 1 51 51 VAL HB H 1 1.936 0.020 . 1 . . . . 51 VAL HB . 11027 1 605 . 1 1 51 51 VAL HG11 H 1 0.750 0.020 . 2 . . . . 51 VAL HG1 . 11027 1 606 . 1 1 51 51 VAL HG12 H 1 0.750 0.020 . 2 . . . . 51 VAL HG1 . 11027 1 607 . 1 1 51 51 VAL HG13 H 1 0.750 0.020 . 2 . . . . 51 VAL HG1 . 11027 1 608 . 1 1 51 51 VAL HG21 H 1 0.750 0.020 . 2 . . . . 51 VAL HG2 . 11027 1 609 . 1 1 51 51 VAL HG22 H 1 0.750 0.020 . 2 . . . . 51 VAL HG2 . 11027 1 610 . 1 1 51 51 VAL HG23 H 1 0.750 0.020 . 2 . . . . 51 VAL HG2 . 11027 1 611 . 1 1 51 51 VAL CG1 C 13 21.676 0.400 . 1 . . . . 51 VAL CG1 . 11027 1 612 . 1 1 51 51 VAL CG2 C 13 18.546 0.400 . 1 . . . . 51 VAL CG2 . 11027 1 613 . 1 1 51 51 VAL C C 13 173.381 0.400 . 1 . . . . 51 VAL C . 11027 1 614 . 1 1 52 52 LYS N N 15 118.323 0.400 . 1 . . . . 52 LYS N . 11027 1 615 . 1 1 52 52 LYS H H 1 8.697 0.020 . 1 . . . . 52 LYS H . 11027 1 616 . 1 1 52 52 LYS CA C 13 54.062 0.400 . 1 . . . . 52 LYS CA . 11027 1 617 . 1 1 52 52 LYS HA H 1 4.831 0.020 . 1 . . . . 52 LYS HA . 11027 1 618 . 1 1 52 52 LYS CB C 13 36.814 0.400 . 1 . . . . 52 LYS CB . 11027 1 619 . 1 1 52 52 LYS HB2 H 1 1.728 0.020 . 2 . . . . 52 LYS HB2 . 11027 1 620 . 1 1 52 52 LYS HB3 H 1 1.728 0.020 . 2 . . . . 52 LYS HB3 . 11027 1 621 . 1 1 52 52 LYS CG C 13 23.932 0.400 . 1 . . . . 52 LYS CG . 11027 1 622 . 1 1 52 52 LYS HG2 H 1 1.439 0.020 . 2 . . . . 52 LYS HG2 . 11027 1 623 . 1 1 52 52 LYS HG3 H 1 1.382 0.020 . 2 . . . . 52 LYS HG3 . 11027 1 624 . 1 1 52 52 LYS CD C 13 29.245 0.400 . 1 . . . . 52 LYS CD . 11027 1 625 . 1 1 52 52 LYS HD2 H 1 1.634 0.020 . 2 . . . . 52 LYS HD2 . 11027 1 626 . 1 1 52 52 LYS HD3 H 1 1.634 0.020 . 2 . . . . 52 LYS HD3 . 11027 1 627 . 1 1 52 52 LYS HE2 H 1 2.953 0.020 . 2 . . . . 52 LYS HE2 . 11027 1 628 . 1 1 52 52 LYS HE3 H 1 2.953 0.020 . 2 . . . . 52 LYS HE3 . 11027 1 629 . 1 1 52 52 LYS C C 13 175.851 0.400 . 1 . . . . 52 LYS C . 11027 1 630 . 1 1 53 53 LYS N N 15 125.862 0.400 . 1 . . . . 53 LYS N . 11027 1 631 . 1 1 53 53 LYS H H 1 9.191 0.020 . 1 . . . . 53 LYS H . 11027 1 632 . 1 1 53 53 LYS CA C 13 58.266 0.400 . 1 . . . . 53 LYS CA . 11027 1 633 . 1 1 53 53 LYS HA H 1 4.539 0.020 . 1 . . . . 53 LYS HA . 11027 1 634 . 1 1 53 53 LYS CB C 13 33.012 0.400 . 1 . . . . 53 LYS CB . 11027 1 635 . 1 1 53 53 LYS HB2 H 1 1.698 0.020 . 2 . . . . 53 LYS HB2 . 11027 1 636 . 1 1 53 53 LYS HB3 H 1 1.829 0.020 . 2 . . . . 53 LYS HB3 . 11027 1 637 . 1 1 53 53 LYS CG C 13 25.495 0.400 . 1 . . . . 53 LYS CG . 11027 1 638 . 1 1 53 53 LYS HG2 H 1 1.413 0.020 . 2 . . . . 53 LYS HG2 . 11027 1 639 . 1 1 53 53 LYS HG3 H 1 1.413 0.020 . 2 . . . . 53 LYS HG3 . 11027 1 640 . 1 1 53 53 LYS CD C 13 29.257 0.400 . 1 . . . . 53 LYS CD . 11027 1 641 . 1 1 53 53 LYS CE C 13 42.814 0.400 . 1 . . . . 53 LYS CE . 11027 1 642 . 1 1 53 53 LYS HE2 H 1 2.982 0.020 . 2 . . . . 53 LYS HE2 . 11027 1 643 . 1 1 53 53 LYS HE3 H 1 2.982 0.020 . 2 . . . . 53 LYS HE3 . 11027 1 644 . 1 1 53 53 LYS C C 13 176.029 0.400 . 1 . . . . 53 LYS C . 11027 1 645 . 1 1 54 54 LEU N N 15 125.645 0.400 . 1 . . . . 54 LEU N . 11027 1 646 . 1 1 54 54 LEU H H 1 8.390 0.020 . 1 . . . . 54 LEU H . 11027 1 647 . 1 1 54 54 LEU CA C 13 53.826 0.400 . 1 . . . . 54 LEU CA . 11027 1 648 . 1 1 54 54 LEU HA H 1 4.565 0.020 . 1 . . . . 54 LEU HA . 11027 1 649 . 1 1 54 54 LEU CB C 13 43.565 0.400 . 1 . . . . 54 LEU CB . 11027 1 650 . 1 1 54 54 LEU HB2 H 1 1.566 0.020 . 2 . . . . 54 LEU HB2 . 11027 1 651 . 1 1 54 54 LEU HB3 H 1 1.566 0.020 . 2 . . . . 54 LEU HB3 . 11027 1 652 . 1 1 54 54 LEU CG C 13 26.347 0.400 . 1 . . . . 54 LEU CG . 11027 1 653 . 1 1 54 54 LEU HG H 1 1.490 0.020 . 1 . . . . 54 LEU HG . 11027 1 654 . 1 1 54 54 LEU HD11 H 1 0.852 0.020 . 2 . . . . 54 LEU HD1 . 11027 1 655 . 1 1 54 54 LEU HD12 H 1 0.852 0.020 . 2 . . . . 54 LEU HD1 . 11027 1 656 . 1 1 54 54 LEU HD13 H 1 0.852 0.020 . 2 . . . . 54 LEU HD1 . 11027 1 657 . 1 1 54 54 LEU HD21 H 1 0.852 0.020 . 2 . . . . 54 LEU HD2 . 11027 1 658 . 1 1 54 54 LEU HD22 H 1 0.852 0.020 . 2 . . . . 54 LEU HD2 . 11027 1 659 . 1 1 54 54 LEU HD23 H 1 0.852 0.020 . 2 . . . . 54 LEU HD2 . 11027 1 660 . 1 1 54 54 LEU CD1 C 13 22.514 0.400 . 1 . . . . 54 LEU CD1 . 11027 1 661 . 1 1 54 54 LEU C C 13 176.630 0.400 . 1 . . . . 54 LEU C . 11027 1 662 . 1 1 55 55 ASP N N 15 121.805 0.400 . 1 . . . . 55 ASP N . 11027 1 663 . 1 1 55 55 ASP H H 1 8.631 0.020 . 1 . . . . 55 ASP H . 11027 1 664 . 1 1 55 55 ASP CA C 13 53.899 0.400 . 1 . . . . 55 ASP CA . 11027 1 665 . 1 1 55 55 ASP HA H 1 4.784 0.020 . 1 . . . . 55 ASP HA . 11027 1 666 . 1 1 55 55 ASP CB C 13 39.999 0.400 . 1 . . . . 55 ASP CB . 11027 1 667 . 1 1 55 55 ASP HB2 H 1 2.827 0.020 . 2 . . . . 55 ASP HB2 . 11027 1 668 . 1 1 55 55 ASP HB3 H 1 2.686 0.020 . 2 . . . . 55 ASP HB3 . 11027 1 669 . 1 1 55 55 ASP C C 13 175.718 0.400 . 1 . . . . 55 ASP C . 11027 1 670 . 1 1 56 56 SER N N 15 116.751 0.400 . 1 . . . . 56 SER N . 11027 1 671 . 1 1 56 56 SER H H 1 8.370 0.020 . 1 . . . . 56 SER H . 11027 1 672 . 1 1 56 56 SER CA C 13 58.118 0.400 . 1 . . . . 56 SER CA . 11027 1 673 . 1 1 56 56 SER HA H 1 4.552 0.020 . 1 . . . . 56 SER HA . 11027 1 674 . 1 1 56 56 SER CB C 13 64.523 0.400 . 1 . . . . 56 SER CB . 11027 1 675 . 1 1 56 56 SER HB2 H 1 3.961 0.020 . 2 . . . . 56 SER HB2 . 11027 1 676 . 1 1 56 56 SER HB3 H 1 3.814 0.020 . 2 . . . . 56 SER HB3 . 11027 1 677 . 1 1 56 56 SER HG H 1 5.042 0.020 . 1 . . . . 56 SER HG . 11027 1 678 . 1 1 56 56 SER C C 13 175.184 0.400 . 1 . . . . 56 SER C . 11027 1 679 . 1 1 57 57 GLY N N 15 111.683 0.400 . 1 . . . . 57 GLY N . 11027 1 680 . 1 1 57 57 GLY H H 1 8.656 0.020 . 1 . . . . 57 GLY H . 11027 1 681 . 1 1 57 57 GLY CA C 13 45.301 0.400 . 1 . . . . 57 GLY CA . 11027 1 682 . 1 1 57 57 GLY HA2 H 1 4.052 0.020 . 2 . . . . 57 GLY HA2 . 11027 1 683 . 1 1 57 57 GLY HA3 H 1 4.052 0.020 . 2 . . . . 57 GLY HA3 . 11027 1 684 . 1 1 57 57 GLY C C 13 174.605 0.400 . 1 . . . . 57 GLY C . 11027 1 685 . 1 1 58 58 THR N N 15 111.906 0.400 . 1 . . . . 58 THR N . 11027 1 686 . 1 1 58 58 THR H H 1 8.181 0.020 . 1 . . . . 58 THR H . 11027 1 687 . 1 1 58 58 THR CA C 13 61.780 0.400 . 1 . . . . 58 THR CA . 11027 1 688 . 1 1 58 58 THR HA H 1 4.409 0.020 . 1 . . . . 58 THR HA . 11027 1 689 . 1 1 58 58 THR CB C 13 69.843 0.400 . 1 . . . . 58 THR CB . 11027 1 690 . 1 1 58 58 THR HB H 1 4.366 0.020 . 1 . . . . 58 THR HB . 11027 1 691 . 1 1 58 58 THR HG21 H 1 1.184 0.020 . 1 . . . . 58 THR HG2 . 11027 1 692 . 1 1 58 58 THR HG22 H 1 1.184 0.020 . 1 . . . . 58 THR HG2 . 11027 1 693 . 1 1 58 58 THR HG23 H 1 1.184 0.020 . 1 . . . . 58 THR HG2 . 11027 1 694 . 1 1 58 58 THR CG2 C 13 21.307 0.400 . 1 . . . . 58 THR CG2 . 11027 1 695 . 1 1 58 58 THR C C 13 175.251 0.400 . 1 . . . . 58 THR C . 11027 1 696 . 1 1 59 59 GLY N N 15 110.941 0.400 . 1 . . . . 59 GLY N . 11027 1 697 . 1 1 59 59 GLY H H 1 8.449 0.020 . 1 . . . . 59 GLY H . 11027 1 698 . 1 1 59 59 GLY CA C 13 45.093 0.400 . 1 . . . . 59 GLY CA . 11027 1 699 . 1 1 59 59 GLY HA2 H 1 4.100 0.020 . 2 . . . . 59 GLY HA2 . 11027 1 700 . 1 1 59 59 GLY HA3 H 1 3.862 0.020 . 2 . . . . 59 GLY HA3 . 11027 1 701 . 1 1 59 59 GLY C C 13 173.693 0.400 . 1 . . . . 59 GLY C . 11027 1 702 . 1 1 60 60 LYS N N 15 120.070 0.400 . 1 . . . . 60 LYS N . 11027 1 703 . 1 1 60 60 LYS H H 1 7.738 0.020 . 1 . . . . 60 LYS H . 11027 1 704 . 1 1 60 60 LYS CA C 13 55.791 0.400 . 1 . . . . 60 LYS CA . 11027 1 705 . 1 1 60 60 LYS HA H 1 4.333 0.020 . 1 . . . . 60 LYS HA . 11027 1 706 . 1 1 60 60 LYS CB C 13 33.303 0.400 . 1 . . . . 60 LYS CB . 11027 1 707 . 1 1 60 60 LYS HB2 H 1 1.765 0.020 . 2 . . . . 60 LYS HB2 . 11027 1 708 . 1 1 60 60 LYS HB3 H 1 1.765 0.020 . 2 . . . . 60 LYS HB3 . 11027 1 709 . 1 1 60 60 LYS CG C 13 24.005 0.400 . 1 . . . . 60 LYS CG . 11027 1 710 . 1 1 60 60 LYS HG2 H 1 1.333 0.020 . 2 . . . . 60 LYS HG2 . 11027 1 711 . 1 1 60 60 LYS HG3 H 1 1.333 0.020 . 2 . . . . 60 LYS HG3 . 11027 1 712 . 1 1 60 60 LYS CD C 13 28.902 0.400 . 1 . . . . 60 LYS CD . 11027 1 713 . 1 1 60 60 LYS HD2 H 1 1.629 0.020 . 2 . . . . 60 LYS HD2 . 11027 1 714 . 1 1 60 60 LYS HD3 H 1 1.629 0.020 . 2 . . . . 60 LYS HD3 . 11027 1 715 . 1 1 60 60 LYS CE C 13 42.033 0.400 . 1 . . . . 60 LYS CE . 11027 1 716 . 1 1 60 60 LYS HE2 H 1 2.948 0.020 . 2 . . . . 60 LYS HE2 . 11027 1 717 . 1 1 60 60 LYS HE3 H 1 2.948 0.020 . 2 . . . . 60 LYS HE3 . 11027 1 718 . 1 1 60 60 LYS C C 13 175.429 0.400 . 1 . . . . 60 LYS C . 11027 1 719 . 1 1 61 61 GLU N N 15 122.891 0.400 . 1 . . . . 61 GLU N . 11027 1 720 . 1 1 61 61 GLU H H 1 8.686 0.020 . 1 . . . . 61 GLU H . 11027 1 721 . 1 1 61 61 GLU CA C 13 55.719 0.400 . 1 . . . . 61 GLU CA . 11027 1 722 . 1 1 61 61 GLU HA H 1 4.514 0.020 . 1 . . . . 61 GLU HA . 11027 1 723 . 1 1 61 61 GLU CB C 13 29.586 0.400 . 1 . . . . 61 GLU CB . 11027 1 724 . 1 1 61 61 GLU HB2 H 1 2.091 0.020 . 2 . . . . 61 GLU HB2 . 11027 1 725 . 1 1 61 61 GLU HB3 H 1 2.091 0.020 . 2 . . . . 61 GLU HB3 . 11027 1 726 . 1 1 61 61 GLU CG C 13 33.941 0.400 . 1 . . . . 61 GLU CG . 11027 1 727 . 1 1 61 61 GLU HG2 H 1 2.302 0.020 . 2 . . . . 61 GLU HG2 . 11027 1 728 . 1 1 61 61 GLU HG3 H 1 2.434 0.020 . 2 . . . . 61 GLU HG3 . 11027 1 729 . 1 1 61 61 GLU C C 13 174.338 0.400 . 1 . . . . 61 GLU C . 11027 1 730 . 1 1 62 62 LEU N N 15 123.976 0.400 . 1 . . . . 62 LEU N . 11027 1 731 . 1 1 62 62 LEU H H 1 8.489 0.020 . 1 . . . . 62 LEU H . 11027 1 732 . 1 1 62 62 LEU CA C 13 53.390 0.400 . 1 . . . . 62 LEU CA . 11027 1 733 . 1 1 62 62 LEU HA H 1 5.402 0.020 . 1 . . . . 62 LEU HA . 11027 1 734 . 1 1 62 62 LEU CB C 13 46.185 0.400 . 1 . . . . 62 LEU CB . 11027 1 735 . 1 1 62 62 LEU HB2 H 1 1.703 0.020 . 2 . . . . 62 LEU HB2 . 11027 1 736 . 1 1 62 62 LEU HB3 H 1 1.382 0.020 . 2 . . . . 62 LEU HB3 . 11027 1 737 . 1 1 62 62 LEU CG C 13 25.495 0.400 . 1 . . . . 62 LEU CG . 11027 1 738 . 1 1 62 62 LEU HG H 1 1.573 0.020 . 1 . . . . 62 LEU HG . 11027 1 739 . 1 1 62 62 LEU HD11 H 1 0.830 0.020 . 2 . . . . 62 LEU HD1 . 11027 1 740 . 1 1 62 62 LEU HD12 H 1 0.830 0.020 . 2 . . . . 62 LEU HD1 . 11027 1 741 . 1 1 62 62 LEU HD13 H 1 0.830 0.020 . 2 . . . . 62 LEU HD1 . 11027 1 742 . 1 1 62 62 LEU HD21 H 1 0.795 0.020 . 2 . . . . 62 LEU HD2 . 11027 1 743 . 1 1 62 62 LEU HD22 H 1 0.795 0.020 . 2 . . . . 62 LEU HD2 . 11027 1 744 . 1 1 62 62 LEU HD23 H 1 0.795 0.020 . 2 . . . . 62 LEU HD2 . 11027 1 745 . 1 1 62 62 LEU CD1 C 13 22.585 0.400 . 1 . . . . 62 LEU CD1 . 11027 1 746 . 1 1 62 62 LEU CD2 C 13 22.500 0.400 . 1 . . . . 62 LEU CD2 . 11027 1 747 . 1 1 62 62 LEU C C 13 177.097 0.400 . 1 . . . . 62 LEU C . 11027 1 748 . 1 1 63 63 VAL N N 15 111.328 0.400 . 1 . . . . 63 VAL N . 11027 1 749 . 1 1 63 63 VAL H H 1 9.149 0.020 . 1 . . . . 63 VAL H . 11027 1 750 . 1 1 63 63 VAL CA C 13 57.902 0.400 . 1 . . . . 63 VAL CA . 11027 1 751 . 1 1 63 63 VAL HA H 1 5.262 0.020 . 1 . . . . 63 VAL HA . 11027 1 752 . 1 1 63 63 VAL CB C 13 35.920 0.400 . 1 . . . . 63 VAL CB . 11027 1 753 . 1 1 63 63 VAL HB H 1 2.006 0.020 . 1 . . . . 63 VAL HB . 11027 1 754 . 1 1 63 63 VAL HG11 H 1 1.073 0.020 . 2 . . . . 63 VAL HG1 . 11027 1 755 . 1 1 63 63 VAL HG12 H 1 1.073 0.020 . 2 . . . . 63 VAL HG1 . 11027 1 756 . 1 1 63 63 VAL HG13 H 1 1.073 0.020 . 2 . . . . 63 VAL HG1 . 11027 1 757 . 1 1 63 63 VAL HG21 H 1 0.821 0.020 . 2 . . . . 63 VAL HG2 . 11027 1 758 . 1 1 63 63 VAL HG22 H 1 0.821 0.020 . 2 . . . . 63 VAL HG2 . 11027 1 759 . 1 1 63 63 VAL HG23 H 1 0.821 0.020 . 2 . . . . 63 VAL HG2 . 11027 1 760 . 1 1 63 63 VAL CG1 C 13 23.508 0.400 . 1 . . . . 63 VAL CG1 . 11027 1 761 . 1 1 63 63 VAL CG2 C 13 19.604 0.400 . 1 . . . . 63 VAL CG2 . 11027 1 762 . 1 1 63 63 VAL C C 13 172.402 0.400 . 1 . . . . 63 VAL C . 11027 1 763 . 1 1 64 64 LEU N N 15 123.325 0.400 . 1 . . . . 64 LEU N . 11027 1 764 . 1 1 64 64 LEU H H 1 8.976 0.020 . 1 . . . . 64 LEU H . 11027 1 765 . 1 1 64 64 LEU CA C 13 52.225 0.400 . 1 . . . . 64 LEU CA . 11027 1 766 . 1 1 64 64 LEU HA H 1 5.132 0.020 . 1 . . . . 64 LEU HA . 11027 1 767 . 1 1 64 64 LEU CB C 13 46.840 0.400 . 1 . . . . 64 LEU CB . 11027 1 768 . 1 1 64 64 LEU HB2 H 1 1.707 0.020 . 2 . . . . 64 LEU HB2 . 11027 1 769 . 1 1 64 64 LEU HB3 H 1 1.372 0.020 . 2 . . . . 64 LEU HB3 . 11027 1 770 . 1 1 64 64 LEU CG C 13 26.418 0.400 . 1 . . . . 64 LEU CG . 11027 1 771 . 1 1 64 64 LEU HG H 1 1.241 0.020 . 1 . . . . 64 LEU HG . 11027 1 772 . 1 1 64 64 LEU HD11 H 1 0.842 0.020 . 2 . . . . 64 LEU HD1 . 11027 1 773 . 1 1 64 64 LEU HD12 H 1 0.842 0.020 . 2 . . . . 64 LEU HD1 . 11027 1 774 . 1 1 64 64 LEU HD13 H 1 0.842 0.020 . 2 . . . . 64 LEU HD1 . 11027 1 775 . 1 1 64 64 LEU HD21 H 1 0.807 0.020 . 2 . . . . 64 LEU HD2 . 11027 1 776 . 1 1 64 64 LEU HD22 H 1 0.807 0.020 . 2 . . . . 64 LEU HD2 . 11027 1 777 . 1 1 64 64 LEU HD23 H 1 0.807 0.020 . 2 . . . . 64 LEU HD2 . 11027 1 778 . 1 1 64 64 LEU CD1 C 13 23.508 0.400 . 1 . . . . 64 LEU CD1 . 11027 1 779 . 1 1 64 64 LEU C C 13 176.519 0.400 . 1 . . . . 64 LEU C . 11027 1 780 . 1 1 65 65 ALA N N 15 127.315 0.400 . 1 . . . . 65 ALA N . 11027 1 781 . 1 1 65 65 ALA H H 1 9.215 0.020 . 1 . . . . 65 ALA H . 11027 1 782 . 1 1 65 65 ALA CA C 13 52.513 0.400 . 1 . . . . 65 ALA CA . 11027 1 783 . 1 1 65 65 ALA HA H 1 4.552 0.020 . 1 . . . . 65 ALA HA . 11027 1 784 . 1 1 65 65 ALA HB1 H 1 1.669 0.020 . 1 . . . . 65 ALA HB . 11027 1 785 . 1 1 65 65 ALA HB2 H 1 1.669 0.020 . 1 . . . . 65 ALA HB . 11027 1 786 . 1 1 65 65 ALA HB3 H 1 1.669 0.020 . 1 . . . . 65 ALA HB . 11027 1 787 . 1 1 65 65 ALA CB C 13 19.254 0.400 . 1 . . . . 65 ALA CB . 11027 1 788 . 1 1 65 65 ALA C C 13 178.232 0.400 . 1 . . . . 65 ALA C . 11027 1 789 . 1 1 66 66 LEU N N 15 127.760 0.400 . 1 . . . . 66 LEU N . 11027 1 790 . 1 1 66 66 LEU H H 1 9.292 0.020 . 1 . . . . 66 LEU H . 11027 1 791 . 1 1 66 66 LEU CA C 13 55.683 0.400 . 1 . . . . 66 LEU CA . 11027 1 792 . 1 1 66 66 LEU HA H 1 3.917 0.020 . 1 . . . . 66 LEU HA . 11027 1 793 . 1 1 66 66 LEU CB C 13 43.863 0.400 . 1 . . . . 66 LEU CB . 11027 1 794 . 1 1 66 66 LEU HB2 H 1 1.280 0.020 . 2 . . . . 66 LEU HB2 . 11027 1 795 . 1 1 66 66 LEU HB3 H 1 0.724 0.020 . 2 . . . . 66 LEU HB3 . 11027 1 796 . 1 1 66 66 LEU CG C 13 26.428 0.400 . 1 . . . . 66 LEU CG . 11027 1 797 . 1 1 66 66 LEU HG H 1 1.406 0.020 . 1 . . . . 66 LEU HG . 11027 1 798 . 1 1 66 66 LEU HD11 H 1 0.694 0.020 . 2 . . . . 66 LEU HD1 . 11027 1 799 . 1 1 66 66 LEU HD12 H 1 0.694 0.020 . 2 . . . . 66 LEU HD1 . 11027 1 800 . 1 1 66 66 LEU HD13 H 1 0.694 0.020 . 2 . . . . 66 LEU HD1 . 11027 1 801 . 1 1 66 66 LEU HD21 H 1 0.624 0.020 . 2 . . . . 66 LEU HD2 . 11027 1 802 . 1 1 66 66 LEU HD22 H 1 0.624 0.020 . 2 . . . . 66 LEU HD2 . 11027 1 803 . 1 1 66 66 LEU HD23 H 1 0.624 0.020 . 2 . . . . 66 LEU HD2 . 11027 1 804 . 1 1 66 66 LEU CD1 C 13 24.988 0.400 . 1 . . . . 66 LEU CD1 . 11027 1 805 . 1 1 66 66 LEU CD2 C 13 21.510 0.400 . 1 . . . . 66 LEU CD2 . 11027 1 806 . 1 1 66 66 LEU C C 13 173.376 0.400 . 1 . . . . 66 LEU C . 11027 1 807 . 1 1 67 67 TYR N N 15 111.780 0.400 . 1 . . . . 67 TYR N . 11027 1 808 . 1 1 67 67 TYR H H 1 7.190 0.020 . 1 . . . . 67 TYR H . 11027 1 809 . 1 1 67 67 TYR CA C 13 54.649 0.400 . 1 . . . . 67 TYR CA . 11027 1 810 . 1 1 67 67 TYR HA H 1 4.575 0.020 . 1 . . . . 67 TYR HA . 11027 1 811 . 1 1 67 67 TYR CB C 13 42.903 0.400 . 1 . . . . 67 TYR CB . 11027 1 812 . 1 1 67 67 TYR HB2 H 1 3.097 0.020 . 2 . . . . 67 TYR HB2 . 11027 1 813 . 1 1 67 67 TYR HB3 H 1 2.177 0.020 . 2 . . . . 67 TYR HB3 . 11027 1 814 . 1 1 67 67 TYR CD1 C 13 133.795 0.400 . 1 . . . . 67 TYR CD1 . 11027 1 815 . 1 1 67 67 TYR HD1 H 1 6.734 0.020 . 1 . . . . 67 TYR HD1 . 11027 1 816 . 1 1 67 67 TYR CE1 C 13 117.392 0.400 . 1 . . . . 67 TYR CE1 . 11027 1 817 . 1 1 67 67 TYR HE1 H 1 6.573 0.020 . 1 . . . . 67 TYR HE1 . 11027 1 818 . 1 1 67 67 TYR CE2 C 13 117.392 0.400 . 1 . . . . 67 TYR CE2 . 11027 1 819 . 1 1 67 67 TYR HE2 H 1 6.573 0.020 . 1 . . . . 67 TYR HE2 . 11027 1 820 . 1 1 67 67 TYR CD2 C 13 133.795 0.400 . 1 . . . . 67 TYR CD2 . 11027 1 821 . 1 1 67 67 TYR HD2 H 1 6.734 0.020 . 1 . . . . 67 TYR HD2 . 11027 1 822 . 1 1 67 67 TYR C C 13 173.353 0.400 . 1 . . . . 67 TYR C . 11027 1 823 . 1 1 68 68 ASP N N 15 117.825 0.400 . 1 . . . . 68 ASP N . 11027 1 824 . 1 1 68 68 ASP H H 1 8.353 0.020 . 1 . . . . 68 ASP H . 11027 1 825 . 1 1 68 68 ASP CA C 13 54.627 0.400 . 1 . . . . 68 ASP CA . 11027 1 826 . 1 1 68 68 ASP HA H 1 4.617 0.020 . 1 . . . . 68 ASP HA . 11027 1 827 . 1 1 68 68 ASP CB C 13 41.452 0.400 . 1 . . . . 68 ASP CB . 11027 1 828 . 1 1 68 68 ASP HB2 H 1 2.827 0.020 . 2 . . . . 68 ASP HB2 . 11027 1 829 . 1 1 68 68 ASP HB3 H 1 2.647 0.020 . 2 . . . . 68 ASP HB3 . 11027 1 830 . 1 1 68 68 ASP C C 13 176.185 0.400 . 1 . . . . 68 ASP C . 11027 1 831 . 1 1 69 69 TYR N N 15 120.102 0.400 . 1 . . . . 69 TYR N . 11027 1 832 . 1 1 69 69 TYR H H 1 8.842 0.020 . 1 . . . . 69 TYR H . 11027 1 833 . 1 1 69 69 TYR CA C 13 59.139 0.400 . 1 . . . . 69 TYR CA . 11027 1 834 . 1 1 69 69 TYR HA H 1 4.848 0.020 . 1 . . . . 69 TYR HA . 11027 1 835 . 1 1 69 69 TYR CB C 13 43.201 0.400 . 1 . . . . 69 TYR CB . 11027 1 836 . 1 1 69 69 TYR HB2 H 1 3.084 0.020 . 2 . . . . 69 TYR HB2 . 11027 1 837 . 1 1 69 69 TYR HB3 H 1 2.827 0.020 . 2 . . . . 69 TYR HB3 . 11027 1 838 . 1 1 69 69 TYR CD1 C 13 133.263 0.400 . 1 . . . . 69 TYR CD1 . 11027 1 839 . 1 1 69 69 TYR HD1 H 1 7.220 0.020 . 1 . . . . 69 TYR HD1 . 11027 1 840 . 1 1 69 69 TYR CE1 C 13 118.046 0.400 . 1 . . . . 69 TYR CE1 . 11027 1 841 . 1 1 69 69 TYR HE1 H 1 6.923 0.020 . 1 . . . . 69 TYR HE1 . 11027 1 842 . 1 1 69 69 TYR CE2 C 13 118.046 0.400 . 1 . . . . 69 TYR CE2 . 11027 1 843 . 1 1 69 69 TYR HE2 H 1 6.923 0.020 . 1 . . . . 69 TYR HE2 . 11027 1 844 . 1 1 69 69 TYR CD2 C 13 133.229 0.400 . 1 . . . . 69 TYR CD2 . 11027 1 845 . 1 1 69 69 TYR HD2 H 1 7.220 0.020 . 1 . . . . 69 TYR HD2 . 11027 1 846 . 1 1 69 69 TYR C C 13 172.847 0.400 . 1 . . . . 69 TYR C . 11027 1 847 . 1 1 70 70 GLN N N 15 125.190 0.400 . 1 . . . . 70 GLN N . 11027 1 848 . 1 1 70 70 GLN H H 1 7.769 0.020 . 1 . . . . 70 GLN H . 11027 1 849 . 1 1 70 70 GLN CA C 13 54.190 0.400 . 1 . . . . 70 GLN CA . 11027 1 850 . 1 1 70 70 GLN HA H 1 4.282 0.020 . 1 . . . . 70 GLN HA . 11027 1 851 . 1 1 70 70 GLN CB C 13 30.336 0.400 . 1 . . . . 70 GLN CB . 11027 1 852 . 1 1 70 70 GLN HB2 H 1 1.913 0.020 . 2 . . . . 70 GLN HB2 . 11027 1 853 . 1 1 70 70 GLN HB3 H 1 1.823 0.020 . 2 . . . . 70 GLN HB3 . 11027 1 854 . 1 1 70 70 GLN CG C 13 33.102 0.400 . 1 . . . . 70 GLN CG . 11027 1 855 . 1 1 70 70 GLN HG2 H 1 2.119 0.020 . 2 . . . . 70 GLN HG2 . 11027 1 856 . 1 1 70 70 GLN HG3 H 1 2.119 0.020 . 2 . . . . 70 GLN HG3 . 11027 1 857 . 1 1 70 70 GLN C C 13 173.849 0.400 . 1 . . . . 70 GLN C . 11027 1 858 . 1 1 71 71 GLU N N 15 122.647 0.400 . 1 . . . . 71 GLU N . 11027 1 859 . 1 1 71 71 GLU H H 1 8.055 0.020 . 1 . . . . 71 GLU H . 11027 1 860 . 1 1 71 71 GLU CA C 13 56.010 0.400 . 1 . . . . 71 GLU CA . 11027 1 861 . 1 1 71 71 GLU HA H 1 4.089 0.020 . 1 . . . . 71 GLU HA . 11027 1 862 . 1 1 71 71 GLU CB C 13 29.227 0.400 . 1 . . . . 71 GLU CB . 11027 1 863 . 1 1 71 71 GLU HB2 H 1 1.961 0.020 . 2 . . . . 71 GLU HB2 . 11027 1 864 . 1 1 71 71 GLU HB3 H 1 1.875 0.020 . 2 . . . . 71 GLU HB3 . 11027 1 865 . 1 1 71 71 GLU CG C 13 33.175 0.400 . 1 . . . . 71 GLU CG . 11027 1 866 . 1 1 71 71 GLU HG2 H 1 2.272 0.020 . 2 . . . . 71 GLU HG2 . 11027 1 867 . 1 1 71 71 GLU HG3 H 1 2.272 0.020 . 2 . . . . 71 GLU HG3 . 11027 1 868 . 1 1 71 71 GLU C C 13 175.273 0.400 . 1 . . . . 71 GLU C . 11027 1 869 . 1 1 72 72 LYS N N 15 123.615 0.400 . 1 . . . . 72 LYS N . 11027 1 870 . 1 1 72 72 LYS H H 1 8.277 0.020 . 1 . . . . 72 LYS H . 11027 1 871 . 1 1 72 72 LYS CA C 13 56.010 0.400 . 1 . . . . 72 LYS CA . 11027 1 872 . 1 1 72 72 LYS HA H 1 4.346 0.020 . 1 . . . . 72 LYS HA . 11027 1 873 . 1 1 72 72 LYS CB C 13 33.085 0.400 . 1 . . . . 72 LYS CB . 11027 1 874 . 1 1 72 72 LYS HB2 H 1 1.784 0.020 . 2 . . . . 72 LYS HB2 . 11027 1 875 . 1 1 72 72 LYS HB3 H 1 1.784 0.020 . 2 . . . . 72 LYS HB3 . 11027 1 876 . 1 1 72 72 LYS CG C 13 24.005 0.400 . 1 . . . . 72 LYS CG . 11027 1 877 . 1 1 72 72 LYS HG2 H 1 1.411 0.020 . 2 . . . . 72 LYS HG2 . 11027 1 878 . 1 1 72 72 LYS HG3 H 1 1.411 0.020 . 2 . . . . 72 LYS HG3 . 11027 1 879 . 1 1 72 72 LYS CD C 13 28.618 0.400 . 1 . . . . 72 LYS CD . 11027 1 880 . 1 1 72 72 LYS HD2 H 1 1.642 0.020 . 2 . . . . 72 LYS HD2 . 11027 1 881 . 1 1 72 72 LYS CE C 13 41.891 0.400 . 1 . . . . 72 LYS CE . 11027 1 882 . 1 1 72 72 LYS C C 13 175.673 0.400 . 1 . . . . 72 LYS C . 11027 1 883 . 1 1 73 73 SER N N 15 122.683 0.400 . 1 . . . . 73 SER N . 11027 1 884 . 1 1 73 73 SER H H 1 8.037 0.020 . 1 . . . . 73 SER H . 11027 1 885 . 1 1 73 73 SER CA C 13 59.503 0.400 . 1 . . . . 73 SER CA . 11027 1 886 . 1 1 73 73 SER HA H 1 4.256 0.020 . 1 . . . . 73 SER HA . 11027 1 887 . 1 1 73 73 SER CB C 13 64.813 0.400 . 1 . . . . 73 SER CB . 11027 1 888 . 1 1 73 73 SER HB2 H 1 3.840 0.020 . 2 . . . . 73 SER HB2 . 11027 1 889 . 1 1 73 73 SER HB3 H 1 3.840 0.020 . 2 . . . . 73 SER HB3 . 11027 1 stop_ save_