data_25772 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25772 _Entry.Title ; 1H assignment of Elafin at 288K ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2015-08-26 _Entry.Accession_date 2015-08-26 _Entry.Last_release_date 2016-03-03 _Entry.Original_release_date 2016-03-03 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Karine Loth . . . . 25772 2 Soha 'Abou Ibrahim Alami' . . . . 25772 3 Chahrazed Habes . . . . 25772 4 Marie-Louise Zani . . . . 25772 5 Agnes Delmas . . . . 25772 6 Thierry Moreau . . . . 25772 7 Celine Landon . . . . 25772 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25772 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 388 25772 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 2 . . 2016-08-04 2015-08-26 update BMRB 'update entry citation' 25772 1 . . 2016-03-03 2015-08-26 original author 'original release' 25772 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 25771 Cementoin 25772 BMRB 25773 Trappin-2 25772 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25772 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 26878852 _Citation.Full_citation . _Citation.Title ; Complete assignment of 15N, 13C Trappin-2 and 1H assignment of its two domains, Elafin and Cementoin. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biomol. NMR Assign.' _Citation.Journal_name_full 'Biomolecular NMR Assignments' _Citation.Journal_volume 10 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1874-270X _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 223 _Citation.Page_last 226 _Citation.Year 2016 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Karine Loth . . . . 25772 1 2 Soha 'Abou Ibrahim Alami' . . . . 25772 1 3 Chahrazed Habes . . . . 25772 1 4 Marie-Louise Zani . . . . 25772 1 5 Agnes Delmas . . . . 25772 1 6 Thierry Moreau . . . . 25772 1 7 Celine Landon . . . . 25772 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Cementoin 25772 1 Elafin 25772 1 'Inflammatory lung diseases' 25772 1 'Protease inhibitor' 25772 1 'Serine proteases' 25772 1 Trappin-2 25772 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25772 _Assembly.ID 1 _Assembly.Name Elafin _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _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 Elafin 1 $Elafin A . yes native no no . . . 25772 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 16 16 SG . 1 . 1 CYS 45 45 SG . . . . . . . . . . 25772 1 2 disulfide single . 1 . 1 CYS 23 23 SG . 1 . 1 CYS 49 49 SG . . . . . . . . . . 25772 1 3 disulfide single . 1 . 1 CYS 32 32 SG . 1 . 1 CYS 44 44 SG . . . . . . . . . . 25772 1 4 disulfide single . 1 . 1 CYS 38 38 SG . 1 . 1 CYS 53 53 SG . . . . . . . . . . 25772 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 2REL . . 'solution NMR' . 'Same sequence' . 25772 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Elafin _Entity.Sf_category entity _Entity.Sf_framecode Elafin _Entity.Entry_ID 25772 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Elafin _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; AQEPVKGPVSTKPGSCPIIL IRCAMLNPPNRCLKDTDCPG IKKCCEGSCGMACFVPQ ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 57 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'free and disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 ALA . 25772 1 2 2 GLN . 25772 1 3 3 GLU . 25772 1 4 4 PRO . 25772 1 5 5 VAL . 25772 1 6 6 LYS . 25772 1 7 7 GLY . 25772 1 8 8 PRO . 25772 1 9 9 VAL . 25772 1 10 10 SER . 25772 1 11 11 THR . 25772 1 12 12 LYS . 25772 1 13 13 PRO . 25772 1 14 14 GLY . 25772 1 15 15 SER . 25772 1 16 16 CYS . 25772 1 17 17 PRO . 25772 1 18 18 ILE . 25772 1 19 19 ILE . 25772 1 20 20 LEU . 25772 1 21 21 ILE . 25772 1 22 22 ARG . 25772 1 23 23 CYS . 25772 1 24 24 ALA . 25772 1 25 25 MET . 25772 1 26 26 LEU . 25772 1 27 27 ASN . 25772 1 28 28 PRO . 25772 1 29 29 PRO . 25772 1 30 30 ASN . 25772 1 31 31 ARG . 25772 1 32 32 CYS . 25772 1 33 33 LEU . 25772 1 34 34 LYS . 25772 1 35 35 ASP . 25772 1 36 36 THR . 25772 1 37 37 ASP . 25772 1 38 38 CYS . 25772 1 39 39 PRO . 25772 1 40 40 GLY . 25772 1 41 41 ILE . 25772 1 42 42 LYS . 25772 1 43 43 LYS . 25772 1 44 44 CYS . 25772 1 45 45 CYS . 25772 1 46 46 GLU . 25772 1 47 47 GLY . 25772 1 48 48 SER . 25772 1 49 49 CYS . 25772 1 50 50 GLY . 25772 1 51 51 MET . 25772 1 52 52 ALA . 25772 1 53 53 CYS . 25772 1 54 54 PHE . 25772 1 55 55 VAL . 25772 1 56 56 PRO . 25772 1 57 57 GLN . 25772 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 25772 1 . GLN 2 2 25772 1 . GLU 3 3 25772 1 . PRO 4 4 25772 1 . VAL 5 5 25772 1 . LYS 6 6 25772 1 . GLY 7 7 25772 1 . PRO 8 8 25772 1 . VAL 9 9 25772 1 . SER 10 10 25772 1 . THR 11 11 25772 1 . LYS 12 12 25772 1 . PRO 13 13 25772 1 . GLY 14 14 25772 1 . SER 15 15 25772 1 . CYS 16 16 25772 1 . PRO 17 17 25772 1 . ILE 18 18 25772 1 . ILE 19 19 25772 1 . LEU 20 20 25772 1 . ILE 21 21 25772 1 . ARG 22 22 25772 1 . CYS 23 23 25772 1 . ALA 24 24 25772 1 . MET 25 25 25772 1 . LEU 26 26 25772 1 . ASN 27 27 25772 1 . PRO 28 28 25772 1 . PRO 29 29 25772 1 . ASN 30 30 25772 1 . ARG 31 31 25772 1 . CYS 32 32 25772 1 . LEU 33 33 25772 1 . LYS 34 34 25772 1 . ASP 35 35 25772 1 . THR 36 36 25772 1 . ASP 37 37 25772 1 . CYS 38 38 25772 1 . PRO 39 39 25772 1 . GLY 40 40 25772 1 . ILE 41 41 25772 1 . LYS 42 42 25772 1 . LYS 43 43 25772 1 . CYS 44 44 25772 1 . CYS 45 45 25772 1 . GLU 46 46 25772 1 . GLY 47 47 25772 1 . SER 48 48 25772 1 . CYS 49 49 25772 1 . GLY 50 50 25772 1 . MET 51 51 25772 1 . ALA 52 52 25772 1 . CYS 53 53 25772 1 . PHE 54 54 25772 1 . VAL 55 55 25772 1 . PRO 56 56 25772 1 . GLN 57 57 25772 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 25772 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $Elafin . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25772 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 25772 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Elafin . 'recombinant technology' 'Pichia pastoris' . . . Pichia pastoris GS115 . . . . . pPIC9 . . . 25772 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25772 _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 Elafin 'natural abundance' . . 1 $Elafin . . 0.08 . . mM . . . . 25772 1 2 'sodium phosphate' 'natural abundance' . . . . . . 25 . . mM . . . . 25772 1 3 'sodium chloride' 'natural abundance' . . . . . . 300 . . mM . . . . 25772 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25772 1 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25772 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 25772 _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' 300 . mM 25772 1 pH 6.1 . pH 25772 1 pressure 1 . atm 25772 1 temperature 288 . K 25772 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 25772 _Software.ID 1 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 25772 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 25772 1 processing 25772 1 stop_ save_ save_Ccpnmr _Software.Sf_category software _Software.Sf_framecode Ccpnmr _Software.Entry_ID 25772 _Software.ID 2 _Software.Name Ccpnmr _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 25772 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25772 2 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 25772 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 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 25772 _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 . 700 . . . 25772 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 25772 _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-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25772 1 2 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25772 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 25772 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 water protons . . . . ppm 4.868 internal direct 1.000000000 . . . . . 25772 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 25772 _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-1H TOCSY' . . . 25772 1 2 '2D 1H-1H NOESY' . . . 25772 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ALA HA H 1 4.067 0.01 . . . . . . 1 Ala HA . 25772 1 2 . 1 1 1 1 ALA HB1 H 1 1.500 0.01 . . . . . . 1 Ala HB . 25772 1 3 . 1 1 1 1 ALA HB2 H 1 1.500 0.01 . . . . . . 1 Ala HB . 25772 1 4 . 1 1 1 1 ALA HB3 H 1 1.500 0.01 . . . . . . 1 Ala HB . 25772 1 5 . 1 1 2 2 GLN H H 1 8.427 0.01 . . . . . . 2 Gln HN . 25772 1 6 . 1 1 2 2 GLN HA H 1 4.330 0.01 . . . . . . 2 Gln HA . 25772 1 7 . 1 1 2 2 GLN HB2 H 1 1.967 0.01 . . . . . . 2 Gln HB2 . 25772 1 8 . 1 1 2 2 GLN HB3 H 1 2.043 0.01 . . . . . . 2 Gln HB3 . 25772 1 9 . 1 1 2 2 GLN HG2 H 1 2.329 0.01 . . . . . . 2 Gln HG2 . 25772 1 10 . 1 1 2 2 GLN HG3 H 1 2.329 0.01 . . . . . . 2 Gln HG3 . 25772 1 11 . 1 1 2 2 GLN HE21 H 1 7.577 0.01 . . . . . . 2 Gln HE21 . 25772 1 12 . 1 1 2 2 GLN HE22 H 1 6.828 0.01 . . . . . . 2 Gln HE22 . 25772 1 13 . 1 1 3 3 GLU H H 1 8.673 0.01 . . . . . . 3 Glu HN . 25772 1 14 . 1 1 3 3 GLU HA H 1 4.543 0.01 . . . . . . 3 Glu HA . 25772 1 15 . 1 1 3 3 GLU HB2 H 1 2.010 0.01 . . . . . . 3 Glu HB2 . 25772 1 16 . 1 1 3 3 GLU HB3 H 1 1.880 0.01 . . . . . . 3 Glu HB3 . 25772 1 17 . 1 1 3 3 GLU HG2 H 1 2.301 0.01 . . . . . . 3 Glu HG2 . 25772 1 18 . 1 1 3 3 GLU HG3 H 1 2.301 0.01 . . . . . . 3 Glu HG3 . 25772 1 19 . 1 1 4 4 PRO HA H 1 4.432 0.01 . . . . . . 4 Pro HA . 25772 1 20 . 1 1 4 4 PRO HB2 H 1 1.894 0.01 . . . . . . 4 Pro HB2 . 25772 1 21 . 1 1 4 4 PRO HB3 H 1 2.308 0.01 . . . . . . 4 Pro HB3 . 25772 1 22 . 1 1 4 4 PRO HG2 H 1 1.986 0.01 . . . . . . 4 Pro HG2 . 25772 1 23 . 1 1 4 4 PRO HG3 H 1 1.986 0.01 . . . . . . 4 Pro HG3 . 25772 1 24 . 1 1 4 4 PRO HD2 H 1 3.756 0.01 . . . . . . 4 Pro HD2 . 25772 1 25 . 1 1 4 4 PRO HD3 H 1 3.579 0.01 . . . . . . 4 Pro HD3 . 25772 1 26 . 1 1 5 5 VAL H H 1 8.336 0.01 . . . . . . 5 Val HN . 25772 1 27 . 1 1 5 5 VAL HA H 1 4.001 0.01 . . . . . . 5 Val HA . 25772 1 28 . 1 1 5 5 VAL HB H 1 2.007 0.01 . . . . . . 5 Val HB . 25772 1 29 . 1 1 5 5 VAL HG11 H 1 0.954 0.01 . . . . . . 5 Val HG1 . 25772 1 30 . 1 1 5 5 VAL HG12 H 1 0.954 0.01 . . . . . . 5 Val HG1 . 25772 1 31 . 1 1 5 5 VAL HG13 H 1 0.954 0.01 . . . . . . 5 Val HG1 . 25772 1 32 . 1 1 5 5 VAL HG21 H 1 0.918 0.01 . . . . . . 5 Val HG2 . 25772 1 33 . 1 1 5 5 VAL HG22 H 1 0.918 0.01 . . . . . . 5 Val HG2 . 25772 1 34 . 1 1 5 5 VAL HG23 H 1 0.918 0.01 . . . . . . 5 Val HG2 . 25772 1 35 . 1 1 6 6 LYS H H 1 8.545 0.01 . . . . . . 6 Lys HN . 25772 1 36 . 1 1 6 6 LYS HA H 1 4.354 0.01 . . . . . . 6 Lys HA . 25772 1 37 . 1 1 6 6 LYS HB2 H 1 1.736 0.01 . . . . . . 6 Lys HB2 . 25772 1 38 . 1 1 6 6 LYS HB3 H 1 1.829 0.01 . . . . . . 6 Lys HB3 . 25772 1 39 . 1 1 6 6 LYS HG2 H 1 1.404 0.01 . . . . . . 6 Lys HG2 . 25772 1 40 . 1 1 6 6 LYS HG3 H 1 1.457 0.01 . . . . . . 6 Lys HG3 . 25772 1 41 . 1 1 6 6 LYS HD2 H 1 1.825 0.01 . . . . . . 6 Lys HD2 . 25772 1 42 . 1 1 6 6 LYS HD3 H 1 1.658 0.01 . . . . . . 6 Lys HD3 . 25772 1 43 . 1 1 6 6 LYS HE2 H 1 2.970 0.01 . . . . . . 6 Lys HE2 . 25772 1 44 . 1 1 6 6 LYS HE3 H 1 2.970 0.01 . . . . . . 6 Lys HE3 . 25772 1 45 . 1 1 7 7 GLY H H 1 8.256 0.01 . . . . . . 7 Gly HN . 25772 1 46 . 1 1 7 7 GLY HA2 H 1 4.133 0.01 . . . . . . 7 Gly HA1 . 25772 1 47 . 1 1 7 7 GLY HA3 H 1 4.014 0.01 . . . . . . 7 Gly HA2 . 25772 1 48 . 1 1 8 8 PRO HA H 1 4.436 0.01 . . . . . . 8 Pro HA . 25772 1 49 . 1 1 8 8 PRO HB2 H 1 1.846 0.01 . . . . . . 8 Pro HB2 . 25772 1 50 . 1 1 8 8 PRO HB3 H 1 2.269 0.01 . . . . . . 8 Pro HB3 . 25772 1 51 . 1 1 8 8 PRO HG2 H 1 1.997 0.01 . . . . . . 8 Pro HG2 . 25772 1 52 . 1 1 8 8 PRO HG3 H 1 1.997 0.01 . . . . . . 8 Pro HG3 . 25772 1 53 . 1 1 8 8 PRO HD2 H 1 3.681 0.01 . . . . . . 8 Pro HD2 . 25772 1 54 . 1 1 8 8 PRO HD3 H 1 3.814 0.01 . . . . . . 8 Pro HD3 . 25772 1 55 . 1 1 9 9 VAL H H 1 8.246 0.01 . . . . . . 9 Val HN . 25772 1 56 . 1 1 9 9 VAL HA H 1 4.065 0.01 . . . . . . 9 Val HA . 25772 1 57 . 1 1 9 9 VAL HB H 1 2.058 0.01 . . . . . . 9 Val HB . 25772 1 58 . 1 1 9 9 VAL HG11 H 1 0.978 0.01 . . . . . . 9 Val HG1 . 25772 1 59 . 1 1 9 9 VAL HG12 H 1 0.978 0.01 . . . . . . 9 Val HG1 . 25772 1 60 . 1 1 9 9 VAL HG13 H 1 0.978 0.01 . . . . . . 9 Val HG1 . 25772 1 61 . 1 1 9 9 VAL HG21 H 1 0.999 0.01 . . . . . . 9 Val HG2 . 25772 1 62 . 1 1 9 9 VAL HG22 H 1 0.999 0.01 . . . . . . 9 Val HG2 . 25772 1 63 . 1 1 9 9 VAL HG23 H 1 0.999 0.01 . . . . . . 9 Val HG2 . 25772 1 64 . 1 1 10 10 SER H H 1 8.517 0.01 . . . . . . 10 Ser HN . 25772 1 65 . 1 1 10 10 SER HA H 1 4.627 0.01 . . . . . . 10 Ser HA . 25772 1 66 . 1 1 10 10 SER HB2 H 1 3.850 0.01 . . . . . . 10 Ser HB2 . 25772 1 67 . 1 1 10 10 SER HB3 H 1 3.931 0.01 . . . . . . 10 Ser HB3 . 25772 1 68 . 1 1 11 11 THR H H 1 8.190 0.01 . . . . . . 11 Thr HN . 25772 1 69 . 1 1 11 11 THR HA H 1 4.522 0.01 . . . . . . 11 Thr HA . 25772 1 70 . 1 1 11 11 THR HB H 1 4.119 0.01 . . . . . . 11 Thr HB . 25772 1 71 . 1 1 11 11 THR HG21 H 1 1.180 0.01 . . . . . . 11 Thr HG2 . 25772 1 72 . 1 1 11 11 THR HG22 H 1 1.180 0.01 . . . . . . 11 Thr HG2 . 25772 1 73 . 1 1 11 11 THR HG23 H 1 1.180 0.01 . . . . . . 11 Thr HG2 . 25772 1 74 . 1 1 12 12 LYS H H 1 9.265 0.01 . . . . . . 12 Lys HN . 25772 1 75 . 1 1 12 12 LYS HA H 1 4.606 0.01 . . . . . . 12 Lys HA . 25772 1 76 . 1 1 12 12 LYS HB2 H 1 2.020 0.01 . . . . . . 12 Lys HB2 . 25772 1 77 . 1 1 12 12 LYS HB3 H 1 1.812 0.01 . . . . . . 12 Lys HB3 . 25772 1 78 . 1 1 12 12 LYS HG2 H 1 1.245 0.01 . . . . . . 12 Lys HG2 . 25772 1 79 . 1 1 12 12 LYS HG3 H 1 1.385 0.01 . . . . . . 12 Lys HG3 . 25772 1 80 . 1 1 12 12 LYS HD2 H 1 1.601 0.01 . . . . . . 12 Lys HD2 . 25772 1 81 . 1 1 12 12 LYS HD3 H 1 1.601 0.01 . . . . . . 12 Lys HD3 . 25772 1 82 . 1 1 12 12 LYS HE2 H 1 2.909 0.01 . . . . . . 12 Lys HE2 . 25772 1 83 . 1 1 12 12 LYS HE3 H 1 2.909 0.01 . . . . . . 12 Lys HE3 . 25772 1 84 . 1 1 13 13 PRO HA H 1 4.452 0.01 . . . . . . 13 Pro HA . 25772 1 85 . 1 1 13 13 PRO HB2 H 1 1.842 0.01 . . . . . . 13 Pro HB2 . 25772 1 86 . 1 1 13 13 PRO HB3 H 1 2.176 0.01 . . . . . . 13 Pro HB3 . 25772 1 87 . 1 1 13 13 PRO HG2 H 1 1.993 0.01 . . . . . . 13 Pro HG2 . 25772 1 88 . 1 1 13 13 PRO HG3 H 1 1.993 0.01 . . . . . . 13 Pro HG3 . 25772 1 89 . 1 1 13 13 PRO HD2 H 1 3.593 0.01 . . . . . . 13 Pro HD2 . 25772 1 90 . 1 1 13 13 PRO HD3 H 1 3.593 0.01 . . . . . . 13 Pro HD3 . 25772 1 91 . 1 1 14 14 GLY H H 1 8.254 0.01 . . . . . . 14 Gly HN . 25772 1 92 . 1 1 14 14 GLY HA2 H 1 4.430 0.01 . . . . . . 14 Gly HA1 . 25772 1 93 . 1 1 14 14 GLY HA3 H 1 3.741 0.01 . . . . . . 14 Gly HA2 . 25772 1 94 . 1 1 15 15 SER H H 1 8.653 0.01 . . . . . . 15 Ser HN . 25772 1 95 . 1 1 15 15 SER HA H 1 4.956 0.01 . . . . . . 15 Ser HA . 25772 1 96 . 1 1 15 15 SER HB2 H 1 3.768 0.01 . . . . . . 15 Ser HB2 . 25772 1 97 . 1 1 15 15 SER HB3 H 1 3.568 0.01 . . . . . . 15 Ser HB3 . 25772 1 98 . 1 1 16 16 CYS H H 1 9.100 0.01 . . . . . . 16 Cys HN . 25772 1 99 . 1 1 16 16 CYS HA H 1 4.560 0.01 . . . . . . 16 Cys HA . 25772 1 100 . 1 1 16 16 CYS HB2 H 1 2.784 0.01 . . . . . . 16 Cys HB2 . 25772 1 101 . 1 1 16 16 CYS HB3 H 1 3.084 0.01 . . . . . . 16 Cys HB3 . 25772 1 102 . 1 1 17 17 PRO HA H 1 4.300 0.01 . . . . . . 17 Pro HA . 25772 1 103 . 1 1 17 17 PRO HB2 H 1 1.545 0.01 . . . . . . 17 Pro HB2 . 25772 1 104 . 1 1 17 17 PRO HB3 H 1 2.089 0.01 . . . . . . 17 Pro HB3 . 25772 1 105 . 1 1 17 17 PRO HG2 H 1 1.413 0.01 . . . . . . 17 Pro HG2 . 25772 1 106 . 1 1 17 17 PRO HG3 H 1 1.656 0.01 . . . . . . 17 Pro HG3 . 25772 1 107 . 1 1 17 17 PRO HD2 H 1 3.347 0.01 . . . . . . 17 Pro HD2 . 25772 1 108 . 1 1 17 17 PRO HD3 H 1 3.512 0.01 . . . . . . 17 Pro HD3 . 25772 1 109 . 1 1 18 18 ILE H H 1 8.456 0.01 . . . . . . 18 Ile HN . 25772 1 110 . 1 1 18 18 ILE HA H 1 3.937 0.01 . . . . . . 18 Ile HA . 25772 1 111 . 1 1 18 18 ILE HB H 1 1.719 0.01 . . . . . . 18 Ile HB . 25772 1 112 . 1 1 18 18 ILE HG12 H 1 1.140 0.01 . . . . . . 18 Ile HG12 . 25772 1 113 . 1 1 18 18 ILE HG13 H 1 1.471 0.01 . . . . . . 18 Ile HG13 . 25772 1 114 . 1 1 18 18 ILE HG21 H 1 0.741 0.01 . . . . . . 18 Ile HG2 . 25772 1 115 . 1 1 18 18 ILE HG22 H 1 0.741 0.01 . . . . . . 18 Ile HG2 . 25772 1 116 . 1 1 18 18 ILE HG23 H 1 0.741 0.01 . . . . . . 18 Ile HG2 . 25772 1 117 . 1 1 18 18 ILE HD11 H 1 0.742 0.01 . . . . . . 18 Ile HD1 . 25772 1 118 . 1 1 18 18 ILE HD12 H 1 0.742 0.01 . . . . . . 18 Ile HD1 . 25772 1 119 . 1 1 18 18 ILE HD13 H 1 0.742 0.01 . . . . . . 18 Ile HD1 . 25772 1 120 . 1 1 19 19 ILE H H 1 8.609 0.01 . . . . . . 19 Ile HN . 25772 1 121 . 1 1 19 19 ILE HA H 1 4.138 0.01 . . . . . . 19 Ile HA . 25772 1 122 . 1 1 19 19 ILE HB H 1 1.676 0.01 . . . . . . 19 Ile HB . 25772 1 123 . 1 1 19 19 ILE HG12 H 1 1.159 0.01 . . . . . . 19 Ile HG12 . 25772 1 124 . 1 1 19 19 ILE HG13 H 1 1.085 0.01 . . . . . . 19 Ile HG13 . 25772 1 125 . 1 1 19 19 ILE HG21 H 1 0.730 0.01 . . . . . . 19 Ile HG2 . 25772 1 126 . 1 1 19 19 ILE HG22 H 1 0.730 0.01 . . . . . . 19 Ile HG2 . 25772 1 127 . 1 1 19 19 ILE HG23 H 1 0.730 0.01 . . . . . . 19 Ile HG2 . 25772 1 128 . 1 1 19 19 ILE HD11 H 1 0.580 0.01 . . . . . . 19 Ile HD1 . 25772 1 129 . 1 1 19 19 ILE HD12 H 1 0.580 0.01 . . . . . . 19 Ile HD1 . 25772 1 130 . 1 1 19 19 ILE HD13 H 1 0.580 0.01 . . . . . . 19 Ile HD1 . 25772 1 131 . 1 1 20 20 LEU H H 1 8.675 0.01 . . . . . . 20 Leu HN . 25772 1 132 . 1 1 20 20 LEU HA H 1 4.317 0.01 . . . . . . 20 Leu HA . 25772 1 133 . 1 1 20 20 LEU HB2 H 1 1.546 0.01 . . . . . . 20 Leu HB2 . 25772 1 134 . 1 1 20 20 LEU HB3 H 1 1.648 0.01 . . . . . . 20 Leu HB3 . 25772 1 135 . 1 1 20 20 LEU HG H 1 1.546 0.01 . . . . . . 20 Leu HG . 25772 1 136 . 1 1 20 20 LEU HD11 H 1 0.870 0.01 . . . . . . 20 Leu HD1 . 25772 1 137 . 1 1 20 20 LEU HD12 H 1 0.870 0.01 . . . . . . 20 Leu HD1 . 25772 1 138 . 1 1 20 20 LEU HD13 H 1 0.870 0.01 . . . . . . 20 Leu HD1 . 25772 1 139 . 1 1 20 20 LEU HD21 H 1 0.769 0.01 . . . . . . 20 Leu HD2 . 25772 1 140 . 1 1 20 20 LEU HD22 H 1 0.769 0.01 . . . . . . 20 Leu HD2 . 25772 1 141 . 1 1 20 20 LEU HD23 H 1 0.769 0.01 . . . . . . 20 Leu HD2 . 25772 1 142 . 1 1 21 21 ILE H H 1 7.394 0.01 . . . . . . 21 Ile HN . 25772 1 143 . 1 1 21 21 ILE HA H 1 4.218 0.01 . . . . . . 21 Ile HA . 25772 1 144 . 1 1 21 21 ILE HB H 1 1.744 0.01 . . . . . . 21 Ile HB . 25772 1 145 . 1 1 21 21 ILE HG12 H 1 1.111 0.01 . . . . . . 21 Ile HG12 . 25772 1 146 . 1 1 21 21 ILE HG13 H 1 1.430 0.01 . . . . . . 21 Ile HG13 . 25772 1 147 . 1 1 21 21 ILE HG21 H 1 0.836 0.01 . . . . . . 21 Ile HG2 . 25772 1 148 . 1 1 21 21 ILE HG22 H 1 0.836 0.01 . . . . . . 21 Ile HG2 . 25772 1 149 . 1 1 21 21 ILE HG23 H 1 0.836 0.01 . . . . . . 21 Ile HG2 . 25772 1 150 . 1 1 21 21 ILE HD11 H 1 0.834 0.01 . . . . . . 21 Ile HD1 . 25772 1 151 . 1 1 21 21 ILE HD12 H 1 0.834 0.01 . . . . . . 21 Ile HD1 . 25772 1 152 . 1 1 21 21 ILE HD13 H 1 0.834 0.01 . . . . . . 21 Ile HD1 . 25772 1 153 . 1 1 22 22 ARG H H 1 8.429 0.01 . . . . . . 22 Arg HN . 25772 1 154 . 1 1 22 22 ARG HA H 1 5.312 0.01 . . . . . . 22 Arg HA . 25772 1 155 . 1 1 22 22 ARG HB2 H 1 1.926 0.01 . . . . . . 22 Arg HB2 . 25772 1 156 . 1 1 22 22 ARG HB3 H 1 1.620 0.01 . . . . . . 22 Arg HB3 . 25772 1 157 . 1 1 22 22 ARG HG2 H 1 1.536 0.01 . . . . . . 22 Arg HG2 . 25772 1 158 . 1 1 22 22 ARG HG3 H 1 1.533 0.01 . . . . . . 22 Arg HG3 . 25772 1 159 . 1 1 22 22 ARG HD2 H 1 3.244 0.01 . . . . . . 22 Arg HD2 . 25772 1 160 . 1 1 22 22 ARG HD3 H 1 3.147 0.01 . . . . . . 22 Arg HD3 . 25772 1 161 . 1 1 22 22 ARG HE H 1 7.099 0.01 . . . . . . 22 Arg HE . 25772 1 162 . 1 1 23 23 CYS H H 1 8.894 0.01 . . . . . . 23 Cys HN . 25772 1 163 . 1 1 23 23 CYS HA H 1 4.612 0.01 . . . . . . 23 Cys HA . 25772 1 164 . 1 1 23 23 CYS HB2 H 1 3.214 0.01 . . . . . . 23 Cys HB2 . 25772 1 165 . 1 1 23 23 CYS HB3 H 1 3.705 0.01 . . . . . . 23 Cys HB3 . 25772 1 166 . 1 1 24 24 ALA H H 1 8.828 0.01 . . . . . . 24 Ala HN . 25772 1 167 . 1 1 24 24 ALA HA H 1 4.416 0.01 . . . . . . 24 Ala HA . 25772 1 168 . 1 1 24 24 ALA HB1 H 1 1.359 0.01 . . . . . . 24 Ala HB . 25772 1 169 . 1 1 24 24 ALA HB2 H 1 1.359 0.01 . . . . . . 24 Ala HB . 25772 1 170 . 1 1 24 24 ALA HB3 H 1 1.359 0.01 . . . . . . 24 Ala HB . 25772 1 171 . 1 1 25 25 MET H H 1 7.210 0.01 . . . . . . 25 Met HN . 25772 1 172 . 1 1 25 25 MET HA H 1 4.261 0.01 . . . . . . 25 Met HA . 25772 1 173 . 1 1 25 25 MET HB2 H 1 1.929 0.01 . . . . . . 25 Met HB2 . 25772 1 174 . 1 1 25 25 MET HB3 H 1 1.929 0.01 . . . . . . 25 Met HB3 . 25772 1 175 . 1 1 25 25 MET HG2 H 1 2.466 0.01 . . . . . . 25 Met HG2 . 25772 1 176 . 1 1 25 25 MET HG3 H 1 2.370 0.01 . . . . . . 25 Met HG3 . 25772 1 177 . 1 1 25 25 MET HE1 H 1 2.089 0.01 . . . . . . 25 Met HE . 25772 1 178 . 1 1 25 25 MET HE2 H 1 2.089 0.01 . . . . . . 25 Met HE . 25772 1 179 . 1 1 25 25 MET HE3 H 1 2.089 0.01 . . . . . . 25 Met HE . 25772 1 180 . 1 1 26 26 LEU H H 1 8.491 0.01 . . . . . . 26 Leu HN . 25772 1 181 . 1 1 26 26 LEU HA H 1 4.189 0.01 . . . . . . 26 Leu HA . 25772 1 182 . 1 1 26 26 LEU HB2 H 1 1.492 0.01 . . . . . . 26 Leu HB2 . 25772 1 183 . 1 1 26 26 LEU HB3 H 1 1.610 0.01 . . . . . . 26 Leu HB3 . 25772 1 184 . 1 1 26 26 LEU HG H 1 1.607 0.01 . . . . . . 26 Leu HG . 25772 1 185 . 1 1 26 26 LEU HD11 H 1 0.912 0.01 . . . . . . 26 Leu HD1 . 25772 1 186 . 1 1 26 26 LEU HD12 H 1 0.912 0.01 . . . . . . 26 Leu HD1 . 25772 1 187 . 1 1 26 26 LEU HD13 H 1 0.912 0.01 . . . . . . 26 Leu HD1 . 25772 1 188 . 1 1 26 26 LEU HD21 H 1 0.864 0.01 . . . . . . 26 Leu HD2 . 25772 1 189 . 1 1 26 26 LEU HD22 H 1 0.864 0.01 . . . . . . 26 Leu HD2 . 25772 1 190 . 1 1 26 26 LEU HD23 H 1 0.864 0.01 . . . . . . 26 Leu HD2 . 25772 1 191 . 1 1 27 27 ASN H H 1 8.757 0.01 . . . . . . 27 Asn HN . 25772 1 192 . 1 1 27 27 ASN HA H 1 4.765 0.01 . . . . . . 27 Asn HA . 25772 1 193 . 1 1 27 27 ASN HB2 H 1 2.696 0.01 . . . . . . 27 Asn HB2 . 25772 1 194 . 1 1 27 27 ASN HB3 H 1 2.638 0.01 . . . . . . 27 Asn HB3 . 25772 1 195 . 1 1 27 27 ASN HD21 H 1 7.636 0.01 . . . . . . 27 Asn HD21 . 25772 1 196 . 1 1 27 27 ASN HD22 H 1 6.885 0.01 . . . . . . 27 Asn HD22 . 25772 1 197 . 1 1 28 28 PRO HA H 1 4.539 0.01 . . . . . . 28 Pro HA . 25772 1 198 . 1 1 28 28 PRO HB2 H 1 2.077 0.01 . . . . . . 28 Pro HB2 . 25772 1 199 . 1 1 28 28 PRO HB3 H 1 1.900 0.01 . . . . . . 28 Pro HB3 . 25772 1 200 . 1 1 28 28 PRO HG2 H 1 1.501 0.01 . . . . . . 28 Pro HG2 . 25772 1 201 . 1 1 28 28 PRO HG3 H 1 1.670 0.01 . . . . . . 28 Pro HG3 . 25772 1 202 . 1 1 28 28 PRO HD2 H 1 3.510 0.01 . . . . . . 28 Pro HD2 . 25772 1 203 . 1 1 28 28 PRO HD3 H 1 3.585 0.01 . . . . . . 28 Pro HD3 . 25772 1 204 . 1 1 29 29 PRO HA H 1 4.361 0.01 . . . . . . 29 Pro HA . 25772 1 205 . 1 1 29 29 PRO HB2 H 1 2.134 0.01 . . . . . . 29 Pro HB2 . 25772 1 206 . 1 1 29 29 PRO HB3 H 1 1.809 0.01 . . . . . . 29 Pro HB3 . 25772 1 207 . 1 1 29 29 PRO HG2 H 1 1.984 0.01 . . . . . . 29 Pro HG2 . 25772 1 208 . 1 1 29 29 PRO HG3 H 1 1.984 0.01 . . . . . . 29 Pro HG3 . 25772 1 209 . 1 1 29 29 PRO HD2 H 1 3.640 0.01 . . . . . . 29 Pro HD2 . 25772 1 210 . 1 1 29 29 PRO HD3 H 1 3.570 0.01 . . . . . . 29 Pro HD3 . 25772 1 211 . 1 1 30 30 ASN H H 1 8.591 0.01 . . . . . . 30 Asn HN . 25772 1 212 . 1 1 30 30 ASN HA H 1 5.270 0.01 . . . . . . 30 Asn HA . 25772 1 213 . 1 1 30 30 ASN HB2 H 1 2.907 0.01 . . . . . . 30 Asn HB2 . 25772 1 214 . 1 1 30 30 ASN HB3 H 1 2.695 0.01 . . . . . . 30 Asn HB3 . 25772 1 215 . 1 1 30 30 ASN HD21 H 1 7.120 0.01 . . . . . . 30 Asn HD21 . 25772 1 216 . 1 1 30 30 ASN HD22 H 1 7.630 0.01 . . . . . . 30 Asn HD22 . 25772 1 217 . 1 1 31 31 ARG H H 1 8.837 0.01 . . . . . . 31 Arg HN . 25772 1 218 . 1 1 31 31 ARG HA H 1 4.358 0.01 . . . . . . 31 Arg HA . 25772 1 219 . 1 1 31 31 ARG HB2 H 1 2.113 0.01 . . . . . . 31 Arg HB2 . 25772 1 220 . 1 1 31 31 ARG HB3 H 1 1.741 0.01 . . . . . . 31 Arg HB3 . 25772 1 221 . 1 1 31 31 ARG HG2 H 1 1.801 0.01 . . . . . . 31 Arg HG2 . 25772 1 222 . 1 1 31 31 ARG HG3 H 1 1.801 0.01 . . . . . . 31 Arg HG3 . 25772 1 223 . 1 1 31 31 ARG HD2 H 1 3.173 0.01 . . . . . . 31 Arg HD2 . 25772 1 224 . 1 1 31 31 ARG HD3 H 1 3.152 0.01 . . . . . . 31 Arg HD3 . 25772 1 225 . 1 1 31 31 ARG HE H 1 7.230 0.01 . . . . . . 31 Arg HE . 25772 1 226 . 1 1 32 32 CYS H H 1 7.596 0.01 . . . . . . 32 Cys HN . 25772 1 227 . 1 1 32 32 CYS HA H 1 4.584 0.01 . . . . . . 32 Cys HA . 25772 1 228 . 1 1 32 32 CYS HB2 H 1 2.941 0.01 . . . . . . 32 Cys HB2 . 25772 1 229 . 1 1 32 32 CYS HB3 H 1 3.144 0.01 . . . . . . 32 Cys HB3 . 25772 1 230 . 1 1 33 33 LEU H H 1 9.064 0.01 . . . . . . 33 Leu HN . 25772 1 231 . 1 1 33 33 LEU HA H 1 4.644 0.01 . . . . . . 33 Leu HA . 25772 1 232 . 1 1 33 33 LEU HB2 H 1 1.649 0.01 . . . . . . 33 Leu HB2 . 25772 1 233 . 1 1 33 33 LEU HB3 H 1 1.521 0.01 . . . . . . 33 Leu HB3 . 25772 1 234 . 1 1 33 33 LEU HG H 1 1.521 0.01 . . . . . . 33 Leu HG . 25772 1 235 . 1 1 33 33 LEU HD11 H 1 0.909 0.01 . . . . . . 33 Leu HD1 . 25772 1 236 . 1 1 33 33 LEU HD12 H 1 0.909 0.01 . . . . . . 33 Leu HD1 . 25772 1 237 . 1 1 33 33 LEU HD13 H 1 0.909 0.01 . . . . . . 33 Leu HD1 . 25772 1 238 . 1 1 33 33 LEU HD21 H 1 0.876 0.01 . . . . . . 33 Leu HD2 . 25772 1 239 . 1 1 33 33 LEU HD22 H 1 0.876 0.01 . . . . . . 33 Leu HD2 . 25772 1 240 . 1 1 33 33 LEU HD23 H 1 0.876 0.01 . . . . . . 33 Leu HD2 . 25772 1 241 . 1 1 34 34 LYS H H 1 8.104 0.01 . . . . . . 34 Lys HN . 25772 1 242 . 1 1 34 34 LYS HA H 1 4.879 0.01 . . . . . . 34 Lys HA . 25772 1 243 . 1 1 34 34 LYS HB2 H 1 2.005 0.01 . . . . . . 34 Lys HB2 . 25772 1 244 . 1 1 34 34 LYS HB3 H 1 1.815 0.01 . . . . . . 34 Lys HB3 . 25772 1 245 . 1 1 34 34 LYS HG2 H 1 1.390 0.01 . . . . . . 34 Lys HG2 . 25772 1 246 . 1 1 34 34 LYS HG3 H 1 1.243 0.01 . . . . . . 34 Lys HG3 . 25772 1 247 . 1 1 34 34 LYS HD2 H 1 1.608 0.01 . . . . . . 34 Lys HD2 . 25772 1 248 . 1 1 34 34 LYS HD3 H 1 1.608 0.01 . . . . . . 34 Lys HD3 . 25772 1 249 . 1 1 34 34 LYS HE2 H 1 2.940 0.01 . . . . . . 34 Lys HE2 . 25772 1 250 . 1 1 34 34 LYS HE3 H 1 2.950 0.01 . . . . . . 34 Lys HE3 . 25772 1 251 . 1 1 35 35 ASP H H 1 9.471 0.01 . . . . . . 35 Asp HN . 25772 1 252 . 1 1 35 35 ASP HA H 1 4.285 0.01 . . . . . . 35 Asp HA . 25772 1 253 . 1 1 35 35 ASP HB2 H 1 2.509 0.01 . . . . . . 35 Asp HB2 . 25772 1 254 . 1 1 35 35 ASP HB3 H 1 3.255 0.01 . . . . . . 35 Asp HB3 . 25772 1 255 . 1 1 36 36 THR H H 1 7.828 0.01 . . . . . . 36 Thr HN . 25772 1 256 . 1 1 36 36 THR HA H 1 4.213 0.01 . . . . . . 36 Thr HA . 25772 1 257 . 1 1 36 36 THR HB H 1 4.498 0.01 . . . . . . 36 Thr HB . 25772 1 258 . 1 1 36 36 THR HG21 H 1 1.286 0.01 . . . . . . 36 Thr HG2 . 25772 1 259 . 1 1 36 36 THR HG22 H 1 1.286 0.01 . . . . . . 36 Thr HG2 . 25772 1 260 . 1 1 36 36 THR HG23 H 1 1.286 0.01 . . . . . . 36 Thr HG2 . 25772 1 261 . 1 1 37 37 ASP H H 1 7.964 0.01 . . . . . . 37 Asp HN . 25772 1 262 . 1 1 37 37 ASP HA H 1 4.624 0.01 . . . . . . 37 Asp HA . 25772 1 263 . 1 1 37 37 ASP HB2 H 1 3.117 0.01 . . . . . . 37 Asp HB2 . 25772 1 264 . 1 1 37 37 ASP HB3 H 1 3.143 0.01 . . . . . . 37 Asp HB3 . 25772 1 265 . 1 1 38 38 CYS H H 1 7.948 0.01 . . . . . . 38 Cys HN . 25772 1 266 . 1 1 38 38 CYS HA H 1 5.045 0.01 . . . . . . 38 Cys HA . 25772 1 267 . 1 1 38 38 CYS HB2 H 1 2.494 0.01 . . . . . . 38 Cys HB2 . 25772 1 268 . 1 1 38 38 CYS HB3 H 1 2.949 0.01 . . . . . . 38 Cys HB3 . 25772 1 269 . 1 1 39 39 PRO HA H 1 4.519 0.01 . . . . . . 39 Pro HA . 25772 1 270 . 1 1 39 39 PRO HB2 H 1 2.261 0.01 . . . . . . 39 Pro HB2 . 25772 1 271 . 1 1 39 39 PRO HB3 H 1 2.131 0.01 . . . . . . 39 Pro HB3 . 25772 1 272 . 1 1 39 39 PRO HG2 H 1 1.954 0.01 . . . . . . 39 Pro HG2 . 25772 1 273 . 1 1 39 39 PRO HG3 H 1 2.069 0.01 . . . . . . 39 Pro HG3 . 25772 1 274 . 1 1 39 39 PRO HD2 H 1 3.596 0.01 . . . . . . 39 Pro HD2 . 25772 1 275 . 1 1 39 39 PRO HD3 H 1 3.939 0.01 . . . . . . 39 Pro HD3 . 25772 1 276 . 1 1 40 40 GLY H H 1 8.686 0.01 . . . . . . 40 Gly HN . 25772 1 277 . 1 1 40 40 GLY HA2 H 1 3.759 0.01 . . . . . . 40 Gly HA1 . 25772 1 278 . 1 1 40 40 GLY HA3 H 1 3.943 0.01 . . . . . . 40 Gly HA2 . 25772 1 279 . 1 1 41 41 ILE H H 1 8.631 0.01 . . . . . . 41 Ile HN . 25772 1 280 . 1 1 41 41 ILE HA H 1 4.319 0.01 . . . . . . 41 Ile HA . 25772 1 281 . 1 1 41 41 ILE HB H 1 2.198 0.01 . . . . . . 41 Ile HB . 25772 1 282 . 1 1 41 41 ILE HG12 H 1 1.082 0.01 . . . . . . 41 Ile HG12 . 25772 1 283 . 1 1 41 41 ILE HG13 H 1 1.318 0.01 . . . . . . 41 Ile HG13 . 25772 1 284 . 1 1 41 41 ILE HG21 H 1 0.946 0.01 . . . . . . 41 Ile HG2 . 25772 1 285 . 1 1 41 41 ILE HG22 H 1 0.946 0.01 . . . . . . 41 Ile HG2 . 25772 1 286 . 1 1 41 41 ILE HG23 H 1 0.946 0.01 . . . . . . 41 Ile HG2 . 25772 1 287 . 1 1 41 41 ILE HD11 H 1 0.959 0.01 . . . . . . 41 Ile HD1 . 25772 1 288 . 1 1 41 41 ILE HD12 H 1 0.959 0.01 . . . . . . 41 Ile HD1 . 25772 1 289 . 1 1 41 41 ILE HD13 H 1 0.959 0.01 . . . . . . 41 Ile HD1 . 25772 1 290 . 1 1 42 42 LYS H H 1 7.846 0.01 . . . . . . 42 Lys HN . 25772 1 291 . 1 1 42 42 LYS HA H 1 4.134 0.01 . . . . . . 42 Lys HA . 25772 1 292 . 1 1 42 42 LYS HB2 H 1 1.949 0.01 . . . . . . 42 Lys HB2 . 25772 1 293 . 1 1 42 42 LYS HB3 H 1 1.673 0.01 . . . . . . 42 Lys HB3 . 25772 1 294 . 1 1 42 42 LYS HG2 H 1 1.265 0.01 . . . . . . 42 Lys HG2 . 25772 1 295 . 1 1 42 42 LYS HG3 H 1 1.262 0.01 . . . . . . 42 Lys HG3 . 25772 1 296 . 1 1 42 42 LYS HD2 H 1 1.418 0.01 . . . . . . 42 Lys HD2 . 25772 1 297 . 1 1 42 42 LYS HD3 H 1 1.418 0.01 . . . . . . 42 Lys HD3 . 25772 1 298 . 1 1 42 42 LYS HE2 H 1 2.791 0.01 . . . . . . 42 Lys HE2 . 25772 1 299 . 1 1 42 42 LYS HE3 H 1 2.791 0.01 . . . . . . 42 Lys HE3 . 25772 1 300 . 1 1 43 43 LYS H H 1 8.802 0.01 . . . . . . 43 Lys HN . 25772 1 301 . 1 1 43 43 LYS HA H 1 4.199 0.01 . . . . . . 43 Lys HA . 25772 1 302 . 1 1 43 43 LYS HB2 H 1 2.041 0.01 . . . . . . 43 Lys HB2 . 25772 1 303 . 1 1 43 43 LYS HB3 H 1 2.041 0.01 . . . . . . 43 Lys HB3 . 25772 1 304 . 1 1 43 43 LYS HG2 H 1 1.477 0.01 . . . . . . 43 Lys HG2 . 25772 1 305 . 1 1 43 43 LYS HG3 H 1 1.590 0.01 . . . . . . 43 Lys HG3 . 25772 1 306 . 1 1 43 43 LYS HD2 H 1 1.635 0.01 . . . . . . 43 Lys HD2 . 25772 1 307 . 1 1 43 43 LYS HD3 H 1 1.632 0.01 . . . . . . 43 Lys HD3 . 25772 1 308 . 1 1 43 43 LYS HE2 H 1 2.714 0.01 . . . . . . 43 Lys HE2 . 25772 1 309 . 1 1 43 43 LYS HE3 H 1 2.714 0.01 . . . . . . 43 Lys HE3 . 25772 1 310 . 1 1 44 44 CYS H H 1 9.262 0.01 . . . . . . 44 Cys HN . 25772 1 311 . 1 1 44 44 CYS HA H 1 4.982 0.01 . . . . . . 44 Cys HA . 25772 1 312 . 1 1 44 44 CYS HB2 H 1 2.715 0.01 . . . . . . 44 Cys HB2 . 25772 1 313 . 1 1 44 44 CYS HB3 H 1 2.518 0.01 . . . . . . 44 Cys HB3 . 25772 1 314 . 1 1 45 45 CYS H H 1 9.486 0.01 . . . . . . 45 Cys HN . 25772 1 315 . 1 1 45 45 CYS HA H 1 5.150 0.01 . . . . . . 45 Cys HA . 25772 1 316 . 1 1 45 45 CYS HB2 H 1 3.289 0.01 . . . . . . 45 Cys HB2 . 25772 1 317 . 1 1 45 45 CYS HB3 H 1 2.745 0.01 . . . . . . 45 Cys HB3 . 25772 1 318 . 1 1 46 46 GLU H H 1 8.954 0.01 . . . . . . 46 Glu HN . 25772 1 319 . 1 1 46 46 GLU HA H 1 4.139 0.01 . . . . . . 46 Glu HA . 25772 1 320 . 1 1 46 46 GLU HB2 H 1 1.975 0.01 . . . . . . 46 Glu HB2 . 25772 1 321 . 1 1 46 46 GLU HB3 H 1 1.919 0.01 . . . . . . 46 Glu HB3 . 25772 1 322 . 1 1 46 46 GLU HG2 H 1 2.366 0.01 . . . . . . 46 Glu HG2 . 25772 1 323 . 1 1 46 46 GLU HG3 H 1 2.269 0.01 . . . . . . 46 Glu HG3 . 25772 1 324 . 1 1 47 47 GLY H H 1 7.947 0.01 . . . . . . 47 Gly HN . 25772 1 325 . 1 1 47 47 GLY HA2 H 1 4.069 0.01 . . . . . . 47 Gly HA1 . 25772 1 326 . 1 1 47 47 GLY HA3 H 1 4.587 0.01 . . . . . . 47 Gly HA2 . 25772 1 327 . 1 1 48 48 SER H H 1 8.767 0.01 . . . . . . 48 Ser HN . 25772 1 328 . 1 1 48 48 SER HA H 1 4.374 0.01 . . . . . . 48 Ser HA . 25772 1 329 . 1 1 48 48 SER HB2 H 1 3.910 0.01 . . . . . . 48 Ser HB2 . 25772 1 330 . 1 1 48 48 SER HB3 H 1 3.910 0.01 . . . . . . 48 Ser HB3 . 25772 1 331 . 1 1 49 49 CYS H H 1 9.123 0.01 . . . . . . 49 Cys HN . 25772 1 332 . 1 1 49 49 CYS HA H 1 5.038 0.01 . . . . . . 49 Cys HA . 25772 1 333 . 1 1 49 49 CYS HB2 H 1 2.930 0.01 . . . . . . 49 Cys HB2 . 25772 1 334 . 1 1 49 49 CYS HB3 H 1 3.076 0.01 . . . . . . 49 Cys HB3 . 25772 1 335 . 1 1 50 50 GLY H H 1 9.032 0.01 . . . . . . 50 Gly HN . 25772 1 336 . 1 1 50 50 GLY HA2 H 1 3.693 0.01 . . . . . . 50 Gly HA1 . 25772 1 337 . 1 1 50 50 GLY HA3 H 1 3.693 0.01 . . . . . . 50 Gly HA2 . 25772 1 338 . 1 1 51 51 MET H H 1 8.899 0.01 . . . . . . 51 Met HN . 25772 1 339 . 1 1 51 51 MET HA H 1 5.102 0.01 . . . . . . 51 Met HA . 25772 1 340 . 1 1 51 51 MET HB2 H 1 2.343 0.01 . . . . . . 51 Met HB2 . 25772 1 341 . 1 1 51 51 MET HB3 H 1 2.680 0.01 . . . . . . 51 Met HB3 . 25772 1 342 . 1 1 51 51 MET HG2 H 1 2.143 0.01 . . . . . . 51 Met HG2 . 25772 1 343 . 1 1 51 51 MET HG3 H 1 2.011 0.01 . . . . . . 51 Met HG3 . 25772 1 344 . 1 1 51 51 MET HE1 H 1 1.971 0.01 . . . . . . 51 Met HE . 25772 1 345 . 1 1 51 51 MET HE2 H 1 1.971 0.01 . . . . . . 51 Met HE . 25772 1 346 . 1 1 51 51 MET HE3 H 1 1.971 0.01 . . . . . . 51 Met HE . 25772 1 347 . 1 1 52 52 ALA H H 1 9.531 0.01 . . . . . . 52 Ala HN . 25772 1 348 . 1 1 52 52 ALA HA H 1 4.436 0.01 . . . . . . 52 Ala HA . 25772 1 349 . 1 1 52 52 ALA HB1 H 1 1.279 0.01 . . . . . . 52 Ala HB . 25772 1 350 . 1 1 52 52 ALA HB2 H 1 1.279 0.01 . . . . . . 52 Ala HB . 25772 1 351 . 1 1 52 52 ALA HB3 H 1 1.279 0.01 . . . . . . 52 Ala HB . 25772 1 352 . 1 1 53 53 CYS H H 1 8.778 0.01 . . . . . . 53 Cys HN . 25772 1 353 . 1 1 53 53 CYS HA H 1 5.546 0.01 . . . . . . 53 Cys HA . 25772 1 354 . 1 1 53 53 CYS HB2 H 1 2.470 0.01 . . . . . . 53 Cys HB2 . 25772 1 355 . 1 1 53 53 CYS HB3 H 1 2.861 0.01 . . . . . . 53 Cys HB3 . 25772 1 356 . 1 1 54 54 PHE H H 1 9.957 0.01 . . . . . . 54 Phe HN . 25772 1 357 . 1 1 54 54 PHE HA H 1 4.825 0.01 . . . . . . 54 Phe HA . 25772 1 358 . 1 1 54 54 PHE HB2 H 1 2.476 0.01 . . . . . . 54 Phe HB2 . 25772 1 359 . 1 1 54 54 PHE HB3 H 1 3.051 0.01 . . . . . . 54 Phe HB3 . 25772 1 360 . 1 1 54 54 PHE HD1 H 1 7.248 0.01 . . . . . . 54 Phe HD . 25772 1 361 . 1 1 54 54 PHE HD2 H 1 7.248 0.01 . . . . . . 54 Phe HD . 25772 1 362 . 1 1 54 54 PHE HE1 H 1 7.406 0.01 . . . . . . 54 Phe HE . 25772 1 363 . 1 1 54 54 PHE HE2 H 1 7.406 0.01 . . . . . . 54 Phe HE . 25772 1 364 . 1 1 54 54 PHE HZ H 1 7.238 0.01 . . . . . . 54 Phe HZ . 25772 1 365 . 1 1 55 55 VAL H H 1 8.950 0.01 . . . . . . 55 Val HN . 25772 1 366 . 1 1 55 55 VAL HA H 1 3.952 0.01 . . . . . . 55 Val HA . 25772 1 367 . 1 1 55 55 VAL HB H 1 2.082 0.01 . . . . . . 55 Val HB . 25772 1 368 . 1 1 55 55 VAL HG11 H 1 1.083 0.01 . . . . . . 55 Val HG1 . 25772 1 369 . 1 1 55 55 VAL HG12 H 1 1.083 0.01 . . . . . . 55 Val HG1 . 25772 1 370 . 1 1 55 55 VAL HG13 H 1 1.083 0.01 . . . . . . 55 Val HG1 . 25772 1 371 . 1 1 55 55 VAL HG21 H 1 1.080 0.01 . . . . . . 55 Val HG2 . 25772 1 372 . 1 1 55 55 VAL HG22 H 1 1.080 0.01 . . . . . . 55 Val HG2 . 25772 1 373 . 1 1 55 55 VAL HG23 H 1 1.080 0.01 . . . . . . 55 Val HG2 . 25772 1 374 . 1 1 56 56 PRO HA H 1 4.524 0.01 . . . . . . 56 Pro HA . 25772 1 375 . 1 1 56 56 PRO HB2 H 1 2.070 0.01 . . . . . . 56 Pro HB2 . 25772 1 376 . 1 1 56 56 PRO HB3 H 1 2.238 0.01 . . . . . . 56 Pro HB3 . 25772 1 377 . 1 1 56 56 PRO HG2 H 1 2.099 0.01 . . . . . . 56 Pro HG2 . 25772 1 378 . 1 1 56 56 PRO HG3 H 1 1.941 0.01 . . . . . . 56 Pro HG3 . 25772 1 379 . 1 1 56 56 PRO HD2 H 1 3.885 0.01 . . . . . . 56 Pro HD2 . 25772 1 380 . 1 1 56 56 PRO HD3 H 1 3.446 0.01 . . . . . . 56 Pro HD3 . 25772 1 381 . 1 1 57 57 GLN H H 1 8.717 0.01 . . . . . . 57 Gln HN . 25772 1 382 . 1 1 57 57 GLN HA H 1 4.205 0.01 . . . . . . 57 Gln HA . 25772 1 383 . 1 1 57 57 GLN HB2 H 1 1.756 0.01 . . . . . . 57 Gln HB2 . 25772 1 384 . 1 1 57 57 GLN HB3 H 1 2.042 0.01 . . . . . . 57 Gln HB3 . 25772 1 385 . 1 1 57 57 GLN HG2 H 1 2.222 0.01 . . . . . . 57 Gln HG2 . 25772 1 386 . 1 1 57 57 GLN HG3 H 1 2.194 0.01 . . . . . . 57 Gln HG3 . 25772 1 387 . 1 1 57 57 GLN HE21 H 1 6.919 0.01 . . . . . . 57 Gln HE21 . 25772 1 388 . 1 1 57 57 GLN HE22 H 1 7.612 0.01 . . . . . . 57 Gln HE22 . 25772 1 stop_ save_