data_25349 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25349 _Entry.Title ; Nedd4 WW3 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-11-17 _Entry.Accession_date 2014-11-17 _Entry.Last_release_date 2016-01-25 _Entry.Original_release_date 2016-01-25 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.99 _Entry.Original_NMR_STAR_version 3.1.1.61 _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 Justin Lecher . . . . 25349 2 'Andrew J.' Dingley . . . . 25349 3 Vineet Panwalkar . . . . 25349 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 25349 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'ICS-6 (Strukturbiochemie) Forschungszentrum Juelich GmbH' . 25349 2 . 'School of Chemical Sciences, The University of Auckland' . 25349 3 . 'Institut fuer Physikalische Biologie, Henrich-Heine-Universitaet' . 25349 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID NMR . 25349 'Protein dynamics' . 25349 'Protein structure' . 25349 'Protein-Peptide complex' . 25349 WW3 . 25349 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25349 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 184 25349 '15N chemical shifts' 44 25349 '1H chemical shifts' 297 25349 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 . . 2016-03-10 2014-11-17 update BMRB 'update entry citation' 25349 1 . . 2016-01-25 2014-11-17 original author 'original release' 25349 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25349 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 26685112 _Citation.Full_citation . _Citation.Title ; The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 55 _Citation.Journal_issue 4 _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 659 _Citation.Page_last 674 _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 Vineet Panwalkar . . . . 25349 1 2 Philipp Neudecker . . . . 25349 1 3 Michael Schmitz . . . . 25349 1 4 Justin Lecher . . . . 25349 1 5 Marianne Schulte . . . . 25349 1 6 Karima Medini . . . . 25349 1 7 Matthias Stoldt . . . . 25349 1 8 Margaret Brimble . A. . . 25349 1 9 Dieter Willbold . . . . 25349 1 10 Andrew Dingley . J. . . 25349 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID NMR 25349 1 'Protein dynamics' 25349 1 'Protein structure' 25349 1 'Protein-peptide complex' 25349 1 'WW domain' 25349 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25349 _Assembly.ID 1 _Assembly.Name WW3 _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass 4966.6205 _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 'E3 ubiquitin-protein ligase Nedd4' 1 $E3_ubiquitin-protein_ligase_Nedd4 A . yes native no no . . . 25349 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_E3_ubiquitin-protein_ligase_Nedd4 _Entity.Sf_category entity _Entity.Sf_framecode E3_ubiquitin-protein_ligase_Nedd4 _Entity.Entry_ID 25349 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name E3_ubiquitin-protein_ligase_Nedd4 _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 ; GSMEQGFLPKGWEVRHAPNG RPFFIDHNTKTTTWEDPRLK IPA ; _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 43 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment WW3 _Entity.Mutation 'First two residues (GS) are cloning artifacts' _Entity.EC_number 6.3.2 _Entity.Calc_isoelectric_point . _Entity.Formula_weight 4966.6205 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 yes UniProt P46934 NEDD4_HUMAN 'E3 ubiquitin-protein ligase NEDD4' . . . . . . . . . . . . . . 25349 1 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 6.3.2 EC 25349 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 GLY . 25349 1 2 2 SER . 25349 1 3 3 MET . 25349 1 4 4 GLU . 25349 1 5 5 GLN . 25349 1 6 6 GLY . 25349 1 7 7 PHE . 25349 1 8 8 LEU . 25349 1 9 9 PRO . 25349 1 10 10 LYS . 25349 1 11 11 GLY . 25349 1 12 12 TRP . 25349 1 13 13 GLU . 25349 1 14 14 VAL . 25349 1 15 15 ARG . 25349 1 16 16 HIS . 25349 1 17 17 ALA . 25349 1 18 18 PRO . 25349 1 19 19 ASN . 25349 1 20 20 GLY . 25349 1 21 21 ARG . 25349 1 22 22 PRO . 25349 1 23 23 PHE . 25349 1 24 24 PHE . 25349 1 25 25 ILE . 25349 1 26 26 ASP . 25349 1 27 27 HIS . 25349 1 28 28 ASN . 25349 1 29 29 THR . 25349 1 30 30 LYS . 25349 1 31 31 THR . 25349 1 32 32 THR . 25349 1 33 33 THR . 25349 1 34 34 TRP . 25349 1 35 35 GLU . 25349 1 36 36 ASP . 25349 1 37 37 PRO . 25349 1 38 38 ARG . 25349 1 39 39 LEU . 25349 1 40 40 LYS . 25349 1 41 41 ILE . 25349 1 42 42 PRO . 25349 1 43 43 ALA . 25349 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 25349 1 . SER 2 2 25349 1 . MET 3 3 25349 1 . GLU 4 4 25349 1 . GLN 5 5 25349 1 . GLY 6 6 25349 1 . PHE 7 7 25349 1 . LEU 8 8 25349 1 . PRO 9 9 25349 1 . LYS 10 10 25349 1 . GLY 11 11 25349 1 . TRP 12 12 25349 1 . GLU 13 13 25349 1 . VAL 14 14 25349 1 . ARG 15 15 25349 1 . HIS 16 16 25349 1 . ALA 17 17 25349 1 . PRO 18 18 25349 1 . ASN 19 19 25349 1 . GLY 20 20 25349 1 . ARG 21 21 25349 1 . PRO 22 22 25349 1 . PHE 23 23 25349 1 . PHE 24 24 25349 1 . ILE 25 25 25349 1 . ASP 26 26 25349 1 . HIS 27 27 25349 1 . ASN 28 28 25349 1 . THR 29 29 25349 1 . LYS 30 30 25349 1 . THR 31 31 25349 1 . THR 32 32 25349 1 . THR 33 33 25349 1 . TRP 34 34 25349 1 . GLU 35 35 25349 1 . ASP 36 36 25349 1 . PRO 37 37 25349 1 . ARG 38 38 25349 1 . LEU 39 39 25349 1 . LYS 40 40 25349 1 . ILE 41 41 25349 1 . PRO 42 42 25349 1 . ALA 43 43 25349 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 25349 _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 $E3_ubiquitin-protein_ligase_Nedd4 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25349 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 25349 _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 $E3_ubiquitin-protein_ligase_Nedd4 . 'recombinant technology' 'Escherichia coli' 'Escherichia coli' . . Escherichia coli 'Rosetta (DE3) pLysS' . . . . . pGEX2TK . . . 25349 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25349 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '1.5 mM' _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 'E3 ubiquitin-protein ligase Nedd4' '[U-13C; U-15N]' . . 1 $E3_ubiquitin-protein_ligase_Nedd4 . protein 1.5 . . mM . . . . 25349 1 2 Na2HPO4 'natural abundance' . . . . . buffer 20.0 . . mM . . . . 25349 1 3 NaCl 'natural abundance' . . . . . salt 50.0 . . mM . . . . 25349 1 4 DSS 'natural abundance' . . . . . . 0.1 . . mM . . . . 25349 1 5 H2O 'natural abundance' . . . . . solvent 90 . . % . . . . 25349 1 6 D2O [U-2H] . . . . . solvent 10 . . % . . . . 25349 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 25349 _Sample_condition_list.ID 1 _Sample_condition_list.Details '20 mM Sodium Phosphate, 50 mM NaCl, pH 6.5' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.050 . M 25349 1 pH 6.500 . pH 25349 1 pressure 1.000 . atm 25349 1 temperature 298.000 . K 25349 1 stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Software.Sf_category software _Software.Sf_framecode CcpNmr_Analysis _Software.Entry_ID 25349 _Software.ID 1 _Software.Name CcpNmr_Analysis _Software.Version 2.4.1 _Software.Details 'The CCPN NMR assignment and data analysis application' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk 25349 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Chemical shift assignment' 25349 1 stop_ save_ save_manual _Method.Sf_category method _Method.Sf_framecode manual _Method.Entry_ID 25349 _Method.ID 1 _Method.Derivation_type . _Method.Details manual _Method.Computer_ID . _Method.Computer_label . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_AVANCE_600 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode AVANCE_600 _NMR_spectrometer.Entry_ID 25349 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 599 save_ save_Agilent_900 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode Agilent_900 _NMR_spectrometer.Entry_ID 25349 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VNMRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 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 25349 _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 'AVANCE 600' Bruker Avance . 599 . . . 25349 1 2 'Agilent 900' Varian VNMRS . 900 . . . 25349 1 stop_ save_ save_QCI_Cryoprobe _NMR_spectrometer_probe.Sf_category NMR_spectrometer_probe _NMR_spectrometer_probe.Sf_framecode QCI_Cryoprobe _NMR_spectrometer_probe.Entry_ID 25349 _NMR_spectrometer_probe.ID 1 _NMR_spectrometer_probe.Details . _NMR_spectrometer_probe.Manufacturer Bruker _NMR_spectrometer_probe.Model na _NMR_spectrometer_probe.Serial_number . _NMR_spectrometer_probe.Diameter 0.005 _NMR_spectrometer_probe.Rotor_length . _NMR_spectrometer_probe.Rotor_composition . _NMR_spectrometer_probe.Internal_volume . _NMR_spectrometer_probe.Spacer_present . loop_ _NMR_probe.Type _NMR_probe.Entry_ID _NMR_probe.NMR_spectrometer_probe_ID liquid 25349 1 stop_ save_ save_HCN_Triple_resonance_cryogenic_probe _NMR_spectrometer_probe.Sf_category NMR_spectrometer_probe _NMR_spectrometer_probe.Sf_framecode HCN_Triple_resonance_cryogenic_probe _NMR_spectrometer_probe.Entry_ID 25349 _NMR_spectrometer_probe.ID 2 _NMR_spectrometer_probe.Details . _NMR_spectrometer_probe.Manufacturer Varian _NMR_spectrometer_probe.Model na _NMR_spectrometer_probe.Serial_number . _NMR_spectrometer_probe.Diameter 0.005 _NMR_spectrometer_probe.Rotor_length . _NMR_spectrometer_probe.Rotor_composition . _NMR_spectrometer_probe.Internal_volume . _NMR_spectrometer_probe.Spacer_present . loop_ _NMR_probe.Type _NMR_probe.Entry_ID _NMR_probe.NMR_spectrometer_probe_ID liquid 25349 2 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 25349 _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 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AVANCE_600 1 $QCI_Cryoprobe . . . . . . . . . . . . . . 25349 1 2 '2D 1H-13C HSQC/HMQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $Agilent_900 2 $HCN_Triple_resonance_cryogenic_probe . . . . . . . . . . . . . . 25349 1 3 '2D 1H-13C HSQC/HMQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $Agilent_900 2 $HCN_Triple_resonance_cryogenic_probe . . . . . . . . . . . . . . 25349 1 4 '2D 1H-15N HSQC/HMQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AVANCE_600 1 $QCI_Cryoprobe . . . . . . . . . . . . . . 25349 1 5 '2D 1H-13C HSQC aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $AVANCE_600 1 $QCI_Cryoprobe . . . . . . . . . . . . . . 25349 1 6 '3D 1H-13C NOESY aromatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $Agilent_900 2 $HCN_Triple_resonance_cryogenic_probe . . . . . . . . . . . . . . 25349 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 25349 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 25349 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 25349 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 25349 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 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list _Assigned_chem_shift_list.Entry_ID 25349 _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 '3D HNCO' 1 $sample_1 isotropic 25349 1 2 '2D 1H-13C HSQC/HMQC' 1 $sample_1 isotropic 25349 1 4 '2D 1H-15N HSQC/HMQC' 1 $sample_1 isotropic 25349 1 6 '3D 1H-13C NOESY aromatic' 1 $sample_1 isotropic 25349 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $CcpNmr_Analysis 1 $manual 25349 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 SER HA H 1 4.791 0.002 . 1 . . . . 2 SER HA . 25349 1 2 . 1 1 2 2 SER CA C 13 54.657 0.2 . 1 . . . . 2 SER CA . 25349 1 3 . 1 1 3 3 MET H H 1 7.506 0.003 . 1 . . . . 3 MET H . 25349 1 4 . 1 1 3 3 MET HA H 1 4.469 0.007 . 1 . . . . 3 MET HA . 25349 1 5 . 1 1 3 3 MET HB2 H 1 2.594 0.01 . 2 . . . . 3 MET HB2 . 25349 1 6 . 1 1 3 3 MET HB3 H 1 2.525 0.007 . 2 . . . . 3 MET HB3 . 25349 1 7 . 1 1 3 3 MET HG2 H 1 2.019 0.006 . 2 . . . . 3 MET HG2 . 25349 1 8 . 1 1 3 3 MET HG3 H 1 2.082 0.005 . 2 . . . . 3 MET HG3 . 25349 1 9 . 1 1 3 3 MET C C 13 176.602 0.2 . 1 . . . . 3 MET C . 25349 1 10 . 1 1 3 3 MET CA C 13 56.014 0.073 . 1 . . . . 3 MET CA . 25349 1 11 . 1 1 3 3 MET CB C 13 32.088 0.051 . 1 . . . . 3 MET CB . 25349 1 12 . 1 1 3 3 MET CG C 13 32.577 0.066 . 1 . . . . 3 MET CG . 25349 1 13 . 1 1 3 3 MET N N 15 121.815 0.117 . 1 . . . . 3 MET N . 25349 1 14 . 1 1 4 4 GLU H H 1 8.479 0.006 . 1 . . . . 4 GLU H . 25349 1 15 . 1 1 4 4 GLU HA H 1 4.216 0.007 . 1 . . . . 4 GLU HA . 25349 1 16 . 1 1 4 4 GLU HB2 H 1 2.035 0.011 . 2 . . . . 4 GLU HB2 . 25349 1 17 . 1 1 4 4 GLU HB3 H 1 1.952 0.018 . 2 . . . . 4 GLU HB3 . 25349 1 18 . 1 1 4 4 GLU HG2 H 1 2.259 0.008 . 2 . . . . 4 GLU HG2 . 25349 1 19 . 1 1 4 4 GLU HG3 H 1 2.147 0.05 . 2 . . . . 4 GLU HG3 . 25349 1 20 . 1 1 4 4 GLU C C 13 176.648 0.2 . 1 . . . . 4 GLU C . 25349 1 21 . 1 1 4 4 GLU CA C 13 56.984 0.139 . 1 . . . . 4 GLU CA . 25349 1 22 . 1 1 4 4 GLU CB C 13 29.948 0.053 . 1 . . . . 4 GLU CB . 25349 1 23 . 1 1 4 4 GLU CG C 13 36.502 0.078 . 1 . . . . 4 GLU CG . 25349 1 24 . 1 1 4 4 GLU N N 15 121.746 0.073 . 1 . . . . 4 GLU N . 25349 1 25 . 1 1 5 5 GLN H H 1 8.283 0.006 . 1 . . . . 5 GLN H . 25349 1 26 . 1 1 5 5 GLN HA H 1 4.29 0.007 . 1 . . . . 5 GLN HA . 25349 1 27 . 1 1 5 5 GLN HB2 H 1 1.956 0.008 . 2 . . . . 5 GLN HB2 . 25349 1 28 . 1 1 5 5 GLN HB3 H 1 2.092 0.007 . 2 . . . . 5 GLN HB3 . 25349 1 29 . 1 1 5 5 GLN HE21 H 1 7.52 0.01 . 1 . . . . 5 GLN HE21 . 25349 1 30 . 1 1 5 5 GLN HE22 H 1 6.873 0.007 . 1 . . . . 5 GLN HE22 . 25349 1 31 . 1 1 5 5 GLN HG2 H 1 2.347 0.005 . 2 . . . . 5 GLN HG2 . 25349 1 32 . 1 1 5 5 GLN HG3 H 1 2.347 0.004 . 2 . . . . 5 GLN HG3 . 25349 1 33 . 1 1 5 5 GLN C C 13 176.36 0.2 . 1 . . . . 5 GLN C . 25349 1 34 . 1 1 5 5 GLN CA C 13 56.023 0.117 . 1 . . . . 5 GLN CA . 25349 1 35 . 1 1 5 5 GLN CB C 13 29.661 0.029 . 1 . . . . 5 GLN CB . 25349 1 36 . 1 1 5 5 GLN CG C 13 34.038 0.046 . 1 . . . . 5 GLN CG . 25349 1 37 . 1 1 5 5 GLN N N 15 120.36 0.067 . 1 . . . . 5 GLN N . 25349 1 38 . 1 1 5 5 GLN NE2 N 15 112.274 0.023 . 1 . . . . 5 GLN NE2 . 25349 1 39 . 1 1 6 6 GLY H H 1 8.273 0.005 . 1 . . . . 6 GLY H . 25349 1 40 . 1 1 6 6 GLY HA2 H 1 3.860 0.005 . 2 . . . . 6 GLY HA2 . 25349 1 41 . 1 1 6 6 GLY HA3 H 1 3.859 0.002 . 2 . . . . 6 GLY HA3 . 25349 1 42 . 1 1 6 6 GLY C C 13 173.805 0.2 . 1 . . . . 6 GLY C . 25349 1 43 . 1 1 6 6 GLY CA C 13 45.259 0.111 . 1 . . . . 6 GLY CA . 25349 1 44 . 1 1 6 6 GLY N N 15 108.725 0.07 . 1 . . . . 6 GLY N . 25349 1 45 . 1 1 7 7 PHE H H 1 8.013 0.007 . 1 . . . . 7 PHE H . 25349 1 46 . 1 1 7 7 PHE HA H 1 4.634 0.034 . 1 . . . . 7 PHE HA . 25349 1 47 . 1 1 7 7 PHE HB2 H 1 3.173 0.008 . 2 . . . . 7 PHE HB2 . 25349 1 48 . 1 1 7 7 PHE HB3 H 1 2.955 0.008 . 2 . . . . 7 PHE HB3 . 25349 1 49 . 1 1 7 7 PHE HD1 H 1 7.256 0.007 . 1 . . . . 7 PHE HD1 . 25349 1 50 . 1 1 7 7 PHE HD2 H 1 7.256 0.007 . 1 . . . . 7 PHE HD2 . 25349 1 51 . 1 1 7 7 PHE HE1 H 1 7.356 0.007 . 1 . . . . 7 PHE HE1 . 25349 1 52 . 1 1 7 7 PHE HE2 H 1 7.356 0.007 . 1 . . . . 7 PHE HE2 . 25349 1 53 . 1 1 7 7 PHE C C 13 175.855 0.2 . 1 . . . . 7 PHE C . 25349 1 54 . 1 1 7 7 PHE CA C 13 57.204 0.075 . 1 . . . . 7 PHE CA . 25349 1 55 . 1 1 7 7 PHE CB C 13 39.549 0.107 . 1 . . . . 7 PHE CB . 25349 1 56 . 1 1 7 7 PHE CD1 C 13 131.69 0.023 . 1 . . . . 7 PHE CD1 . 25349 1 57 . 1 1 7 7 PHE CD2 C 13 131.69 0.023 . 1 . . . . 7 PHE CD2 . 25349 1 58 . 1 1 7 7 PHE CE1 C 13 131.53 0.2 . 1 . . . . 7 PHE CE1 . 25349 1 59 . 1 1 7 7 PHE CE2 C 13 131.53 0.2 . 1 . . . . 7 PHE CE2 . 25349 1 60 . 1 1 7 7 PHE N N 15 119.228 0.088 . 1 . . . . 7 PHE N . 25349 1 61 . 1 1 8 8 LEU H H 1 8.47 0.011 . 1 . . . . 8 LEU H . 25349 1 62 . 1 1 8 8 LEU HA H 1 4.256 0.007 . 1 . . . . 8 LEU HA . 25349 1 63 . 1 1 8 8 LEU HB2 H 1 1.683 0.005 . 2 . . . . 8 LEU HB2 . 25349 1 64 . 1 1 8 8 LEU HB3 H 1 1.481 0.005 . 2 . . . . 8 LEU HB3 . 25349 1 65 . 1 1 8 8 LEU HD11 H 1 0.801 0.002 . 2 . . . . 8 LEU HD11 . 25349 1 66 . 1 1 8 8 LEU HD12 H 1 0.801 0.002 . 2 . . . . 8 LEU HD12 . 25349 1 67 . 1 1 8 8 LEU HD13 H 1 0.801 0.002 . 2 . . . . 8 LEU HD13 . 25349 1 68 . 1 1 8 8 LEU HD21 H 1 0.801 0.002 . 2 . . . . 8 LEU HD21 . 25349 1 69 . 1 1 8 8 LEU HD22 H 1 0.801 0.002 . 2 . . . . 8 LEU HD22 . 25349 1 70 . 1 1 8 8 LEU HD23 H 1 0.801 0.002 . 2 . . . . 8 LEU HD23 . 25349 1 71 . 1 1 8 8 LEU HG H 1 0.981 0.004 . 1 . . . . 8 LEU HG . 25349 1 72 . 1 1 8 8 LEU CA C 13 52.639 0.126 . 1 . . . . 8 LEU CA . 25349 1 73 . 1 1 8 8 LEU CB C 13 42.311 0.108 . 1 . . . . 8 LEU CB . 25349 1 74 . 1 1 8 8 LEU CD1 C 13 24.11 0.025 . 1 . . . . 8 LEU CD1 . 25349 1 75 . 1 1 8 8 LEU CD2 C 13 24.104 0.033 . 1 . . . . 8 LEU CD2 . 25349 1 76 . 1 1 8 8 LEU CG C 13 25.808 0.009 . 1 . . . . 8 LEU CG . 25349 1 77 . 1 1 8 8 LEU N N 15 123.647 0.071 . 1 . . . . 8 LEU N . 25349 1 78 . 1 1 9 9 PRO HA H 1 4.442 0.005 . 1 . . . . 9 PRO HA . 25349 1 79 . 1 1 9 9 PRO HB2 H 1 2.355 0.003 . 2 . . . . 9 PRO HB2 . 25349 1 80 . 1 1 9 9 PRO HB3 H 1 1.853 0.005 . 2 . . . . 9 PRO HB3 . 25349 1 81 . 1 1 9 9 PRO HD2 H 1 3.363 0.005 . 2 . . . . 9 PRO HD2 . 25349 1 82 . 1 1 9 9 PRO HD3 H 1 2.718 0.004 . 2 . . . . 9 PRO HD3 . 25349 1 83 . 1 1 9 9 PRO HG2 H 1 1.268 0.007 . 2 . . . . 9 PRO HG2 . 25349 1 84 . 1 1 9 9 PRO HG3 H 1 1.638 0.002 . 2 . . . . 9 PRO HG3 . 25349 1 85 . 1 1 9 9 PRO C C 13 175.81 0.2 . 1 . . . . 9 PRO C . 25349 1 86 . 1 1 9 9 PRO CA C 13 62.015 0.076 . 1 . . . . 9 PRO CA . 25349 1 87 . 1 1 9 9 PRO CB C 13 31.417 0.022 . 1 . . . . 9 PRO CB . 25349 1 88 . 1 1 9 9 PRO CD C 13 50.079 0.029 . 1 . . . . 9 PRO CD . 25349 1 89 . 1 1 9 9 PRO CG C 13 27.051 0.023 . 1 . . . . 9 PRO CG . 25349 1 90 . 1 1 10 10 LYS H H 1 8.445 0.004 . 1 . . . . 10 LYS H . 25349 1 91 . 1 1 10 10 LYS HA H 1 4.196 0.006 . 1 . . . . 10 LYS HA . 25349 1 92 . 1 1 10 10 LYS HB2 H 1 1.872 0.011 . 2 . . . . 10 LYS HB2 . 25349 1 93 . 1 1 10 10 LYS HB3 H 1 1.875 0.008 . 2 . . . . 10 LYS HB3 . 25349 1 94 . 1 1 10 10 LYS HD2 H 1 1.758 0.007 . 2 . . . . 10 LYS HD2 . 25349 1 95 . 1 1 10 10 LYS HD3 H 1 1.772 0.033 . 2 . . . . 10 LYS HD3 . 25349 1 96 . 1 1 10 10 LYS HE2 H 1 3.038 0.017 . 2 . . . . 10 LYS HE2 . 25349 1 97 . 1 1 10 10 LYS HE3 H 1 3.039 0.018 . 2 . . . . 10 LYS HE3 . 25349 1 98 . 1 1 10 10 LYS HG2 H 1 1.592 0.022 . 2 . . . . 10 LYS HG2 . 25349 1 99 . 1 1 10 10 LYS HG3 H 1 1.568 0.034 . 2 . . . . 10 LYS HG3 . 25349 1 100 . 1 1 10 10 LYS C C 13 178.511 0.2 . 1 . . . . 10 LYS C . 25349 1 101 . 1 1 10 10 LYS CA C 13 58.233 0.041 . 1 . . . . 10 LYS CA . 25349 1 102 . 1 1 10 10 LYS CB C 13 32.512 0.035 . 1 . . . . 10 LYS CB . 25349 1 103 . 1 1 10 10 LYS CD C 13 29.344 0.04 . 1 . . . . 10 LYS CD . 25349 1 104 . 1 1 10 10 LYS CE C 13 42.283 0.086 . 1 . . . . 10 LYS CE . 25349 1 105 . 1 1 10 10 LYS CG C 13 24.769 0.024 . 1 . . . . 10 LYS CG . 25349 1 106 . 1 1 10 10 LYS N N 15 121.478 0.062 . 1 . . . . 10 LYS N . 25349 1 107 . 1 1 11 11 GLY H H 1 9.071 0.005 . 1 . . . . 11 GLY H . 25349 1 108 . 1 1 11 11 GLY HA2 H 1 4.313 0.007 . 2 . . . . 11 GLY HA2 . 25349 1 109 . 1 1 11 11 GLY HA3 H 1 3.849 0.008 . 2 . . . . 11 GLY HA3 . 25349 1 110 . 1 1 11 11 GLY C C 13 172.921 0.2 . 1 . . . . 11 GLY C . 25349 1 111 . 1 1 11 11 GLY CA C 13 45.879 0.108 . 1 . . . . 11 GLY CA . 25349 1 112 . 1 1 11 11 GLY N N 15 113.615 0.065 . 1 . . . . 11 GLY N . 25349 1 113 . 1 1 12 12 TRP H H 1 7.906 0.005 . 1 . . . . 12 TRP H . 25349 1 114 . 1 1 12 12 TRP HA H 1 5.834 0.008 . 1 . . . . 12 TRP HA . 25349 1 115 . 1 1 12 12 TRP HB2 H 1 3.308 0.014 . 2 . . . . 12 TRP HB2 . 25349 1 116 . 1 1 12 12 TRP HB3 H 1 3.101 0.008 . 2 . . . . 12 TRP HB3 . 25349 1 117 . 1 1 12 12 TRP HD1 H 1 7.052 0.006 . 1 . . . . 12 TRP HD1 . 25349 1 118 . 1 1 12 12 TRP HE1 H 1 10.347 0.004 . 1 . . . . 12 TRP HE1 . 25349 1 119 . 1 1 12 12 TRP HE3 H 1 7.335 0.018 . 1 . . . . 12 TRP HE3 . 25349 1 120 . 1 1 12 12 TRP HH2 H 1 7.134 0.013 . 1 . . . . 12 TRP HH2 . 25349 1 121 . 1 1 12 12 TRP HZ2 H 1 7.385 0.016 . 1 . . . . 12 TRP HZ2 . 25349 1 122 . 1 1 12 12 TRP HZ3 H 1 6.962 0.007 . 1 . . . . 12 TRP HZ3 . 25349 1 123 . 1 1 12 12 TRP C C 13 176.846 0.2 . 1 . . . . 12 TRP C . 25349 1 124 . 1 1 12 12 TRP CA C 13 56.65 0.088 . 1 . . . . 12 TRP CA . 25349 1 125 . 1 1 12 12 TRP CB C 13 31.262 0.034 . 1 . . . . 12 TRP CB . 25349 1 126 . 1 1 12 12 TRP CD1 C 13 126.924 0.024 . 1 . . . . 12 TRP CD1 . 25349 1 127 . 1 1 12 12 TRP CE3 C 13 119.304 0.024 . 1 . . . . 12 TRP CE3 . 25349 1 128 . 1 1 12 12 TRP CH2 C 13 124.139 0.015 . 1 . . . . 12 TRP CH2 . 25349 1 129 . 1 1 12 12 TRP CZ2 C 13 115.251 0.015 . 1 . . . . 12 TRP CZ2 . 25349 1 130 . 1 1 12 12 TRP CZ3 C 13 119.015 0.045 . 1 . . . . 12 TRP CZ3 . 25349 1 131 . 1 1 12 12 TRP N N 15 118.746 0.074 . 1 . . . . 12 TRP N . 25349 1 132 . 1 1 12 12 TRP NE1 N 15 130.156 0.04 . 1 . . . . 12 TRP NE1 . 25349 1 133 . 1 1 13 13 GLU H H 1 9.347 0.006 . 1 . . . . 13 GLU H . 25349 1 134 . 1 1 13 13 GLU HA H 1 4.81 0.015 . 1 . . . . 13 GLU HA . 25349 1 135 . 1 1 13 13 GLU HB2 H 1 2.36 0.007 . 1 . . . . 13 GLU HB2 . 25349 1 136 . 1 1 13 13 GLU HB3 H 1 2.36 0.007 . 1 . . . . 13 GLU HB3 . 25349 1 137 . 1 1 13 13 GLU HG2 H 1 2.128 0.02 . 2 . . . . 13 GLU HG2 . 25349 1 138 . 1 1 13 13 GLU HG3 H 1 2.127 0.02 . 2 . . . . 13 GLU HG3 . 25349 1 139 . 1 1 13 13 GLU C C 13 173.954 0.2 . 1 . . . . 13 GLU C . 25349 1 140 . 1 1 13 13 GLU CA C 13 54.909 0.1 . 1 . . . . 13 GLU CA . 25349 1 141 . 1 1 13 13 GLU CB C 13 34.138 0.057 . 1 . . . . 13 GLU CB . 25349 1 142 . 1 1 13 13 GLU CG C 13 36.619 0.056 . 1 . . . . 13 GLU CG . 25349 1 143 . 1 1 13 13 GLU N N 15 121.833 0.074 . 1 . . . . 13 GLU N . 25349 1 144 . 1 1 14 14 VAL H H 1 8.545 0.006 . 1 . . . . 14 VAL H . 25349 1 145 . 1 1 14 14 VAL HA H 1 4.637 0.009 . 1 . . . . 14 VAL HA . 25349 1 146 . 1 1 14 14 VAL HB H 1 1.897 0.007 . 1 . . . . 14 VAL HB . 25349 1 147 . 1 1 14 14 VAL HG11 H 1 0.65 0.003 . 2 . . . . 14 VAL HG11 . 25349 1 148 . 1 1 14 14 VAL HG12 H 1 0.65 0.003 . 2 . . . . 14 VAL HG12 . 25349 1 149 . 1 1 14 14 VAL HG13 H 1 0.65 0.003 . 2 . . . . 14 VAL HG13 . 25349 1 150 . 1 1 14 14 VAL HG21 H 1 0.781 0.007 . 2 . . . . 14 VAL HG21 . 25349 1 151 . 1 1 14 14 VAL HG22 H 1 0.781 0.007 . 2 . . . . 14 VAL HG22 . 25349 1 152 . 1 1 14 14 VAL HG23 H 1 0.781 0.007 . 2 . . . . 14 VAL HG23 . 25349 1 153 . 1 1 14 14 VAL C C 13 174.416 0.2 . 1 . . . . 14 VAL C . 25349 1 154 . 1 1 14 14 VAL CA C 13 60.025 0.075 . 1 . . . . 14 VAL CA . 25349 1 155 . 1 1 14 14 VAL CB C 13 33.861 0.067 . 1 . . . . 14 VAL CB . 25349 1 156 . 1 1 14 14 VAL CG1 C 13 22.462 0.009 . 2 . . . . 14 VAL CG1 . 25349 1 157 . 1 1 14 14 VAL CG2 C 13 19.752 0.03 . 2 . . . . 14 VAL CG2 . 25349 1 158 . 1 1 14 14 VAL N N 15 123.137 0.074 . 1 . . . . 14 VAL N . 25349 1 159 . 1 1 15 15 ARG H H 1 8.246 0.006 . 1 . . . . 15 ARG H . 25349 1 160 . 1 1 15 15 ARG HA H 1 4.314 0.006 . 1 . . . . 15 ARG HA . 25349 1 161 . 1 1 15 15 ARG HB2 H 1 1.296 0.004 . 2 . . . . 15 ARG HB2 . 25349 1 162 . 1 1 15 15 ARG HB3 H 1 0.211 0.005 . 2 . . . . 15 ARG HB3 . 25349 1 163 . 1 1 15 15 ARG HD2 H 1 3.141 0.011 . 2 . . . . 15 ARG HD2 . 25349 1 164 . 1 1 15 15 ARG HD3 H 1 2.93 0.005 . 2 . . . . 15 ARG HD3 . 25349 1 165 . 1 1 15 15 ARG HE H 1 7.125 0.041 . 1 . . . . 15 ARG HE . 25349 1 166 . 1 1 15 15 ARG HG2 H 1 1.187 0.004 . 2 . . . . 15 ARG HG2 . 25349 1 167 . 1 1 15 15 ARG HG3 H 1 1.297 0.01 . 2 . . . . 15 ARG HG3 . 25349 1 168 . 1 1 15 15 ARG C C 13 173.405 0.2 . 1 . . . . 15 ARG C . 25349 1 169 . 1 1 15 15 ARG CA C 13 53.582 0.077 . 1 . . . . 15 ARG CA . 25349 1 170 . 1 1 15 15 ARG CB C 13 33.831 0.046 . 1 . . . . 15 ARG CB . 25349 1 171 . 1 1 15 15 ARG CD C 13 43.354 0.107 . 1 . . . . 15 ARG CD . 25349 1 172 . 1 1 15 15 ARG CG C 13 27.541 0.049 . 1 . . . . 15 ARG CG . 25349 1 173 . 1 1 15 15 ARG N N 15 127.139 0.059 . 1 . . . . 15 ARG N . 25349 1 174 . 1 1 15 15 ARG NE N 15 116.081 0.2 . 1 . . . . 15 ARG NE . 25349 1 175 . 1 1 16 16 HIS H H 1 8.197 0.007 . 1 . . . . 16 HIS H . 25349 1 176 . 1 1 16 16 HIS HA H 1 4.956 0.013 . 1 . . . . 16 HIS HA . 25349 1 177 . 1 1 16 16 HIS HB2 H 1 2.858 0.008 . 2 . . . . 16 HIS HB2 . 25349 1 178 . 1 1 16 16 HIS HB3 H 1 2.858 0.008 . 2 . . . . 16 HIS HB3 . 25349 1 179 . 1 1 16 16 HIS HD2 H 1 6.932 0.01 . 1 . . . . 16 HIS HD2 . 25349 1 180 . 1 1 16 16 HIS HE1 H 1 7.961 0.006 . 1 . . . . 16 HIS HE1 . 25349 1 181 . 1 1 16 16 HIS C C 13 175.392 0.2 . 1 . . . . 16 HIS C . 25349 1 182 . 1 1 16 16 HIS CA C 13 56.284 0.034 . 1 . . . . 16 HIS CA . 25349 1 183 . 1 1 16 16 HIS CB C 13 31.783 0.054 . 1 . . . . 16 HIS CB . 25349 1 184 . 1 1 16 16 HIS CD2 C 13 120.225 0.063 . 1 . . . . 16 HIS CD2 . 25349 1 185 . 1 1 16 16 HIS N N 15 115.693 0.071 . 1 . . . . 16 HIS N . 25349 1 186 . 1 1 17 17 ALA H H 1 9.095 0.005 . 1 . . . . 17 ALA H . 25349 1 187 . 1 1 17 17 ALA HA H 1 4.681 0.012 . 1 . . . . 17 ALA HA . 25349 1 188 . 1 1 17 17 ALA HB1 H 1 1.824 0.005 . 1 . . . . 17 ALA HB1 . 25349 1 189 . 1 1 17 17 ALA HB2 H 1 1.824 0.005 . 1 . . . . 17 ALA HB2 . 25349 1 190 . 1 1 17 17 ALA HB3 H 1 1.824 0.005 . 1 . . . . 17 ALA HB3 . 25349 1 191 . 1 1 17 17 ALA CA C 13 50.955 0.184 . 1 . . . . 17 ALA CA . 25349 1 192 . 1 1 17 17 ALA CB C 13 17.816 0.034 . 1 . . . . 17 ALA CB . 25349 1 193 . 1 1 17 17 ALA N N 15 127.216 0.085 . 1 . . . . 17 ALA N . 25349 1 194 . 1 1 18 18 PRO HA H 1 4.363 0.006 . 1 . . . . 18 PRO HA . 25349 1 195 . 1 1 18 18 PRO HB2 H 1 2.393 0.008 . 2 . . . . 18 PRO HB2 . 25349 1 196 . 1 1 18 18 PRO HB3 H 1 1.842 0.012 . 2 . . . . 18 PRO HB3 . 25349 1 197 . 1 1 18 18 PRO HD2 H 1 3.712 0.018 . 2 . . . . 18 PRO HD2 . 25349 1 198 . 1 1 18 18 PRO HD3 H 1 3.713 0.015 . 2 . . . . 18 PRO HD3 . 25349 1 199 . 1 1 18 18 PRO HG2 H 1 1.973 0.017 . 2 . . . . 18 PRO HG2 . 25349 1 200 . 1 1 18 18 PRO HG3 H 1 1.963 0.004 . 2 . . . . 18 PRO HG3 . 25349 1 201 . 1 1 18 18 PRO C C 13 176.801 0.2 . 1 . . . . 18 PRO C . 25349 1 202 . 1 1 18 18 PRO CA C 13 65.484 0.06 . 1 . . . . 18 PRO CA . 25349 1 203 . 1 1 18 18 PRO CB C 13 31.604 0.055 . 1 . . . . 18 PRO CB . 25349 1 204 . 1 1 18 18 PRO CD C 13 50.543 0.2 . 1 . . . . 18 PRO CD . 25349 1 205 . 1 1 18 18 PRO CG C 13 27.892 0.048 . 1 . . . . 18 PRO CG . 25349 1 206 . 1 1 19 19 ASN H H 1 7.732 0.008 . 1 . . . . 19 ASN H . 25349 1 207 . 1 1 19 19 ASN HA H 1 4.656 0.009 . 1 . . . . 19 ASN HA . 25349 1 208 . 1 1 19 19 ASN HB2 H 1 3.246 0.007 . 1 . . . . 19 ASN HB2 . 25349 1 209 . 1 1 19 19 ASN HB3 H 1 2.88 0.005 . 1 . . . . 19 ASN HB3 . 25349 1 210 . 1 1 19 19 ASN HD21 H 1 7.525 0.003 . 1 . . . . 19 ASN HD21 . 25349 1 211 . 1 1 19 19 ASN HD22 H 1 6.394 0.005 . 1 . . . . 19 ASN HD22 . 25349 1 212 . 1 1 19 19 ASN C C 13 176.337 0.2 . 1 . . . . 19 ASN C . 25349 1 213 . 1 1 19 19 ASN CB C 13 37.467 0.082 . 1 . . . . 19 ASN CB . 25349 1 214 . 1 1 19 19 ASN N N 15 112.324 0.077 . 1 . . . . 19 ASN N . 25349 1 215 . 1 1 19 19 ASN ND2 N 15 109.101 0.023 . 1 . . . . 19 ASN ND2 . 25349 1 216 . 1 1 20 20 GLY H H 1 8.577 0.005 . 1 . . . . 20 GLY H . 25349 1 217 . 1 1 20 20 GLY HA2 H 1 4.350 0.005 . 2 . . . . 20 GLY HA2 . 25349 1 218 . 1 1 20 20 GLY HA3 H 1 3.725 0.009 . 2 . . . . 20 GLY HA3 . 25349 1 219 . 1 1 20 20 GLY C C 13 174.207 0.2 . 1 . . . . 20 GLY C . 25349 1 220 . 1 1 20 20 GLY CA C 13 45.235 0.155 . 1 . . . . 20 GLY CA . 25349 1 221 . 1 1 20 20 GLY N N 15 108.672 0.074 . 1 . . . . 20 GLY N . 25349 1 222 . 1 1 21 21 ARG H H 1 7.813 0.01 . 1 . . . . 21 ARG H . 25349 1 223 . 1 1 21 21 ARG HA H 1 4.724 0.005 . 1 . . . . 21 ARG HA . 25349 1 224 . 1 1 21 21 ARG HB2 H 1 2.029 0.008 . 2 . . . . 21 ARG HB2 . 25349 1 225 . 1 1 21 21 ARG HB3 H 1 2.029 0.008 . 2 . . . . 21 ARG HB3 . 25349 1 226 . 1 1 21 21 ARG HD2 H 1 2.958 0.004 . 2 . . . . 21 ARG HD2 . 25349 1 227 . 1 1 21 21 ARG HD3 H 1 2.716 0.005 . 2 . . . . 21 ARG HD3 . 25349 1 228 . 1 1 21 21 ARG HE H 1 7.137 0.004 . 1 . . . . 21 ARG HE . 25349 1 229 . 1 1 21 21 ARG HG2 H 1 1.773 0.003 . 2 . . . . 21 ARG HG2 . 25349 1 230 . 1 1 21 21 ARG HG3 H 1 1.907 0.008 . 2 . . . . 21 ARG HG3 . 25349 1 231 . 1 1 21 21 ARG CA C 13 54.55 0.05 . 1 . . . . 21 ARG CA . 25349 1 232 . 1 1 21 21 ARG CB C 13 31.351 0.06 . 1 . . . . 21 ARG CB . 25349 1 233 . 1 1 21 21 ARG CD C 13 43.859 0.108 . 1 . . . . 21 ARG CD . 25349 1 234 . 1 1 21 21 ARG CG C 13 26.623 0.045 . 1 . . . . 21 ARG CG . 25349 1 235 . 1 1 21 21 ARG N N 15 123.427 0.067 . 1 . . . . 21 ARG N . 25349 1 236 . 1 1 21 21 ARG NE N 15 115.678 0.2 . 1 . . . . 21 ARG NE . 25349 1 237 . 1 1 22 22 PRO HA H 1 4.798 0.007 . 1 . . . . 22 PRO HA . 25349 1 238 . 1 1 22 22 PRO HB2 H 1 1.732 0.005 . 2 . . . . 22 PRO HB2 . 25349 1 239 . 1 1 22 22 PRO HB3 H 1 1.511 0.004 . 2 . . . . 22 PRO HB3 . 25349 1 240 . 1 1 22 22 PRO HD2 H 1 4.144 0.006 . 2 . . . . 22 PRO HD2 . 25349 1 241 . 1 1 22 22 PRO HD3 H 1 3.899 0.005 . 2 . . . . 22 PRO HD3 . 25349 1 242 . 1 1 22 22 PRO HG2 H 1 2.307 0.006 . 2 . . . . 22 PRO HG2 . 25349 1 243 . 1 1 22 22 PRO HG3 H 1 2.143 0.006 . 2 . . . . 22 PRO HG3 . 25349 1 244 . 1 1 22 22 PRO C C 13 175.485 0.2 . 1 . . . . 22 PRO C . 25349 1 245 . 1 1 22 22 PRO CA C 13 62.371 0.009 . 1 . . . . 22 PRO CA . 25349 1 246 . 1 1 22 22 PRO CB C 13 32.178 0.03 . 1 . . . . 22 PRO CB . 25349 1 247 . 1 1 22 22 PRO CD C 13 50.611 0.207 . 1 . . . . 22 PRO CD . 25349 1 248 . 1 1 22 22 PRO CG C 13 27.31 0.023 . 1 . . . . 22 PRO CG . 25349 1 249 . 1 1 23 23 PHE H H 1 8.362 0.007 . 1 . . . . 23 PHE H . 25349 1 250 . 1 1 23 23 PHE HA H 1 4.606 0.007 . 1 . . . . 23 PHE HA . 25349 1 251 . 1 1 23 23 PHE HB2 H 1 2.460 0.011 . 2 . . . . 23 PHE HB2 . 25349 1 252 . 1 1 23 23 PHE HB3 H 1 2.261 0.011 . 2 . . . . 23 PHE HB3 . 25349 1 253 . 1 1 23 23 PHE HD1 H 1 6.671 0.006 . 1 . . . . 23 PHE HD1 . 25349 1 254 . 1 1 23 23 PHE HD2 H 1 6.671 0.006 . 1 . . . . 23 PHE HD2 . 25349 1 255 . 1 1 23 23 PHE HE1 H 1 6.859 0.008 . 1 . . . . 23 PHE HE1 . 25349 1 256 . 1 1 23 23 PHE HE2 H 1 6.859 0.008 . 1 . . . . 23 PHE HE2 . 25349 1 257 . 1 1 23 23 PHE C C 13 171.675 0.2 . 1 . . . . 23 PHE C . 25349 1 258 . 1 1 23 23 PHE CA C 13 55.689 0.139 . 1 . . . . 23 PHE CA . 25349 1 259 . 1 1 23 23 PHE CB C 13 40.163 0.17 . 1 . . . . 23 PHE CB . 25349 1 260 . 1 1 23 23 PHE CD1 C 13 132.302 0.019 . 1 . . . . 23 PHE CD1 . 25349 1 261 . 1 1 23 23 PHE CD2 C 13 132.302 0.019 . 1 . . . . 23 PHE CD2 . 25349 1 262 . 1 1 23 23 PHE CE1 C 13 130.403 0.041 . 1 . . . . 23 PHE CE1 . 25349 1 263 . 1 1 23 23 PHE CE2 C 13 130.403 0.041 . 1 . . . . 23 PHE CE2 . 25349 1 264 . 1 1 23 23 PHE N N 15 117.25 0.062 . 1 . . . . 23 PHE N . 25349 1 265 . 1 1 24 24 PHE H H 1 8.775 0.011 . 1 . . . . 24 PHE H . 25349 1 266 . 1 1 24 24 PHE HA H 1 5.212 0.011 . 1 . . . . 24 PHE HA . 25349 1 267 . 1 1 24 24 PHE HB2 H 1 3.183 0.01 . 2 . . . . 24 PHE HB2 . 25349 1 268 . 1 1 24 24 PHE HB3 H 1 3.182 0.01 . 2 . . . . 24 PHE HB3 . 25349 1 269 . 1 1 24 24 PHE HD1 H 1 7.061 0.005 . 1 . . . . 24 PHE HD1 . 25349 1 270 . 1 1 24 24 PHE HD2 H 1 7.061 0.005 . 1 . . . . 24 PHE HD2 . 25349 1 271 . 1 1 24 24 PHE HE1 H 1 7.185 0.01 . 1 . . . . 24 PHE HE1 . 25349 1 272 . 1 1 24 24 PHE HE2 H 1 7.185 0.01 . 1 . . . . 24 PHE HE2 . 25349 1 273 . 1 1 24 24 PHE C C 13 174.481 0.2 . 1 . . . . 24 PHE C . 25349 1 274 . 1 1 24 24 PHE CA C 13 56.924 0.092 . 1 . . . . 24 PHE CA . 25349 1 275 . 1 1 24 24 PHE CB C 13 41.665 0.093 . 1 . . . . 24 PHE CB . 25349 1 276 . 1 1 24 24 PHE CD1 C 13 132.305 0.023 . 1 . . . . 24 PHE CD1 . 25349 1 277 . 1 1 24 24 PHE CD2 C 13 132.305 0.023 . 1 . . . . 24 PHE CD2 . 25349 1 278 . 1 1 24 24 PHE CE1 C 13 130.779 0.015 . 1 . . . . 24 PHE CE1 . 25349 1 279 . 1 1 24 24 PHE CE2 C 13 130.779 0.015 . 1 . . . . 24 PHE CE2 . 25349 1 280 . 1 1 24 24 PHE N N 15 117.735 0.088 . 1 . . . . 24 PHE N . 25349 1 281 . 1 1 25 25 ILE H H 1 9.092 0.009 . 1 . . . . 25 ILE H . 25349 1 282 . 1 1 25 25 ILE HA H 1 4.321 0.006 . 1 . . . . 25 ILE HA . 25349 1 283 . 1 1 25 25 ILE HB H 1 1.381 0.016 . 1 . . . . 25 ILE HB . 25349 1 284 . 1 1 25 25 ILE HD11 H 1 0.17 0.005 . 1 . . . . 25 ILE HD11 . 25349 1 285 . 1 1 25 25 ILE HD12 H 1 0.17 0.005 . 1 . . . . 25 ILE HD12 . 25349 1 286 . 1 1 25 25 ILE HD13 H 1 0.17 0.005 . 1 . . . . 25 ILE HD13 . 25349 1 287 . 1 1 25 25 ILE HG12 H 1 0.885 0.018 . 2 . . . . 25 ILE HG12 . 25349 1 288 . 1 1 25 25 ILE HG13 H 1 1.251 0.003 . 2 . . . . 25 ILE HG13 . 25349 1 289 . 1 1 25 25 ILE HG21 H 1 0.641 0.003 . 1 . . . . 25 ILE HG21 . 25349 1 290 . 1 1 25 25 ILE HG22 H 1 0.641 0.003 . 1 . . . . 25 ILE HG22 . 25349 1 291 . 1 1 25 25 ILE HG23 H 1 0.641 0.003 . 1 . . . . 25 ILE HG23 . 25349 1 292 . 1 1 25 25 ILE C C 13 173.95 0.2 . 1 . . . . 25 ILE C . 25349 1 293 . 1 1 25 25 ILE CA C 13 59.986 0.039 . 1 . . . . 25 ILE CA . 25349 1 294 . 1 1 25 25 ILE CB C 13 41.105 0.078 . 1 . . . . 25 ILE CB . 25349 1 295 . 1 1 25 25 ILE CD1 C 13 16.3 0.043 . 1 . . . . 25 ILE CD1 . 25349 1 296 . 1 1 25 25 ILE CG1 C 13 27.459 0.023 . 1 . . . . 25 ILE CG1 . 25349 1 297 . 1 1 25 25 ILE CG2 C 13 14.177 0.051 . 1 . . . . 25 ILE CG2 . 25349 1 298 . 1 1 25 25 ILE N N 15 122.391 0.083 . 1 . . . . 25 ILE N . 25349 1 299 . 1 1 26 26 ASP H H 1 8.182 0.004 . 1 . . . . 26 ASP H . 25349 1 300 . 1 1 26 26 ASP HA H 1 3.677 0.02 . 1 . . . . 26 ASP HA . 25349 1 301 . 1 1 26 26 ASP HB2 H 1 2.056 0.008 . 2 . . . . 26 ASP HB2 . 25349 1 302 . 1 1 26 26 ASP HB3 H 1 0.263 0.05 . 2 . . . . 26 ASP HB3 . 25349 1 303 . 1 1 26 26 ASP C C 13 177.841 0.2 . 1 . . . . 26 ASP C . 25349 1 304 . 1 1 26 26 ASP CA C 13 51.384 0.109 . 1 . . . . 26 ASP CA . 25349 1 305 . 1 1 26 26 ASP CB C 13 39.595 0.095 . 1 . . . . 26 ASP CB . 25349 1 306 . 1 1 26 26 ASP N N 15 124.611 0.058 . 1 . . . . 26 ASP N . 25349 1 307 . 1 1 27 27 HIS H H 1 8.719 0.007 . 1 . . . . 27 HIS H . 25349 1 308 . 1 1 27 27 HIS HA H 1 4.234 0.027 . 1 . . . . 27 HIS HA . 25349 1 309 . 1 1 27 27 HIS HB2 H 1 3.357 0.007 . 1 . . . . 27 HIS HB2 . 25349 1 310 . 1 1 27 27 HIS HB3 H 1 3.071 0.01 . 1 . . . . 27 HIS HB3 . 25349 1 311 . 1 1 27 27 HIS HD2 H 1 6.973 0.015 . 1 . . . . 27 HIS HD2 . 25349 1 312 . 1 1 27 27 HIS HE1 H 1 7.912 0.005 . 1 . . . . 27 HIS HE1 . 25349 1 313 . 1 1 27 27 HIS HE2 H 1 8.124 0.004 . 1 . . . . 27 HIS HE2 . 25349 1 314 . 1 1 27 27 HIS C C 13 176.759 0.2 . 1 . . . . 27 HIS C . 25349 1 315 . 1 1 27 27 HIS CA C 13 58.504 0.105 . 1 . . . . 27 HIS CA . 25349 1 316 . 1 1 27 27 HIS CB C 13 29.71 0.029 . 1 . . . . 27 HIS CB . 25349 1 317 . 1 1 27 27 HIS CD2 C 13 121.968 0.036 . 1 . . . . 27 HIS CD2 . 25349 1 318 . 1 1 27 27 HIS N N 15 122.958 0.062 . 1 . . . . 27 HIS N . 25349 1 319 . 1 1 28 28 ASN H H 1 8.437 0.006 . 1 . . . . 28 ASN H . 25349 1 320 . 1 1 28 28 ASN HA H 1 4.477 0.01 . 1 . . . . 28 ASN HA . 25349 1 321 . 1 1 28 28 ASN HB2 H 1 3.254 0.005 . 2 . . . . 28 ASN HB2 . 25349 1 322 . 1 1 28 28 ASN HB3 H 1 2.739 0.008 . 2 . . . . 28 ASN HB3 . 25349 1 323 . 1 1 28 28 ASN HD21 H 1 8.041 0.006 . 1 . . . . 28 ASN HD21 . 25349 1 324 . 1 1 28 28 ASN HD22 H 1 7.613 0.015 . 1 . . . . 28 ASN HD22 . 25349 1 325 . 1 1 28 28 ASN CA C 13 55.791 0.109 . 1 . . . . 28 ASN CA . 25349 1 326 . 1 1 28 28 ASN CB C 13 38.766 0.064 . 1 . . . . 28 ASN CB . 25349 1 327 . 1 1 28 28 ASN N N 15 116.109 0.072 . 1 . . . . 28 ASN N . 25349 1 328 . 1 1 28 28 ASN ND2 N 15 117.346 0.033 . 1 . . . . 28 ASN ND2 . 25349 1 329 . 1 1 29 29 THR H H 1 6.738 0.015 . 1 . . . . 29 THR H . 25349 1 330 . 1 1 29 29 THR HA H 1 4.317 0.006 . 1 . . . . 29 THR HA . 25349 1 331 . 1 1 29 29 THR HB H 1 4.312 0.002 . 1 . . . . 29 THR HB . 25349 1 332 . 1 1 29 29 THR HG21 H 1 1.158 0.005 . 1 . . . . 29 THR HG21 . 25349 1 333 . 1 1 29 29 THR HG22 H 1 1.158 0.005 . 1 . . . . 29 THR HG22 . 25349 1 334 . 1 1 29 29 THR HG23 H 1 1.158 0.005 . 1 . . . . 29 THR HG23 . 25349 1 335 . 1 1 29 29 THR C C 13 174.417 0.2 . 1 . . . . 29 THR C . 25349 1 336 . 1 1 29 29 THR CA C 13 61.128 0.041 . 1 . . . . 29 THR CA . 25349 1 337 . 1 1 29 29 THR CB C 13 70.544 0.038 . 1 . . . . 29 THR CB . 25349 1 338 . 1 1 29 29 THR CG2 C 13 21.149 0.023 . 1 . . . . 29 THR CG2 . 25349 1 339 . 1 1 29 29 THR N N 15 104.932 0.2 . 1 . . . . 29 THR N . 25349 1 340 . 1 1 30 30 LYS H H 1 8.023 0.006 . 1 . . . . 30 LYS H . 25349 1 341 . 1 1 30 30 LYS HA H 1 3.793 0.022 . 1 . . . . 30 LYS HA . 25349 1 342 . 1 1 30 30 LYS HB2 H 1 2.076 0.007 . 2 . . . . 30 LYS HB2 . 25349 1 343 . 1 1 30 30 LYS HB3 H 1 2.077 0.007 . 2 . . . . 30 LYS HB3 . 25349 1 344 . 1 1 30 30 LYS HD2 H 1 1.811 0.009 . 2 . . . . 30 LYS HD2 . 25349 1 345 . 1 1 30 30 LYS HD3 H 1 1.632 0.008 . 2 . . . . 30 LYS HD3 . 25349 1 346 . 1 1 30 30 LYS HE2 H 1 3.003 0.009 . 2 . . . . 30 LYS HE2 . 25349 1 347 . 1 1 30 30 LYS HE3 H 1 3.001 0.008 . 2 . . . . 30 LYS HE3 . 25349 1 348 . 1 1 30 30 LYS HG2 H 1 1.31 0.006 . 2 . . . . 30 LYS HG2 . 25349 1 349 . 1 1 30 30 LYS HG3 H 1 1.31 0.006 . 2 . . . . 30 LYS HG3 . 25349 1 350 . 1 1 30 30 LYS C C 13 175.862 0.2 . 1 . . . . 30 LYS C . 25349 1 351 . 1 1 30 30 LYS CA C 13 56.996 0.151 . 1 . . . . 30 LYS CA . 25349 1 352 . 1 1 30 30 LYS CB C 13 29.412 0.083 . 1 . . . . 30 LYS CB . 25349 1 353 . 1 1 30 30 LYS CD C 13 29.05 0.134 . 1 . . . . 30 LYS CD . 25349 1 354 . 1 1 30 30 LYS CE C 13 42.529 0.082 . 1 . . . . 30 LYS CE . 25349 1 355 . 1 1 30 30 LYS CG C 13 24.991 0.04 . 1 . . . . 30 LYS CG . 25349 1 356 . 1 1 30 30 LYS N N 15 119.758 0.059 . 1 . . . . 30 LYS N . 25349 1 357 . 1 1 31 31 THR H H 1 7.462 0.008 . 1 . . . . 31 THR H . 25349 1 358 . 1 1 31 31 THR HA H 1 4.574 0.019 . 1 . . . . 31 THR HA . 25349 1 359 . 1 1 31 31 THR HB H 1 3.978 0.012 . 1 . . . . 31 THR HB . 25349 1 360 . 1 1 31 31 THR HG21 H 1 1.136 0.007 . 1 . . . . 31 THR HG21 . 25349 1 361 . 1 1 31 31 THR HG22 H 1 1.136 0.007 . 1 . . . . 31 THR HG22 . 25349 1 362 . 1 1 31 31 THR HG23 H 1 1.136 0.007 . 1 . . . . 31 THR HG23 . 25349 1 363 . 1 1 31 31 THR C C 13 173.355 0.2 . 1 . . . . 31 THR C . 25349 1 364 . 1 1 31 31 THR CA C 13 60.997 0.045 . 1 . . . . 31 THR CA . 25349 1 365 . 1 1 31 31 THR CB C 13 71.856 0.035 . 1 . . . . 31 THR CB . 25349 1 366 . 1 1 31 31 THR CG2 C 13 21.42 0.038 . 1 . . . . 31 THR CG2 . 25349 1 367 . 1 1 31 31 THR N N 15 111.267 0.082 . 1 . . . . 31 THR N . 25349 1 368 . 1 1 32 32 THR H H 1 8.294 0.007 . 1 . . . . 32 THR H . 25349 1 369 . 1 1 32 32 THR HA H 1 5.197 0.006 . 1 . . . . 32 THR HA . 25349 1 370 . 1 1 32 32 THR HB H 1 3.835 0.016 . 1 . . . . 32 THR HB . 25349 1 371 . 1 1 32 32 THR HG21 H 1 0.98 0.004 . 1 . . . . 32 THR HG21 . 25349 1 372 . 1 1 32 32 THR HG22 H 1 0.98 0.004 . 1 . . . . 32 THR HG22 . 25349 1 373 . 1 1 32 32 THR HG23 H 1 0.98 0.004 . 1 . . . . 32 THR HG23 . 25349 1 374 . 1 1 32 32 THR C C 13 173.714 0.2 . 1 . . . . 32 THR C . 25349 1 375 . 1 1 32 32 THR CA C 13 60.597 0.082 . 1 . . . . 32 THR CA . 25349 1 376 . 1 1 32 32 THR CB C 13 71.058 0.122 . 1 . . . . 32 THR CB . 25349 1 377 . 1 1 32 32 THR CG2 C 13 21.882 0.023 . 1 . . . . 32 THR CG2 . 25349 1 378 . 1 1 32 32 THR N N 15 115.966 0.053 . 1 . . . . 32 THR N . 25349 1 379 . 1 1 33 33 THR H H 1 9.181 0.007 . 1 . . . . 33 THR H . 25349 1 380 . 1 1 33 33 THR HA H 1 4.813 0.013 . 1 . . . . 33 THR HA . 25349 1 381 . 1 1 33 33 THR HB H 1 4.351 0.006 . 1 . . . . 33 THR HB . 25349 1 382 . 1 1 33 33 THR HG21 H 1 1.556 0.004 . 1 . . . . 33 THR HG21 . 25349 1 383 . 1 1 33 33 THR HG22 H 1 1.556 0.004 . 1 . . . . 33 THR HG22 . 25349 1 384 . 1 1 33 33 THR HG23 H 1 1.556 0.004 . 1 . . . . 33 THR HG23 . 25349 1 385 . 1 1 33 33 THR C C 13 172.228 0.2 . 1 . . . . 33 THR C . 25349 1 386 . 1 1 33 33 THR CA C 13 59.37 0.118 . 1 . . . . 33 THR CA . 25349 1 387 . 1 1 33 33 THR CB C 13 69.742 0.033 . 1 . . . . 33 THR CB . 25349 1 388 . 1 1 33 33 THR CG2 C 13 20.273 0.028 . 1 . . . . 33 THR CG2 . 25349 1 389 . 1 1 33 33 THR N N 15 118.179 0.077 . 1 . . . . 33 THR N . 25349 1 390 . 1 1 34 34 TRP H H 1 8.7 0.009 . 1 . . . . 34 TRP H . 25349 1 391 . 1 1 34 34 TRP HA H 1 5.063 0.01 . 1 . . . . 34 TRP HA . 25349 1 392 . 1 1 34 34 TRP HB2 H 1 3.726 0.007 . 2 . . . . 34 TRP HB2 . 25349 1 393 . 1 1 34 34 TRP HB3 H 1 3.177 0.007 . 2 . . . . 34 TRP HB3 . 25349 1 394 . 1 1 34 34 TRP HD1 H 1 7.369 0.026 . 1 . . . . 34 TRP HD1 . 25349 1 395 . 1 1 34 34 TRP HE1 H 1 10.061 0.002 . 1 . . . . 34 TRP HE1 . 25349 1 396 . 1 1 34 34 TRP HH2 H 1 6.999 0.006 . 1 . . . . 34 TRP HH2 . 25349 1 397 . 1 1 34 34 TRP HZ2 H 1 7.279 0.006 . 1 . . . . 34 TRP HZ2 . 25349 1 398 . 1 1 34 34 TRP HZ3 H 1 6.847 0.003 . 1 . . . . 34 TRP HZ3 . 25349 1 399 . 1 1 34 34 TRP C C 13 176.658 0.2 . 1 . . . . 34 TRP C . 25349 1 400 . 1 1 34 34 TRP CA C 13 57.917 0.265 . 1 . . . . 34 TRP CA . 25349 1 401 . 1 1 34 34 TRP CB C 13 30.45 0.025 . 1 . . . . 34 TRP CB . 25349 1 402 . 1 1 34 34 TRP CD1 C 13 128.008 0.013 . 1 . . . . 34 TRP CD1 . 25349 1 403 . 1 1 34 34 TRP CH2 C 13 123.98 0.016 . 1 . . . . 34 TRP CH2 . 25349 1 404 . 1 1 34 34 TRP CZ2 C 13 114.25 0.004 . 1 . . . . 34 TRP CZ2 . 25349 1 405 . 1 1 34 34 TRP CZ3 C 13 121.313 0.02 . 1 . . . . 34 TRP CZ3 . 25349 1 406 . 1 1 34 34 TRP N N 15 124.933 0.071 . 1 . . . . 34 TRP N . 25349 1 407 . 1 1 34 34 TRP NE1 N 15 128.742 0.016 . 1 . . . . 34 TRP NE1 . 25349 1 408 . 1 1 35 35 GLU H H 1 8.65 0.006 . 1 . . . . 35 GLU H . 25349 1 409 . 1 1 35 35 GLU HA H 1 4.354 0.005 . 1 . . . . 35 GLU HA . 25349 1 410 . 1 1 35 35 GLU HB2 H 1 1.919 0.005 . 2 . . . . 35 GLU HB2 . 25349 1 411 . 1 1 35 35 GLU HB3 H 1 1.919 0.005 . 2 . . . . 35 GLU HB3 . 25349 1 412 . 1 1 35 35 GLU HG2 H 1 2.17 0.036 . 2 . . . . 35 GLU HG2 . 25349 1 413 . 1 1 35 35 GLU HG3 H 1 2.218 0.044 . 2 . . . . 35 GLU HG3 . 25349 1 414 . 1 1 35 35 GLU C C 13 174.243 0.2 . 1 . . . . 35 GLU C . 25349 1 415 . 1 1 35 35 GLU CA C 13 55.664 0.129 . 1 . . . . 35 GLU CA . 25349 1 416 . 1 1 35 35 GLU CB C 13 30.419 0.022 . 1 . . . . 35 GLU CB . 25349 1 417 . 1 1 35 35 GLU CG C 13 36.329 0.044 . 1 . . . . 35 GLU CG . 25349 1 418 . 1 1 35 35 GLU N N 15 122.061 0.071 . 1 . . . . 35 GLU N . 25349 1 419 . 1 1 36 36 ASP H H 1 8.21 0.007 . 1 . . . . 36 ASP H . 25349 1 420 . 1 1 36 36 ASP HA H 1 2.823 0.05 . 1 . . . . 36 ASP HA . 25349 1 421 . 1 1 36 36 ASP HB2 H 1 2.65 0.009 . 2 . . . . 36 ASP HB2 . 25349 1 422 . 1 1 36 36 ASP HB3 H 1 2.326 0.007 . 2 . . . . 36 ASP HB3 . 25349 1 423 . 1 1 36 36 ASP CA C 13 50.762 0.008 . 1 . . . . 36 ASP CA . 25349 1 424 . 1 1 36 36 ASP CB C 13 42.073 0.064 . 1 . . . . 36 ASP CB . 25349 1 425 . 1 1 36 36 ASP N N 15 126.259 0.064 . 1 . . . . 36 ASP N . 25349 1 426 . 1 1 37 37 PRO HA H 1 4.029 0.01 . 1 . . . . 37 PRO HA . 25349 1 427 . 1 1 37 37 PRO HB2 H 1 1.116 0.021 . 2 . . . . 37 PRO HB2 . 25349 1 428 . 1 1 37 37 PRO HB3 H 1 1.108 0.029 . 2 . . . . 37 PRO HB3 . 25349 1 429 . 1 1 37 37 PRO HD2 H 1 2.84 0.013 . 2 . . . . 37 PRO HD2 . 25349 1 430 . 1 1 37 37 PRO HD3 H 1 2.84 0.017 . 2 . . . . 37 PRO HD3 . 25349 1 431 . 1 1 37 37 PRO HG2 H 1 0.741 0.021 . 2 . . . . 37 PRO HG2 . 25349 1 432 . 1 1 37 37 PRO HG3 H 1 0.424 0.028 . 2 . . . . 37 PRO HG3 . 25349 1 433 . 1 1 37 37 PRO C C 13 178.022 0.2 . 1 . . . . 37 PRO C . 25349 1 434 . 1 1 37 37 PRO CA C 13 63.465 0.043 . 1 . . . . 37 PRO CA . 25349 1 435 . 1 1 37 37 PRO CB C 13 31.334 0.047 . 1 . . . . 37 PRO CB . 25349 1 436 . 1 1 37 37 PRO CD C 13 50.098 0.04 . 1 . . . . 37 PRO CD . 25349 1 437 . 1 1 37 37 PRO CG C 13 26.071 0.023 . 1 . . . . 37 PRO CG . 25349 1 438 . 1 1 38 38 ARG H H 1 8.376 0.007 . 1 . . . . 38 ARG H . 25349 1 439 . 1 1 38 38 ARG HA H 1 3.889 0.006 . 1 . . . . 38 ARG HA . 25349 1 440 . 1 1 38 38 ARG HB2 H 1 1.821 0.015 . 2 . . . . 38 ARG HB2 . 25349 1 441 . 1 1 38 38 ARG HB3 H 1 1.623 0.013 . 2 . . . . 38 ARG HB3 . 25349 1 442 . 1 1 38 38 ARG HD2 H 1 2.99 0.015 . 2 . . . . 38 ARG HD2 . 25349 1 443 . 1 1 38 38 ARG HD3 H 1 2.99 0.015 . 2 . . . . 38 ARG HD3 . 25349 1 444 . 1 1 38 38 ARG HE H 1 8.677 0.028 . 1 . . . . 38 ARG HE . 25349 1 445 . 1 1 38 38 ARG HG2 H 1 1.254 0.02 . 2 . . . . 38 ARG HG2 . 25349 1 446 . 1 1 38 38 ARG HG3 H 1 1.253 0.02 . 2 . . . . 38 ARG HG3 . 25349 1 447 . 1 1 38 38 ARG C C 13 176.963 0.2 . 1 . . . . 38 ARG C . 25349 1 448 . 1 1 38 38 ARG CA C 13 57.102 0.116 . 1 . . . . 38 ARG CA . 25349 1 449 . 1 1 38 38 ARG CB C 13 29.945 0.025 . 1 . . . . 38 ARG CB . 25349 1 450 . 1 1 38 38 ARG CD C 13 43.351 0.092 . 1 . . . . 38 ARG CD . 25349 1 451 . 1 1 38 38 ARG CG C 13 26.85 0.033 . 1 . . . . 38 ARG CG . 25349 1 452 . 1 1 38 38 ARG N N 15 118.747 0.059 . 1 . . . . 38 ARG N . 25349 1 453 . 1 1 38 38 ARG NE N 15 116.026 0.2 . 1 . . . . 38 ARG NE . 25349 1 454 . 1 1 39 39 LEU H H 1 7.312 0.008 . 1 . . . . 39 LEU H . 25349 1 455 . 1 1 39 39 LEU HA H 1 4.237 0.005 . 1 . . . . 39 LEU HA . 25349 1 456 . 1 1 39 39 LEU HB2 H 1 1.572 0.007 . 2 . . . . 39 LEU HB2 . 25349 1 457 . 1 1 39 39 LEU HB3 H 1 1.644 0.004 . 2 . . . . 39 LEU HB3 . 25349 1 458 . 1 1 39 39 LEU HD11 H 1 0.937 0.004 . 2 . . . . 39 LEU HD11 . 25349 1 459 . 1 1 39 39 LEU HD12 H 1 0.937 0.004 . 2 . . . . 39 LEU HD12 . 25349 1 460 . 1 1 39 39 LEU HD13 H 1 0.937 0.004 . 2 . . . . 39 LEU HD13 . 25349 1 461 . 1 1 39 39 LEU HD21 H 1 0.785 0.005 . 2 . . . . 39 LEU HD21 . 25349 1 462 . 1 1 39 39 LEU HD22 H 1 0.785 0.005 . 2 . . . . 39 LEU HD22 . 25349 1 463 . 1 1 39 39 LEU HD23 H 1 0.785 0.005 . 2 . . . . 39 LEU HD23 . 25349 1 464 . 1 1 39 39 LEU HG H 1 1.433 0.015 . 1 . . . . 39 LEU HG . 25349 1 465 . 1 1 39 39 LEU C C 13 176.911 0.2 . 1 . . . . 39 LEU C . 25349 1 466 . 1 1 39 39 LEU CA C 13 54.773 0.059 . 1 . . . . 39 LEU CA . 25349 1 467 . 1 1 39 39 LEU CB C 13 42.129 0.057 . 1 . . . . 39 LEU CB . 25349 1 468 . 1 1 39 39 LEU CD1 C 13 25.163 0.031 . 2 . . . . 39 LEU CD1 . 25349 1 469 . 1 1 39 39 LEU CD2 C 13 22.678 0.025 . 2 . . . . 39 LEU CD2 . 25349 1 470 . 1 1 39 39 LEU CG C 13 27.135 0.016 . 1 . . . . 39 LEU CG . 25349 1 471 . 1 1 39 39 LEU N N 15 117.856 0.081 . 1 . . . . 39 LEU N . 25349 1 472 . 1 1 40 40 LYS H H 1 7.448 0.007 . 1 . . . . 40 LYS H . 25349 1 473 . 1 1 40 40 LYS HA H 1 4.257 0.007 . 1 . . . . 40 LYS HA . 25349 1 474 . 1 1 40 40 LYS HB2 H 1 1.628 0.01 . 2 . . . . 40 LYS HB2 . 25349 1 475 . 1 1 40 40 LYS HB3 H 1 1.752 0.007 . 2 . . . . 40 LYS HB3 . 25349 1 476 . 1 1 40 40 LYS HD2 H 1 1.754 0.012 . 2 . . . . 40 LYS HD2 . 25349 1 477 . 1 1 40 40 LYS HD3 H 1 1.615 0.009 . 2 . . . . 40 LYS HD3 . 25349 1 478 . 1 1 40 40 LYS HE2 H 1 2.943 0.008 . 2 . . . . 40 LYS HE2 . 25349 1 479 . 1 1 40 40 LYS HE3 H 1 2.944 0.012 . 2 . . . . 40 LYS HE3 . 25349 1 480 . 1 1 40 40 LYS HG2 H 1 1.297 0.016 . 2 . . . . 40 LYS HG2 . 25349 1 481 . 1 1 40 40 LYS HG3 H 1 1.315 0.027 . 2 . . . . 40 LYS HG3 . 25349 1 482 . 1 1 40 40 LYS C C 13 175.891 0.2 . 1 . . . . 40 LYS C . 25349 1 483 . 1 1 40 40 LYS CA C 13 55.716 0.131 . 1 . . . . 40 LYS CA . 25349 1 484 . 1 1 40 40 LYS CB C 13 33.027 0.054 . 1 . . . . 40 LYS CB . 25349 1 485 . 1 1 40 40 LYS CD C 13 29.04 0.047 . 1 . . . . 40 LYS CD . 25349 1 486 . 1 1 40 40 LYS CE C 13 42.269 0.079 . 1 . . . . 40 LYS CE . 25349 1 487 . 1 1 40 40 LYS CG C 13 24.644 0.029 . 1 . . . . 40 LYS CG . 25349 1 488 . 1 1 40 40 LYS N N 15 120.141 0.057 . 1 . . . . 40 LYS N . 25349 1 489 . 1 1 41 41 ILE H H 1 7.975 0.007 . 1 . . . . 41 ILE H . 25349 1 490 . 1 1 41 41 ILE HA H 1 4.35 0.007 . 1 . . . . 41 ILE HA . 25349 1 491 . 1 1 41 41 ILE HB H 1 1.806 0.006 . 1 . . . . 41 ILE HB . 25349 1 492 . 1 1 41 41 ILE HD11 H 1 0.825 0.007 . 1 . . . . 41 ILE HD11 . 25349 1 493 . 1 1 41 41 ILE HD12 H 1 0.825 0.007 . 1 . . . . 41 ILE HD12 . 25349 1 494 . 1 1 41 41 ILE HD13 H 1 0.825 0.007 . 1 . . . . 41 ILE HD13 . 25349 1 495 . 1 1 41 41 ILE HG12 H 1 1.468 0.005 . 2 . . . . 41 ILE HG12 . 25349 1 496 . 1 1 41 41 ILE HG13 H 1 1.122 0.006 . 2 . . . . 41 ILE HG13 . 25349 1 497 . 1 1 41 41 ILE HG21 H 1 0.923 0.006 . 1 . . . . 41 ILE HG21 . 25349 1 498 . 1 1 41 41 ILE HG22 H 1 0.923 0.006 . 1 . . . . 41 ILE HG22 . 25349 1 499 . 1 1 41 41 ILE HG23 H 1 0.923 0.006 . 1 . . . . 41 ILE HG23 . 25349 1 500 . 1 1 41 41 ILE CA C 13 58.57 0.077 . 1 . . . . 41 ILE CA . 25349 1 501 . 1 1 41 41 ILE CB C 13 38.754 0.039 . 1 . . . . 41 ILE CB . 25349 1 502 . 1 1 41 41 ILE CD1 C 13 12.654 0.072 . 1 . . . . 41 ILE CD1 . 25349 1 503 . 1 1 41 41 ILE CG1 C 13 27.043 0.028 . 1 . . . . 41 ILE CG1 . 25349 1 504 . 1 1 41 41 ILE CG2 C 13 16.96 0.029 . 1 . . . . 41 ILE CG2 . 25349 1 505 . 1 1 41 41 ILE N N 15 124.111 0.063 . 1 . . . . 41 ILE N . 25349 1 506 . 1 1 42 42 PRO HA H 1 4.347 0.003 . 1 . . . . 42 PRO HA . 25349 1 507 . 1 1 42 42 PRO HB2 H 1 2.248 0.006 . 2 . . . . 42 PRO HB2 . 25349 1 508 . 1 1 42 42 PRO HB3 H 1 2.248 0.006 . 2 . . . . 42 PRO HB3 . 25349 1 509 . 1 1 42 42 PRO HD2 H 1 3.83 0.01 . 2 . . . . 42 PRO HD2 . 25349 1 510 . 1 1 42 42 PRO HD3 H 1 3.588 0.006 . 2 . . . . 42 PRO HD3 . 25349 1 511 . 1 1 42 42 PRO HG2 H 1 1.994 0.004 . 2 . . . . 42 PRO HG2 . 25349 1 512 . 1 1 42 42 PRO HG3 H 1 1.916 0.005 . 2 . . . . 42 PRO HG3 . 25349 1 513 . 1 1 42 42 PRO C C 13 175.612 0.2 . 1 . . . . 42 PRO C . 25349 1 514 . 1 1 42 42 PRO CA C 13 63.445 0.059 . 1 . . . . 42 PRO CA . 25349 1 515 . 1 1 42 42 PRO CB C 13 32.009 0.029 . 1 . . . . 42 PRO CB . 25349 1 516 . 1 1 42 42 PRO CD C 13 50.75 0.287 . 1 . . . . 42 PRO CD . 25349 1 517 . 1 1 42 42 PRO CG C 13 27.372 0.018 . 1 . . . . 42 PRO CG . 25349 1 518 . 1 1 43 43 ALA H H 1 7.945 0.005 . 1 . . . . 43 ALA H . 25349 1 519 . 1 1 43 43 ALA HA H 1 4.117 0.01 . 1 . . . . 43 ALA HA . 25349 1 520 . 1 1 43 43 ALA HB1 H 1 1.334 0.005 . 1 . . . . 43 ALA HB1 . 25349 1 521 . 1 1 43 43 ALA HB2 H 1 1.334 0.005 . 1 . . . . 43 ALA HB2 . 25349 1 522 . 1 1 43 43 ALA HB3 H 1 1.334 0.005 . 1 . . . . 43 ALA HB3 . 25349 1 523 . 1 1 43 43 ALA CA C 13 53.715 0.054 . 1 . . . . 43 ALA CA . 25349 1 524 . 1 1 43 43 ALA CB C 13 20.224 0.065 . 1 . . . . 43 ALA CB . 25349 1 525 . 1 1 43 43 ALA N N 15 130.261 0.071 . 1 . . . . 43 ALA N . 25349 1 stop_ save_