data_53425 ####################### # Entry information # ####################### save_entry_information_1 _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information_1 _Entry.ID 53425 _Entry.Title ; mefp-12 -FP12 peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2025-11-15 _Entry.Accession_date 2025-11-15 _Entry.Last_release_date 2025-11-17 _Entry.Original_release_date 2025-11-17 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.14.0 _Entry.NMR_STAR_dict_location . _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details 'mefp-12 -FP12 peptide 30 AA peptide assigned using 800 MHz and cryoprobe' _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 Mathieu Rivard . D. . 0009-0004-5646-6368 53425 2 Alexandre Poulhazan . . . 0000-0001-5217-5070 53425 3 Max Renner-Rao . J. . . 53425 4 Emilie Duthoo . . . 0000-0003-1053-1617 53425 5 Franziska Jehle . . . 0000-0001-5960-0850 53425 6 Patrick Flammang . . . 0000-0001-9938-1154 53425 7 Daniel Jackson . J. . 0000-0001-9045-381X 53425 8 Matthew Harrington . J. . 0000-0003-1417-9251 53425 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'McGill University' . 53425 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 53425 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 119 53425 '15N chemical shifts' 30 53425 '1H chemical shifts' 254 53425 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2025-12-16 . original BMRB . 53425 stop_ save_ ############### # Citations # ############### save_citations_1 _Citation.Sf_category citations _Citation.Sf_framecode citations_1 _Citation.Entry_ID 53425 _Citation.ID 1 _Citation.Name . _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID . _Citation.DOI . _Citation.Full_citation . _Citation.Title ; Histidine-rich coiled-coils promote zinc-dependent self-assembly and curing of porous mussel glues ; _Citation.Status submitted _Citation.Type journal _Citation.Journal_abbrev 'Nat. Commun.' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _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 Mathieu Rivard . D. . . 53425 1 2 Alexandre Poulhazan . . . . 53425 1 3 Max Renner-Rao . J. . . 53425 1 4 Emilie Duthoo . . . . 53425 1 5 Franziska Jehle . . . . 53425 1 6 Patrick Flammang . . . . 53425 1 7 Daniel Jackson . J. . . 53425 1 8 Matthew Harrington . J. . . 53425 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly_1 _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly_1 _Assembly.Entry_ID 53425 _Assembly.ID 1 _Assembly.Name 'mefp-12 -FP12' _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 no _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange no _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 'mefp-12 -FP12' 1 $entity_1 . . yes native no no . . . 53425 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 53425 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity_1 _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 ; VDYHIKRLHKHTKYHLAAAE HQHKKHLNER ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq 1 _Entity.Polymer_author_seq_details 'acetylated sequence, synthesized using rink-amide resin' _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 30 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _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 . VAL . 53425 1 2 . ASP . 53425 1 3 . TYR . 53425 1 4 . HIS . 53425 1 5 . ILE . 53425 1 6 . LYS . 53425 1 7 . ARG . 53425 1 8 . LEU . 53425 1 9 . HIS . 53425 1 10 . LYS . 53425 1 11 . HIS . 53425 1 12 . THR . 53425 1 13 . LYS . 53425 1 14 . TYR . 53425 1 15 . HIS . 53425 1 16 . LEU . 53425 1 17 . ALA . 53425 1 18 . ALA . 53425 1 19 . ALA . 53425 1 20 . GLU . 53425 1 21 . HIS . 53425 1 22 . GLN . 53425 1 23 . HIS . 53425 1 24 . LYS . 53425 1 25 . LYS . 53425 1 26 . HIS . 53425 1 27 . LEU . 53425 1 28 . ASN . 53425 1 29 . GLU . 53425 1 30 . ARG . 53425 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 . VAL 1 1 53425 1 . ASP 2 2 53425 1 . TYR 3 3 53425 1 . HIS 4 4 53425 1 . ILE 5 5 53425 1 . LYS 6 6 53425 1 . ARG 7 7 53425 1 . LEU 8 8 53425 1 . HIS 9 9 53425 1 . LYS 10 10 53425 1 . HIS 11 11 53425 1 . THR 12 12 53425 1 . LYS 13 13 53425 1 . TYR 14 14 53425 1 . HIS 15 15 53425 1 . LEU 16 16 53425 1 . ALA 17 17 53425 1 . ALA 18 18 53425 1 . ALA 19 19 53425 1 . GLU 20 20 53425 1 . HIS 21 21 53425 1 . GLN 22 22 53425 1 . HIS 23 23 53425 1 . LYS 24 24 53425 1 . LYS 25 25 53425 1 . HIS 26 26 53425 1 . LEU 27 27 53425 1 . ASN 28 28 53425 1 . GLU 29 29 53425 1 . ARG 30 30 53425 1 stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source_1 _Entity_natural_src_list.Entry_ID 53425 _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 $entity_1 . 6550 organism . 'Mytilus edulis' 'blue mussel' . . Eukaryota Metazoa Mytilus edulis . . . . . . . . . . . . 'peptide designed from histidine-rich domain of the newly sequenced mefp-12 mussel foot protein found in native plaque' 53425 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source_1 _Entity_experimental_src_list.Entry_ID 53425 _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 $entity_1 . 'chemical synthesis' . . . . . . . . . . . . . . . . 53425 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 53425 _Sample.ID 1 _Sample.Name 'mefp-12 -FP12 pH 4.0 at 5mg/mL' _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number 1 _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 'mefp-12 -FP12' . . . 1 $entity_1 . . 5 . . mg/mL . . . . 53425 1 2 H2O 'natural abundance' . . . . . . 90 . . % . . . . 53425 1 3 D2O '[U-100% 2H]' . . . . . . 10 . . % . . . . 53425 1 4 DSS 'natural abundance' . . . . . . 5 . . uM . . . . 53425 1 5 'sodium chloride' 'natural abundance' . . . . . . 1 . . M . . . . 53425 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 53425 _Sample_condition_list.ID 1 _Sample_condition_list.Name 'native in solution 1M NaCl' _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' 1 . M 53425 1 pH 4.3 . pH 53425 1 pressure 1 . atm 53425 1 temperature 298 . K 53425 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 53425 _Software.ID 1 _Software.Type . _Software.Name TOPSPIN _Software.Version 4.0.9 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' . 53425 1 collection . 53425 1 'data analysis' . 53425 1 'peak picking' . 53425 1 processing . 53425 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 53425 _Software.ID 2 _Software.Type . _Software.Name MestReNova _Software.Version 16.0.0 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' . 53425 2 'data analysis' . 53425 2 'peak picking' . 53425 2 processing . 53425 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 53425 _NMR_spectrometer.ID 1 _NMR_spectrometer.Name '800 MHz QANUC McGill University (Montreal, Canada)' _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model 'AVANCE III' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_experiment_list_1 _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list_1 _Experiment_list.Entry_ID 53425 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NUS_flag _Experiment.Interleaved_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.Details _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-1H COSY' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 53425 1 2 '2D 1H-1H TOCSY' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 53425 1 3 '2D 1H-1H NOESY' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 53425 1 4 '2D 1H-13C HSQC' no no no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 53425 1 5 '2D 1H-15N HSQC' no yes no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 53425 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_1 _Chem_shift_reference.Entry_ID 53425 _Chem_shift_reference.ID 1 _Chem_shift_reference.Name DSS _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . 53425 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . 53425 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_chemical_shifts_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_1 _Assigned_chem_shift_list.Entry_ID 53425 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name 'mefp-12 -FP12 peptide pH4.3' _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 $chem_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.01 _Assigned_chem_shift_list.Chem_shift_13C_err 0.3 _Assigned_chem_shift_list.Chem_shift_15N_err 0.2 _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 COSY' . . . 53425 1 2 '2D 1H-1H TOCSY' . . . 53425 1 3 '2D 1H-1H NOESY' . . . 53425 1 4 '2D 1H-13C HSQC' . . . 53425 1 5 '2D 1H-15N HSQC' . . . 53425 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 $software_1 . . 53425 1 2 $software_2 . . 53425 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_assembly_asym_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.Ambiguity_set_ID _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 VAL H H 1 8.117 0.01 . 1 . . . . . 1 VAL H . 53425 1 2 . 1 . 1 1 1 VAL HA H 1 3.948 0.01 . 1 . . . . . 1 VAL HA . 53425 1 3 . 1 . 1 1 1 VAL HB H 1 1.924 0.01 . 1 . . . . . 1 VAL HB . 53425 1 4 . 1 . 1 1 1 VAL HG11 H 1 0.870 0.01 . . . . . . . 1 VAL HG1 . 53425 1 5 . 1 . 1 1 1 VAL HG12 H 1 0.870 0.01 . . . . . . . 1 VAL HG1 . 53425 1 6 . 1 . 1 1 1 VAL HG13 H 1 0.870 0.01 . . . . . . . 1 VAL HG1 . 53425 1 7 . 1 . 1 1 1 VAL HG21 H 1 0.750 0.01 . . . . . . . 1 VAL HG2 . 53425 1 8 . 1 . 1 1 1 VAL HG22 H 1 0.750 0.01 . . . . . . . 1 VAL HG2 . 53425 1 9 . 1 . 1 1 1 VAL HG23 H 1 0.750 0.01 . . . . . . . 1 VAL HG2 . 53425 1 10 . 1 . 1 1 1 VAL CA C 13 62.49 0.30 . 1 . . . . . 1 VAL CA . 53425 1 11 . 1 . 1 1 1 VAL CB C 13 29.89 0.30 . 1 . . . . . 1 VAL CB . 53425 1 12 . 1 . 1 1 1 VAL CG1 C 13 20.44 0.30 . . . . . . . 1 VAL CG1 . 53425 1 13 . 1 . 1 1 1 VAL CG2 C 13 20.90 0.30 . . . . . . . 1 VAL CG2 . 53425 1 14 . 1 . 1 1 1 VAL N N 15 125.28 0.20 . 1 . . . . . 1 VAL N . 53425 1 15 . 1 . 1 2 2 ASP H H 1 8.322 0.01 . 1 . . . . . 2 ASP H . 53425 1 16 . 1 . 1 2 2 ASP HA H 1 4.618 0.01 . 1 . . . . . 2 ASP HA . 53425 1 17 . 1 . 1 2 2 ASP HB2 H 1 2.597 0.01 . . . . . . . 2 ASP HB2 . 53425 1 18 . 1 . 1 2 2 ASP HB3 H 1 2.730 0.01 . . . . . . . 2 ASP HB3 . 53425 1 19 . 1 . 1 2 2 ASP CA C 13 53.45 0.30 . 1 . . . . . 2 ASP CA . 53425 1 20 . 1 . 1 2 2 ASP CB C 13 40.89 0.30 . 1 . . . . . 2 ASP CB . 53425 1 21 . 1 . 1 2 2 ASP N N 15 125.41 0.20 . 1 . . . . . 2 ASP N . 53425 1 22 . 1 . 1 3 3 TYR H H 1 8.176 0.01 . 1 . . . . . 3 TYR H . 53425 1 23 . 1 . 1 3 3 TYR HA H 1 4.438 0.01 . 1 . . . . . 3 TYR HA . 53425 1 24 . 1 . 1 3 3 TYR HB2 H 1 3.053 0.01 . . . . . . . 3 TYR HB2 . 53425 1 25 . 1 . 1 3 3 TYR HB3 H 1 2.884 0.01 . . . . . . . 3 TYR HB3 . 53425 1 26 . 1 . 1 3 3 TYR HD1 H 1 7.063 0.01 . . . . . . . 3 TYR HD1 . 53425 1 27 . 1 . 1 3 3 TYR HD2 H 1 7.063 0.01 . . . . . . . 3 TYR HD2 . 53425 1 28 . 1 . 1 3 3 TYR HE1 H 1 6.772 0.01 . . . . . . . 3 TYR HE1 . 53425 1 29 . 1 . 1 3 3 TYR HE2 H 1 6.772 0.01 . . . . . . . 3 TYR HE2 . 53425 1 30 . 1 . 1 3 3 TYR CA C 13 58.57 0.30 . 1 . . . . . 3 TYR CA . 53425 1 31 . 1 . 1 3 3 TYR CB C 13 38.23 0.30 . 1 . . . . . 3 TYR CB . 53425 1 32 . 1 . 1 3 3 TYR CD1 C 13 132.95 0.30 . . . . . . . 3 TYR CD1 . 53425 1 33 . 1 . 1 3 3 TYR CD2 C 13 132.95 0.30 . . . . . . . 3 TYR CD2 . 53425 1 34 . 1 . 1 3 3 TYR CE1 C 13 118.12 0.30 . . . . . . . 3 TYR CE1 . 53425 1 35 . 1 . 1 3 3 TYR CE2 C 13 118.12 0.30 . . . . . . . 3 TYR CE2 . 53425 1 36 . 1 . 1 3 3 TYR N N 15 121.69 0.20 . 1 . . . . . 3 TYR N . 53425 1 37 . 1 . 1 4 4 HIS H H 1 8.480 0.01 . 1 . . . . . 4 HIS H . 53425 1 38 . 1 . 1 4 4 HIS HA H 1 4.487 0.01 . 1 . . . . . 4 HIS HA . 53425 1 39 . 1 . 1 4 4 HIS HB2 H 1 3.263 0.01 . . . . . . . 4 HIS HB2 . 53425 1 40 . 1 . 1 4 4 HIS HB3 H 1 3.204 0.01 . . . . . . . 4 HIS HB3 . 53425 1 41 . 1 . 1 4 4 HIS HD1 H 1 7.238 0.01 . 1 . . . . . 4 HIS HD1 . 53425 1 42 . 1 . 1 4 4 HIS HD2 H 1 7.238 0.01 . 1 . . . . . 4 HIS HD2 . 53425 1 43 . 1 . 1 4 4 HIS HE1 H 1 8.568 0.01 . 1 . . . . . 4 HIS HE1 . 53425 1 44 . 1 . 1 4 4 HIS HE2 H 1 8.568 0.01 . 1 . . . . . 4 HIS HE2 . 53425 1 45 . 1 . 1 4 4 HIS CA C 13 56.37 0.30 . 1 . . . . . 4 HIS CA . 53425 1 46 . 1 . 1 4 4 HIS CB C 13 28.12 0.30 . 1 . . . . . 4 HIS CB . 53425 1 47 . 1 . 1 4 4 HIS CD2 C 13 119.81 0.30 . 1 . . . . . 4 HIS CD2 . 53425 1 48 . 1 . 1 4 4 HIS CE1 C 13 136.08 0.30 . 1 . . . . . 4 HIS CE1 . 53425 1 49 . 1 . 1 4 4 HIS N N 15 119.83 0.20 . 1 . . . . . 4 HIS N . 53425 1 50 . 1 . 1 5 5 ILE H H 1 7.879 0.01 . 1 . . . . . 5 ILE H . 53425 1 51 . 1 . 1 5 5 ILE HA H 1 4.055 0.01 . 1 . . . . . 5 ILE HA . 53425 1 52 . 1 . 1 5 5 ILE HB H 1 1.863 0.01 . 1 . . . . . 5 ILE HB . 53425 1 53 . 1 . 1 5 5 ILE HG12 H 1 1.446 0.01 . . . . . . . 5 ILE HG12 . 53425 1 54 . 1 . 1 5 5 ILE HG13 H 1 1.180 0.01 . . . . . . . 5 ILE HG13 . 53425 1 55 . 1 . 1 5 5 ILE HG21 H 1 0.890 0.01 . 1 . . . . . 5 ILE HG2 . 53425 1 56 . 1 . 1 5 5 ILE HG22 H 1 0.890 0.01 . 1 . . . . . 5 ILE HG2 . 53425 1 57 . 1 . 1 5 5 ILE HG23 H 1 0.890 0.01 . 1 . . . . . 5 ILE HG2 . 53425 1 58 . 1 . 1 5 5 ILE CA C 13 61.45 0.30 . 1 . . . . . 5 ILE CA . 53425 1 59 . 1 . 1 5 5 ILE CB C 13 38.51 0.30 . 1 . . . . . 5 ILE CB . 53425 1 60 . 1 . 1 5 5 ILE CG1 C 13 27.55 0.30 . 1 . . . . . 5 ILE CG1 . 53425 1 61 . 1 . 1 5 5 ILE CG2 C 13 27.55 0.30 . 1 . . . . . 5 ILE CG2 . 53425 1 62 . 1 . 1 5 5 ILE CD1 C 13 12.77 0.30 . 1 . . . . . 5 ILE CD1 . 53425 1 63 . 1 . 1 5 5 ILE N N 15 121.26 0.20 . 1 . . . . . 5 ILE N . 53425 1 64 . 1 . 1 6 6 LYS H H 1 8.318 0.01 . 1 . . . . . 6 LYS H . 53425 1 65 . 1 . 1 6 6 LYS HA H 1 4.272 0.01 . 1 . . . . . 6 LYS HA . 53425 1 66 . 1 . 1 6 6 LYS HB2 H 1 1.804 0.01 . . . . . . . 6 LYS HB2 . 53425 1 67 . 1 . 1 6 6 LYS HB3 H 1 1.766 0.01 . . . . . . . 6 LYS HB3 . 53425 1 68 . 1 . 1 6 6 LYS HG2 H 1 1.480 0.01 . . . . . . . 6 LYS HG2 . 53425 1 69 . 1 . 1 6 6 LYS HG3 H 1 1.393 0.01 . . . . . . . 6 LYS HG3 . 53425 1 70 . 1 . 1 6 6 LYS HD2 H 1 1.687 0.01 . . . . . . . 6 LYS HD2 . 53425 1 71 . 1 . 1 6 6 LYS HD3 H 1 1.687 0.01 . . . . . . . 6 LYS HD3 . 53425 1 72 . 1 . 1 6 6 LYS HE2 H 1 2.997 0.01 . . . . . . . 6 LYS HE2 . 53425 1 73 . 1 . 1 6 6 LYS HE3 H 1 2.997 0.01 . . . . . . . 6 LYS HE3 . 53425 1 74 . 1 . 1 6 6 LYS HZ1 H 1 7.874 0.01 . 1 . . . . . 6 LYS QZ . 53425 1 75 . 1 . 1 6 6 LYS HZ2 H 1 7.874 0.01 . 1 . . . . . 6 LYS QZ . 53425 1 76 . 1 . 1 6 6 LYS HZ3 H 1 7.874 0.01 . 1 . . . . . 6 LYS QZ . 53425 1 77 . 1 . 1 6 6 LYS CA C 13 55.10 0.30 . 1 . . . . . 6 LYS CA . 53425 1 78 . 1 . 1 6 6 LYS CB C 13 32.94 0.30 . 1 . . . . . 6 LYS CB . 53425 1 79 . 1 . 1 6 6 LYS CG C 13 24.98 0.30 . 1 . . . . . 6 LYS CG . 53425 1 80 . 1 . 1 6 6 LYS CD C 13 29.01 0.30 . 1 . . . . . 6 LYS CD . 53425 1 81 . 1 . 1 6 6 LYS CE C 13 41.87 0.30 . 1 . . . . . 6 LYS CE . 53425 1 82 . 1 . 1 6 6 LYS N N 15 121.06 0.20 . 1 . . . . . 6 LYS N . 53425 1 83 . 1 . 1 7 7 ARG H H 1 8.221 0.01 . 1 . . . . . 7 ARG H . 53425 1 84 . 1 . 1 7 7 ARG HA H 1 4.309 0.01 . 1 . . . . . 7 ARG HA . 53425 1 85 . 1 . 1 7 7 ARG HB2 H 1 1.784 0.01 . . . . . . . 7 ARG HB2 . 53425 1 86 . 1 . 1 7 7 ARG HB3 H 1 1.724 0.01 . . . . . . . 7 ARG HB3 . 53425 1 87 . 1 . 1 7 7 ARG HG2 H 1 1.596 0.01 . . . . . . . 7 ARG HG2 . 53425 1 88 . 1 . 1 7 7 ARG HG3 H 1 1.596 0.01 . . . . . . . 7 ARG HG3 . 53425 1 89 . 1 . 1 7 7 ARG HD2 H 1 3.177 0.01 . . . . . . . 7 ARG HD2 . 53425 1 90 . 1 . 1 7 7 ARG HD3 H 1 3.177 0.01 . . . . . . . 7 ARG HD3 . 53425 1 91 . 1 . 1 7 7 ARG HE H 1 7.874 0.01 . 1 . . . . . 7 ARG HE . 53425 1 92 . 1 . 1 7 7 ARG CA C 13 56.19 0.30 . 1 . . . . . 7 ARG CA . 53425 1 93 . 1 . 1 7 7 ARG CB C 13 30.29 0.30 . 1 . . . . . 7 ARG CB . 53425 1 94 . 1 . 1 7 7 ARG CG C 13 27.33 0.30 . 1 . . . . . 7 ARG CG . 53425 1 95 . 1 . 1 7 7 ARG CD C 13 43.26 0.30 . 1 . . . . . 7 ARG CD . 53425 1 96 . 1 . 1 7 7 ARG N N 15 121.36 0.20 . 1 . . . . . 7 ARG N . 53425 1 97 . 1 . 1 8 8 LEU H H 1 8.421 0.01 . 1 . . . . . 8 LEU H . 53425 1 98 . 1 . 1 8 8 LEU HA H 1 4.307 0.01 . 1 . . . . . 8 LEU HA . 53425 1 99 . 1 . 1 8 8 LEU HB2 H 1 1.631 0.01 . . . . . . . 8 LEU HB2 . 53425 1 100 . 1 . 1 8 8 LEU HB3 H 1 1.631 0.01 . . . . . . . 8 LEU HB3 . 53425 1 101 . 1 . 1 8 8 LEU HG H 1 1.565 0.01 . 1 . . . . . 8 LEU HG . 53425 1 102 . 1 . 1 8 8 LEU HD11 H 1 0.878 0.01 . . . . . . . 8 LEU HD1 . 53425 1 103 . 1 . 1 8 8 LEU HD12 H 1 0.878 0.01 . . . . . . . 8 LEU HD1 . 53425 1 104 . 1 . 1 8 8 LEU HD13 H 1 0.878 0.01 . . . . . . . 8 LEU HD1 . 53425 1 105 . 1 . 1 8 8 LEU HD21 H 1 0.923 0.01 . . . . . . . 8 LEU HD2 . 53425 1 106 . 1 . 1 8 8 LEU HD22 H 1 0.923 0.01 . . . . . . . 8 LEU HD2 . 53425 1 107 . 1 . 1 8 8 LEU HD23 H 1 0.923 0.01 . . . . . . . 8 LEU HD2 . 53425 1 108 . 1 . 1 8 8 LEU CA C 13 56.11 0.30 . 1 . . . . . 8 LEU CA . 53425 1 109 . 1 . 1 8 8 LEU CB C 13 42.44 0.30 . 1 . . . . . 8 LEU CB . 53425 1 110 . 1 . 1 8 8 LEU CG C 13 26.96 0.30 . 1 . . . . . 8 LEU CG . 53425 1 111 . 1 . 1 8 8 LEU CD1 C 13 23.52 0.30 . . . . . . . 8 LEU CD1 . 53425 1 112 . 1 . 1 8 8 LEU CD2 C 13 24.75 0.30 . . . . . . . 8 LEU CD2 . 53425 1 113 . 1 . 1 8 8 LEU N N 15 123.89 0.20 . 1 . . . . . 8 LEU N . 53425 1 114 . 1 . 1 9 9 HIS H H 1 8.672 0.01 . 1 . . . . . 9 HIS H . 53425 1 115 . 1 . 1 9 9 HIS HA H 1 4.694 0.01 . 1 . . . . . 9 HIS HA . 53425 1 116 . 1 . 1 9 9 HIS HB2 H 1 3.268 0.01 . . . . . . . 9 HIS HB2 . 53425 1 117 . 1 . 1 9 9 HIS HB3 H 1 3.171 0.01 . . . . . . . 9 HIS HB3 . 53425 1 118 . 1 . 1 9 9 HIS HD1 H 1 7.306 0.01 . 1 . . . . . 9 HIS HD1 . 53425 1 119 . 1 . 1 9 9 HIS HD2 H 1 7.306 0.01 . 1 . . . . . 9 HIS HD2 . 53425 1 120 . 1 . 1 9 9 HIS HE1 H 1 8.612 0.01 . 1 . . . . . 9 HIS HE1 . 53425 1 121 . 1 . 1 9 9 HIS HE2 H 1 8.612 0.01 . 1 . . . . . 9 HIS HE2 . 53425 1 122 . 1 . 1 9 9 HIS CA C 13 55.05 0.30 . 1 . . . . . 9 HIS CA . 53425 1 123 . 1 . 1 9 9 HIS CB C 13 28.97 0.30 . 1 . . . . . 9 HIS CB . 53425 1 124 . 1 . 1 9 9 HIS CD2 C 13 119.97 0.30 . 1 . . . . . 9 HIS CD2 . 53425 1 125 . 1 . 1 9 9 HIS CE1 C 13 136.16 0.30 . 1 . . . . . 9 HIS CE1 . 53425 1 126 . 1 . 1 9 9 HIS N N 15 119.83 0.20 . 1 . . . . . 9 HIS N . 53425 1 127 . 1 . 1 10 10 LYS H H 1 8.233 0.01 . 1 . . . . . 10 LYS H . 53425 1 128 . 1 . 1 10 10 LYS HA H 1 4.309 0.01 . 1 . . . . . 10 LYS HA . 53425 1 129 . 1 . 1 10 10 LYS HB2 H 1 1.799 0.01 . . . . . . . 10 LYS HB2 . 53425 1 130 . 1 . 1 10 10 LYS HB3 H 1 1.731 0.01 . . . . . . . 10 LYS HB3 . 53425 1 131 . 1 . 1 10 10 LYS HG2 H 1 1.369 0.01 . . . . . . . 10 LYS HG2 . 53425 1 132 . 1 . 1 10 10 LYS HG3 H 1 1.369 0.01 . . . . . . . 10 LYS HG3 . 53425 1 133 . 1 . 1 10 10 LYS HD2 H 1 1.596 0.01 . . . . . . . 10 LYS HD2 . 53425 1 134 . 1 . 1 10 10 LYS HD3 H 1 1.596 0.01 . . . . . . . 10 LYS HD3 . 53425 1 135 . 1 . 1 10 10 LYS HE2 H 1 2.926 0.01 . . . . . . . 10 LYS HE2 . 53425 1 136 . 1 . 1 10 10 LYS HE3 H 1 2.926 0.01 . . . . . . . 10 LYS HE3 . 53425 1 137 . 1 . 1 10 10 LYS HZ1 H 1 7.887 0.01 . 1 . . . . . 10 LYS QZ . 53425 1 138 . 1 . 1 10 10 LYS HZ2 H 1 7.887 0.01 . 1 . . . . . 10 LYS QZ . 53425 1 139 . 1 . 1 10 10 LYS HZ3 H 1 7.887 0.01 . 1 . . . . . 10 LYS QZ . 53425 1 140 . 1 . 1 10 10 LYS CA C 13 56.22 0.30 . 1 . . . . . 10 LYS CA . 53425 1 141 . 1 . 1 10 10 LYS CB C 13 30.23 0.30 . 1 . . . . . 10 LYS CB . 53425 1 142 . 1 . 1 10 10 LYS CG C 13 24.81 0.30 . 1 . . . . . 10 LYS CG . 53425 1 143 . 1 . 1 10 10 LYS CD C 13 27.33 0.30 . 1 . . . . . 10 LYS CD . 53425 1 144 . 1 . 1 10 10 LYS CE C 13 41.82 0.30 . 1 . . . . . 10 LYS CE . 53425 1 145 . 1 . 1 10 10 LYS N N 15 121.36 0.20 . 1 . . . . . 10 LYS N . 53425 1 146 . 1 . 1 11 11 HIS H H 1 8.721 0.01 . 1 . . . . . 11 HIS H . 53425 1 147 . 1 . 1 11 11 HIS HA H 1 4.799 0.01 . 1 . . . . . 11 HIS HA . 53425 1 148 . 1 . 1 11 11 HIS HB2 H 1 3.266 0.01 . . . . . . . 11 HIS HB2 . 53425 1 149 . 1 . 1 11 11 HIS HB3 H 1 3.187 0.01 . . . . . . . 11 HIS HB3 . 53425 1 150 . 1 . 1 11 11 HIS HD1 H 1 7.292 0.01 . 1 . . . . . 11 HIS HD1 . 53425 1 151 . 1 . 1 11 11 HIS HD2 H 1 7.292 0.01 . 1 . . . . . 11 HIS HD2 . 53425 1 152 . 1 . 1 11 11 HIS HE1 H 1 8.590 0.01 . 1 . . . . . 11 HIS HE1 . 53425 1 153 . 1 . 1 11 11 HIS HE2 H 1 8.590 0.01 . 1 . . . . . 11 HIS HE2 . 53425 1 154 . 1 . 1 11 11 HIS CA C 13 55.05 0.30 . 1 . . . . . 11 HIS CA . 53425 1 155 . 1 . 1 11 11 HIS CB C 13 29.04 0.30 . 1 . . . . . 11 HIS CB . 53425 1 156 . 1 . 1 11 11 HIS CD2 C 13 119.83 0.30 . 1 . . . . . 11 HIS CD2 . 53425 1 157 . 1 . 1 11 11 HIS CE1 C 13 136.08 0.30 . 1 . . . . . 11 HIS CE1 . 53425 1 158 . 1 . 1 11 11 HIS N N 15 119.94 0.20 . 1 . . . . . 11 HIS N . 53425 1 159 . 1 . 1 12 12 THR H H 1 8.269 0.01 . 1 . . . . . 12 THR H . 53425 1 160 . 1 . 1 12 12 THR HA H 1 4.306 0.01 . 1 . . . . . 12 THR HA . 53425 1 161 . 1 . 1 12 12 THR HB H 1 4.102 0.01 . 1 . . . . . 12 THR HB . 53425 1 162 . 1 . 1 12 12 THR HG1 H 1 1.129 0.01 . 1 . . . . . 12 THR HG1 . 53425 1 163 . 1 . 1 12 12 THR CA C 13 62.00 0.30 . 1 . . . . . 12 THR CA . 53425 1 164 . 1 . 1 12 12 THR CB C 13 69.89 0.30 . 1 . . . . . 12 THR CB . 53425 1 165 . 1 . 1 12 12 THR CG2 C 13 21.59 0.30 . 1 . . . . . 12 THR CG2 . 53425 1 166 . 1 . 1 12 12 THR N N 15 119.01 0.20 . 1 . . . . . 12 THR N . 53425 1 167 . 1 . 1 13 13 LYS H H 1 8.440 0.01 . 1 . . . . . 13 LYS H . 53425 1 168 . 1 . 1 13 13 LYS HA H 1 4.269 0.01 . 1 . . . . . 13 LYS HA . 53425 1 169 . 1 . 1 13 13 LYS HB2 H 1 1.799 0.01 . . . . . . . 13 LYS HB2 . 53425 1 170 . 1 . 1 13 13 LYS HB3 H 1 1.731 0.01 . . . . . . . 13 LYS HB3 . 53425 1 171 . 1 . 1 13 13 LYS HG2 H 1 1.378 0.01 . . . . . . . 13 LYS HG2 . 53425 1 172 . 1 . 1 13 13 LYS HG3 H 1 1.431 0.01 . . . . . . . 13 LYS HG3 . 53425 1 173 . 1 . 1 13 13 LYS HD2 H 1 1.691 0.01 . . . . . . . 13 LYS HD2 . 53425 1 174 . 1 . 1 13 13 LYS HD3 H 1 1.691 0.01 . . . . . . . 13 LYS HD3 . 53425 1 175 . 1 . 1 13 13 LYS HE2 H 1 2.990 0.01 . . . . . . . 13 LYS HE2 . 53425 1 176 . 1 . 1 13 13 LYS HE3 H 1 2.990 0.01 . . . . . . . 13 LYS HE3 . 53425 1 177 . 1 . 1 13 13 LYS HZ1 H 1 7.249 0.01 . 1 . . . . . 13 LYS QZ . 53425 1 178 . 1 . 1 13 13 LYS HZ2 H 1 7.249 0.01 . 1 . . . . . 13 LYS QZ . 53425 1 179 . 1 . 1 13 13 LYS HZ3 H 1 7.249 0.01 . 1 . . . . . 13 LYS QZ . 53425 1 180 . 1 . 1 13 13 LYS CA C 13 56.29 0.30 . 1 . . . . . 13 LYS CA . 53425 1 181 . 1 . 1 13 13 LYS CB C 13 33.12 0.30 . 1 . . . . . 13 LYS CB . 53425 1 182 . 1 . 1 13 13 LYS CG C 13 24.88 0.30 . 1 . . . . . 13 LYS CG . 53425 1 183 . 1 . 1 13 13 LYS CD C 13 28.94 0.30 . 1 . . . . . 13 LYS CD . 53425 1 184 . 1 . 1 13 13 LYS CE C 13 41.85 0.30 . 1 . . . . . 13 LYS CE . 53425 1 185 . 1 . 1 13 13 LYS N N 15 123.02 0.20 . 1 . . . . . 13 LYS N . 53425 1 186 . 1 . 1 14 14 TYR H H 1 8.225 0.01 . 1 . . . . . 14 TYR H . 53425 1 187 . 1 . 1 14 14 TYR HA H 1 4.532 0.01 . 1 . . . . . 14 TYR HA . 53425 1 188 . 1 . 1 14 14 TYR HB2 H 1 2.935 0.01 . . . . . . . 14 TYR HB2 . 53425 1 189 . 1 . 1 14 14 TYR HB3 H 1 3.058 0.01 . . . . . . . 14 TYR HB3 . 53425 1 190 . 1 . 1 14 14 TYR HD1 H 1 7.086 0.01 . . . . . . . 14 TYR HD1 . 53425 1 191 . 1 . 1 14 14 TYR HD2 H 1 7.086 0.01 . . . . . . . 14 TYR HD2 . 53425 1 192 . 1 . 1 14 14 TYR HE1 H 1 6.796 0.01 . . . . . . . 14 TYR HE1 . 53425 1 193 . 1 . 1 14 14 TYR HE2 H 1 6.796 0.01 . . . . . . . 14 TYR HE2 . 53425 1 194 . 1 . 1 14 14 TYR CA C 13 57.73 0.30 . 1 . . . . . 14 TYR CA . 53425 1 195 . 1 . 1 14 14 TYR CB C 13 39.13 0.30 . 1 . . . . . 14 TYR CB . 53425 1 196 . 1 . 1 14 14 TYR CD1 C 13 133.07 0.30 . . . . . . . 14 TYR CD1 . 53425 1 197 . 1 . 1 14 14 TYR CD2 C 13 133.07 0.30 . . . . . . . 14 TYR CD2 . 53425 1 198 . 1 . 1 14 14 TYR CE1 C 13 118.12 0.30 . . . . . . . 14 TYR CE1 . 53425 1 199 . 1 . 1 14 14 TYR CE2 C 13 118.12 0.30 . . . . . . . 14 TYR CE2 . 53425 1 200 . 1 . 1 14 14 TYR N N 15 121.36 0.20 . 1 . . . . . 14 TYR N . 53425 1 201 . 1 . 1 15 15 HIS H H 1 8.403 0.01 . 1 . . . . . 15 HIS H . 53425 1 202 . 1 . 1 15 15 HIS HA H 1 4.611 0.01 . 1 . . . . . 15 HIS HA . 53425 1 203 . 1 . 1 15 15 HIS HB2 H 1 3.177 0.01 . . . . . . . 15 HIS HB2 . 53425 1 204 . 1 . 1 15 15 HIS HB3 H 1 3.102 0.01 . . . . . . . 15 HIS HB3 . 53425 1 205 . 1 . 1 15 15 HIS HD1 H 1 7.227 0.01 . 1 . . . . . 15 HIS HD1 . 53425 1 206 . 1 . 1 15 15 HIS HD2 H 1 7.227 0.01 . 1 . . . . . 15 HIS HD2 . 53425 1 207 . 1 . 1 15 15 HIS HE1 H 1 8.566 0.01 . 1 . . . . . 15 HIS HE1 . 53425 1 208 . 1 . 1 15 15 HIS HE2 H 1 8.566 0.01 . 1 . . . . . 15 HIS HE2 . 53425 1 209 . 1 . 1 15 15 HIS CA C 13 54.87 0.30 . 1 . . . . . 15 HIS CA . 53425 1 210 . 1 . 1 15 15 HIS CB C 13 29.28 0.30 . 1 . . . . . 15 HIS CB . 53425 1 211 . 1 . 1 15 15 HIS CD2 C 13 119.81 0.30 . 1 . . . . . 15 HIS CD2 . 53425 1 212 . 1 . 1 15 15 HIS CE1 C 13 136.08 0.30 . 1 . . . . . 15 HIS CE1 . 53425 1 213 . 1 . 1 15 15 HIS N N 15 120.76 0.20 . 1 . . . . . 15 HIS N . 53425 1 214 . 1 . 1 16 16 LEU H H 1 8.254 0.01 . 1 . . . . . 16 LEU H . 53425 1 215 . 1 . 1 16 16 LEU HA H 1 4.284 0.01 . 1 . . . . . 16 LEU HA . 53425 1 216 . 1 . 1 16 16 LEU HB2 H 1 1.574 0.01 . . . . . . . 16 LEU HB2 . 53425 1 217 . 1 . 1 16 16 LEU HB3 H 1 1.574 0.01 . . . . . . . 16 LEU HB3 . 53425 1 218 . 1 . 1 16 16 LEU HG H 1 1.563 0.01 . 1 . . . . . 16 LEU HG . 53425 1 219 . 1 . 1 16 16 LEU HD11 H 1 0.890 0.01 . . . . . . . 16 LEU HD1 . 53425 1 220 . 1 . 1 16 16 LEU HD12 H 1 0.890 0.01 . . . . . . . 16 LEU HD1 . 53425 1 221 . 1 . 1 16 16 LEU HD13 H 1 0.890 0.01 . . . . . . . 16 LEU HD1 . 53425 1 222 . 1 . 1 16 16 LEU HD21 H 1 0.945 0.01 . . . . . . . 16 LEU HD2 . 53425 1 223 . 1 . 1 16 16 LEU HD22 H 1 0.945 0.01 . . . . . . . 16 LEU HD2 . 53425 1 224 . 1 . 1 16 16 LEU HD23 H 1 0.945 0.01 . . . . . . . 16 LEU HD2 . 53425 1 225 . 1 . 1 16 16 LEU CA C 13 55.13 0.30 . 1 . . . . . 16 LEU CA . 53425 1 226 . 1 . 1 16 16 LEU CB C 13 42.39 0.30 . 1 . . . . . 16 LEU CB . 53425 1 227 . 1 . 1 16 16 LEU CG C 13 27.03 0.30 . 1 . . . . . 16 LEU CG . 53425 1 228 . 1 . 1 16 16 LEU CD1 C 13 23.69 0.30 . . . . . . . 16 LEU CD1 . 53425 1 229 . 1 . 1 16 16 LEU CD2 C 13 24.76 0.30 . . . . . . . 16 LEU CD2 . 53425 1 230 . 1 . 1 16 16 LEU N N 15 122.91 0.20 . 1 . . . . . 16 LEU N . 53425 1 231 . 1 . 1 17 17 ALA H H 1 8.264 0.01 . 1 . . . . . 17 ALA H . 53425 1 232 . 1 . 1 17 17 ALA HA H 1 4.298 0.01 . 1 . . . . . 17 ALA HA . 53425 1 233 . 1 . 1 17 17 ALA HB1 H 1 1.359 0.01 . 1 . . . . . 17 ALA HB . 53425 1 234 . 1 . 1 17 17 ALA HB2 H 1 1.359 0.01 . 1 . . . . . 17 ALA HB . 53425 1 235 . 1 . 1 17 17 ALA HB3 H 1 1.359 0.01 . 1 . . . . . 17 ALA HB . 53425 1 236 . 1 . 1 17 17 ALA CA C 13 52.33 0.30 . 1 . . . . . 17 ALA CA . 53425 1 237 . 1 . 1 17 17 ALA CB C 13 19.16 0.30 . 1 . . . . . 17 ALA CB . 53425 1 238 . 1 . 1 17 17 ALA N N 15 125.59 0.20 . 1 . . . . . 17 ALA N . 53425 1 239 . 1 . 1 18 18 ALA H H 1 8.285 0.01 . 1 . . . . . 18 ALA H . 53425 1 240 . 1 . 1 18 18 ALA HA H 1 4.247 0.01 . 1 . . . . . 18 ALA HA . 53425 1 241 . 1 . 1 18 18 ALA HB1 H 1 1.377 0.01 . 1 . . . . . 18 ALA HB . 53425 1 242 . 1 . 1 18 18 ALA HB2 H 1 1.377 0.01 . 1 . . . . . 18 ALA HB . 53425 1 243 . 1 . 1 18 18 ALA HB3 H 1 1.377 0.01 . 1 . . . . . 18 ALA HB . 53425 1 244 . 1 . 1 18 18 ALA CA C 13 52.35 0.30 . 1 . . . . . 18 ALA CA . 53425 1 245 . 1 . 1 18 18 ALA CB C 13 19.15 0.30 . 1 . . . . . 18 ALA CB . 53425 1 246 . 1 . 1 18 18 ALA N N 15 123.30 0.20 . 1 . . . . . 18 ALA N . 53425 1 247 . 1 . 1 19 19 ALA H H 1 8.402 0.01 . 1 . . . . . 19 ALA H . 53425 1 248 . 1 . 1 19 19 ALA HA H 1 4.295 0.01 . 1 . . . . . 19 ALA HA . 53425 1 249 . 1 . 1 19 19 ALA HB1 H 1 1.383 0.01 . 1 . . . . . 19 ALA HB . 53425 1 250 . 1 . 1 19 19 ALA HB2 H 1 1.383 0.01 . 1 . . . . . 19 ALA HB . 53425 1 251 . 1 . 1 19 19 ALA HB3 H 1 1.383 0.01 . 1 . . . . . 19 ALA HB . 53425 1 252 . 1 . 1 19 19 ALA CA C 13 52.26 0.30 . 1 . . . . . 19 ALA CA . 53425 1 253 . 1 . 1 19 19 ALA CB C 13 19.13 0.30 . 1 . . . . . 19 ALA CB . 53425 1 254 . 1 . 1 19 19 ALA N N 15 122.94 0.20 . 1 . . . . . 19 ALA N . 53425 1 255 . 1 . 1 20 20 GLU H H 1 8.423 0.01 . 1 . . . . . 20 GLU H . 53425 1 256 . 1 . 1 20 20 GLU HA H 1 4.304 0.01 . 1 . . . . . 20 GLU HA . 53425 1 257 . 1 . 1 20 20 GLU HB2 H 1 2.035 0.01 . . . . . . . 20 GLU HB2 . 53425 1 258 . 1 . 1 20 20 GLU HB3 H 1 1.940 0.01 . . . . . . . 20 GLU HB3 . 53425 1 259 . 1 . 1 20 20 GLU HG2 H 1 2.359 0.01 . . . . . . . 20 GLU HG2 . 53425 1 260 . 1 . 1 20 20 GLU HG3 H 1 2.297 0.01 . . . . . . . 20 GLU HG3 . 53425 1 261 . 1 . 1 20 20 GLU CA C 13 56.30 0.30 . 1 . . . . . 20 GLU CA . 53425 1 262 . 1 . 1 20 20 GLU CB C 13 29.38 0.30 . 1 . . . . . 20 GLU CB . 53425 1 263 . 1 . 1 20 20 GLU CG C 13 35.45 0.30 . 1 . . . . . 20 GLU CG . 53425 1 264 . 1 . 1 20 20 GLU N N 15 123.84 0.20 . 1 . . . . . 20 GLU N . 53425 1 265 . 1 . 1 21 21 HIS H H 1 8.556 0.01 . 1 . . . . . 21 HIS H . 53425 1 266 . 1 . 1 21 21 HIS HA H 1 4.694 0.01 . 1 . . . . . 21 HIS HA . 53425 1 267 . 1 . 1 21 21 HIS HB2 H 1 3.268 0.01 . . . . . . . 21 HIS HB2 . 53425 1 268 . 1 . 1 21 21 HIS HB3 H 1 3.159 0.01 . . . . . . . 21 HIS HB3 . 53425 1 269 . 1 . 1 21 21 HIS HD1 H 1 7.259 0.01 . 1 . . . . . 21 HIS HD1 . 53425 1 270 . 1 . 1 21 21 HIS HD2 H 1 7.259 0.01 . 1 . . . . . 21 HIS HD2 . 53425 1 271 . 1 . 1 21 21 HIS HE1 H 1 8.573 0.01 . 1 . . . . . 21 HIS HE1 . 53425 1 272 . 1 . 1 21 21 HIS HE2 H 1 8.573 0.01 . 1 . . . . . 21 HIS HE2 . 53425 1 273 . 1 . 1 21 21 HIS CA C 13 55.04 0.30 . 1 . . . . . 21 HIS CA . 53425 1 274 . 1 . 1 21 21 HIS CB C 13 28.89 0.30 . 1 . . . . . 21 HIS CB . 53425 1 275 . 1 . 1 21 21 HIS CD2 C 13 119.77 0.30 . 1 . . . . . 21 HIS CD2 . 53425 1 276 . 1 . 1 21 21 HIS CE1 C 13 136.08 0.30 . 1 . . . . . 21 HIS CE1 . 53425 1 277 . 1 . 1 21 21 HIS N N 15 118.99 0.20 . 1 . . . . . 21 HIS N . 53425 1 278 . 1 . 1 22 22 GLN H H 1 8.346 0.01 . 1 . . . . . 22 GLN H . 53425 1 279 . 1 . 1 22 22 GLN HA H 1 4.330 0.01 . 1 . . . . . 22 GLN HA . 53425 1 280 . 1 . 1 22 22 GLN HB2 H 1 2.104 0.01 . . . . . . . 22 GLN HB2 . 53425 1 281 . 1 . 1 22 22 GLN HB3 H 1 1.970 0.01 . . . . . . . 22 GLN HB3 . 53425 1 282 . 1 . 1 22 22 GLN HG2 H 1 2.310 0.01 . . . . . . . 22 GLN HG2 . 53425 1 283 . 1 . 1 22 22 GLN HG3 H 1 2.349 0.01 . . . . . . . 22 GLN HG3 . 53425 1 284 . 1 . 1 22 22 GLN HE21 H 1 6.900 0.01 . . . . . . . 22 GLN HE21 . 53425 1 285 . 1 . 1 22 22 GLN HE22 H 1 7.538 0.01 . . . . . . . 22 GLN HE22 . 53425 1 286 . 1 . 1 22 22 GLN CA C 13 56.23 0.30 . 1 . . . . . 22 GLN CA . 53425 1 287 . 1 . 1 22 22 GLN CB C 13 30.16 0.30 . 1 . . . . . 22 GLN CB . 53425 1 288 . 1 . 1 22 22 GLN CG C 13 33.66 0.30 . 1 . . . . . 22 GLN CG . 53425 1 289 . 1 . 1 22 22 GLN N N 15 122.42 0.20 . 1 . . . . . 22 GLN N . 53425 1 290 . 1 . 1 23 23 HIS H H 1 8.686 0.01 . 1 . . . . . 23 HIS H . 53425 1 291 . 1 . 1 23 23 HIS HA H 1 4.723 0.01 . 1 . . . . . 23 HIS HA . 53425 1 292 . 1 . 1 23 23 HIS HB2 H 1 3.272 0.01 . . . . . . . 23 HIS HB2 . 53425 1 293 . 1 . 1 23 23 HIS HB3 H 1 3.181 0.01 . . . . . . . 23 HIS HB3 . 53425 1 294 . 1 . 1 23 23 HIS HD1 H 1 7.295 0.01 . 1 . . . . . 23 HIS HD1 . 53425 1 295 . 1 . 1 23 23 HIS HD2 H 1 7.295 0.01 . 1 . . . . . 23 HIS HD2 . 53425 1 296 . 1 . 1 23 23 HIS HE1 H 1 8.549 0.01 . 1 . . . . . 23 HIS HE1 . 53425 1 297 . 1 . 1 23 23 HIS HE2 H 1 8.549 0.01 . 1 . . . . . 23 HIS HE2 . 53425 1 298 . 1 . 1 23 23 HIS CA C 13 54.98 0.30 . 1 . . . . . 23 HIS CA . 53425 1 299 . 1 . 1 23 23 HIS CB C 13 29.02 0.30 . 1 . . . . . 23 HIS CB . 53425 1 300 . 1 . 1 23 23 HIS CD2 C 13 119.87 0.30 . 1 . . . . . 23 HIS CD2 . 53425 1 301 . 1 . 1 23 23 HIS CE1 C 13 136.08 0.30 . 1 . . . . . 23 HIS CE1 . 53425 1 302 . 1 . 1 23 23 HIS N N 15 119.96 0.20 . 1 . . . . . 23 HIS N . 53425 1 303 . 1 . 1 24 24 LYS H H 1 8.448 0.01 . 1 . . . . . 24 LYS H . 53425 1 304 . 1 . 1 24 24 LYS HA H 1 4.241 0.01 . 1 . . . . . 24 LYS HA . 53425 1 305 . 1 . 1 24 24 LYS HB2 H 1 1.783 0.01 . . . . . . . 24 LYS HB2 . 53425 1 306 . 1 . 1 24 24 LYS HB3 H 1 1.763 0.01 . . . . . . . 24 LYS HB3 . 53425 1 307 . 1 . 1 24 24 LYS HG2 H 1 1.386 0.01 . . . . . . . 24 LYS HG2 . 53425 1 308 . 1 . 1 24 24 LYS HG3 H 1 1.442 0.01 . . . . . . . 24 LYS HG3 . 53425 1 309 . 1 . 1 24 24 LYS HD2 H 1 1.686 0.01 . . . . . . . 24 LYS HD2 . 53425 1 310 . 1 . 1 24 24 LYS HD3 H 1 1.686 0.01 . . . . . . . 24 LYS HD3 . 53425 1 311 . 1 . 1 24 24 LYS HE2 H 1 2.994 0.01 . . . . . . . 24 LYS HE2 . 53425 1 312 . 1 . 1 24 24 LYS HE3 H 1 2.994 0.01 . . . . . . . 24 LYS HE3 . 53425 1 313 . 1 . 1 24 24 LYS HZ1 H 1 7.540 0.01 . 1 . . . . . 24 LYS QZ . 53425 1 314 . 1 . 1 24 24 LYS HZ2 H 1 7.540 0.01 . 1 . . . . . 24 LYS QZ . 53425 1 315 . 1 . 1 24 24 LYS HZ3 H 1 7.540 0.01 . 1 . . . . . 24 LYS QZ . 53425 1 316 . 1 . 1 24 24 LYS CA C 13 56.29 0.30 . 1 . . . . . 24 LYS CA . 53425 1 317 . 1 . 1 24 24 LYS CB C 13 30.80 0.30 . 1 . . . . . 24 LYS CB . 53425 1 318 . 1 . 1 24 24 LYS CG C 13 24.92 0.30 . 1 . . . . . 24 LYS CG . 53425 1 319 . 1 . 1 24 24 LYS CD C 13 29.01 0.30 . 1 . . . . . 24 LYS CD . 53425 1 320 . 1 . 1 24 24 LYS CE C 13 41.87 0.30 . 1 . . . . . 24 LYS CE . 53425 1 321 . 1 . 1 24 24 LYS N N 15 122.68 0.20 . 1 . . . . . 24 LYS N . 53425 1 322 . 1 . 1 25 25 LYS H H 1 8.385 0.01 . 1 . . . . . 25 LYS H . 53425 1 323 . 1 . 1 25 25 LYS HA H 1 4.280 0.01 . 1 . . . . . 25 LYS HA . 53425 1 324 . 1 . 1 25 25 LYS HB2 H 1 1.766 0.01 . . . . . . . 25 LYS HB2 . 53425 1 325 . 1 . 1 25 25 LYS HB3 H 1 1.691 0.01 . . . . . . . 25 LYS HB3 . 53425 1 326 . 1 . 1 25 25 LYS HG2 H 1 1.390 0.01 . . . . . . . 25 LYS HG2 . 53425 1 327 . 1 . 1 25 25 LYS HG3 H 1 1.390 0.01 . . . . . . . 25 LYS HG3 . 53425 1 328 . 1 . 1 25 25 LYS HD2 H 1 1.654 0.01 . . . . . . . 25 LYS HD2 . 53425 1 329 . 1 . 1 25 25 LYS HD3 H 1 1.654 0.01 . . . . . . . 25 LYS HD3 . 53425 1 330 . 1 . 1 25 25 LYS HE2 H 1 2.988 0.01 . . . . . . . 25 LYS HE2 . 53425 1 331 . 1 . 1 25 25 LYS HE3 H 1 2.988 0.01 . . . . . . . 25 LYS HE3 . 53425 1 332 . 1 . 1 25 25 LYS HZ1 H 1 7.750 0.01 . 1 . . . . . 25 LYS QZ . 53425 1 333 . 1 . 1 25 25 LYS HZ2 H 1 7.750 0.01 . 1 . . . . . 25 LYS QZ . 53425 1 334 . 1 . 1 25 25 LYS HZ3 H 1 7.750 0.01 . 1 . . . . . 25 LYS QZ . 53425 1 335 . 1 . 1 25 25 LYS CA C 13 56.21 0.30 . 1 . . . . . 25 LYS CA . 53425 1 336 . 1 . 1 25 25 LYS CB C 13 30.96 0.30 . 1 . . . . . 25 LYS CB . 53425 1 337 . 1 . 1 25 25 LYS CG C 13 24.92 0.30 . 1 . . . . . 25 LYS CG . 53425 1 338 . 1 . 1 25 25 LYS CD C 13 29.01 0.30 . 1 . . . . . 25 LYS CD . 53425 1 339 . 1 . 1 25 25 LYS CE C 13 41.83 0.30 . 1 . . . . . 25 LYS CE . 53425 1 340 . 1 . 1 25 25 LYS N N 15 122.40 0.20 . 1 . . . . . 25 LYS N . 53425 1 341 . 1 . 1 26 26 HIS H H 1 8.526 0.01 . 1 . . . . . 26 HIS H . 53425 1 342 . 1 . 1 26 26 HIS HA H 1 4.702 0.01 . 1 . . . . . 26 HIS HA . 53425 1 343 . 1 . 1 26 26 HIS HB2 H 1 3.237 0.01 . . . . . . . 26 HIS HB2 . 53425 1 344 . 1 . 1 26 26 HIS HB3 H 1 3.146 0.01 . . . . . . . 26 HIS HB3 . 53425 1 345 . 1 . 1 26 26 HIS HD1 H 1 7.265 0.01 . 1 . . . . . 26 HIS HD1 . 53425 1 346 . 1 . 1 26 26 HIS HD2 H 1 7.265 0.01 . 1 . . . . . 26 HIS HD2 . 53425 1 347 . 1 . 1 26 26 HIS HE1 H 1 8.604 0.01 . 1 . . . . . 26 HIS HE1 . 53425 1 348 . 1 . 1 26 26 HIS HE2 H 1 8.604 0.01 . 1 . . . . . 26 HIS HE2 . 53425 1 349 . 1 . 1 26 26 HIS CA C 13 54.89 0.30 . 1 . . . . . 26 HIS CA . 53425 1 350 . 1 . 1 26 26 HIS CB C 13 28.92 0.30 . 1 . . . . . 26 HIS CB . 53425 1 351 . 1 . 1 26 26 HIS CD2 C 13 119.87 0.30 . 1 . . . . . 26 HIS CD2 . 53425 1 352 . 1 . 1 26 26 HIS CE1 C 13 136.16 0.30 . 1 . . . . . 26 HIS CE1 . 53425 1 353 . 1 . 1 26 26 HIS N N 15 118.69 0.20 . 1 . . . . . 26 HIS N . 53425 1 354 . 1 . 1 27 27 LEU H H 1 8.148 0.01 . 1 . . . . . 27 LEU H . 53425 1 355 . 1 . 1 27 27 LEU HA H 1 4.300 0.01 . 1 . . . . . 27 LEU HA . 53425 1 356 . 1 . 1 27 27 LEU HB2 H 1 1.602 0.01 . . . . . . . 27 LEU HB2 . 53425 1 357 . 1 . 1 27 27 LEU HB3 H 1 1.602 0.01 . . . . . . . 27 LEU HB3 . 53425 1 358 . 1 . 1 27 27 LEU HG H 1 1.476 0.01 . 1 . . . . . 27 LEU HG . 53425 1 359 . 1 . 1 27 27 LEU HD11 H 1 0.845 0.01 . . . . . . . 27 LEU HD1 . 53425 1 360 . 1 . 1 27 27 LEU HD12 H 1 0.845 0.01 . . . . . . . 27 LEU HD1 . 53425 1 361 . 1 . 1 27 27 LEU HD13 H 1 0.845 0.01 . . . . . . . 27 LEU HD1 . 53425 1 362 . 1 . 1 27 27 LEU HD21 H 1 0.917 0.01 . . . . . . . 27 LEU HD2 . 53425 1 363 . 1 . 1 27 27 LEU HD22 H 1 0.917 0.01 . . . . . . . 27 LEU HD2 . 53425 1 364 . 1 . 1 27 27 LEU HD23 H 1 0.917 0.01 . . . . . . . 27 LEU HD2 . 53425 1 365 . 1 . 1 27 27 LEU CA C 13 55.53 0.30 . 1 . . . . . 27 LEU CA . 53425 1 366 . 1 . 1 27 27 LEU CB C 13 42.45 0.30 . 1 . . . . . 27 LEU CB . 53425 1 367 . 1 . 1 27 27 LEU CG C 13 24.93 0.30 . 1 . . . . . 27 LEU CG . 53425 1 368 . 1 . 1 27 27 LEU CD1 C 13 23.47 0.30 . . . . . . . 27 LEU CD1 . 53425 1 369 . 1 . 1 27 27 LEU CD2 C 13 24.82 0.30 . . . . . . . 27 LEU CD2 . 53425 1 370 . 1 . 1 27 27 LEU N N 15 126.84 0.20 . 1 . . . . . 27 LEU N . 53425 1 371 . 1 . 1 28 28 ASN H H 1 8.602 0.01 . 1 . . . . . 28 ASN H . 53425 1 372 . 1 . 1 28 28 ASN HA H 1 4.666 0.01 . 1 . . . . . 28 ASN HA . 53425 1 373 . 1 . 1 28 28 ASN HB2 H 1 2.771 0.01 . . . . . . . 28 ASN HB2 . 53425 1 374 . 1 . 1 28 28 ASN HB3 H 1 2.876 0.01 . . . . . . . 28 ASN HB3 . 53425 1 375 . 1 . 1 28 28 ASN HD21 H 1 6.945 0.01 . . . . . . . 28 ASN HD21 . 53425 1 376 . 1 . 1 28 28 ASN HD22 H 1 7.630 0.01 . . . . . . . 28 ASN HD22 . 53425 1 377 . 1 . 1 28 28 ASN CA C 13 53.25 0.30 . 1 . . . . . 28 ASN CA . 53425 1 378 . 1 . 1 28 28 ASN CB C 13 38.24 0.30 . 1 . . . . . 28 ASN CB . 53425 1 379 . 1 . 1 28 28 ASN N N 15 119.12 0.20 . 1 . . . . . 28 ASN N . 53425 1 380 . 1 . 1 29 29 GLU H H 1 8.294 0.01 . 1 . . . . . 29 GLU H . 53425 1 381 . 1 . 1 29 29 GLU HA H 1 4.227 0.01 . 1 . . . . . 29 GLU HA . 53425 1 382 . 1 . 1 29 29 GLU HB2 H 1 1.973 0.01 . . . . . . . 29 GLU HB2 . 53425 1 383 . 1 . 1 29 29 GLU HB3 H 1 1.921 0.01 . . . . . . . 29 GLU HB3 . 53425 1 384 . 1 . 1 29 29 GLU HG2 H 1 2.278 0.01 . . . . . . . 29 GLU HG2 . 53425 1 385 . 1 . 1 29 29 GLU HG3 H 1 2.231 0.01 . . . . . . . 29 GLU HG3 . 53425 1 386 . 1 . 1 29 29 GLU CA C 13 56.34 0.30 . 1 . . . . . 29 GLU CA . 53425 1 387 . 1 . 1 29 29 GLU CB C 13 30.07 0.30 . 1 . . . . . 29 GLU CB . 53425 1 388 . 1 . 1 29 29 GLU CG C 13 35.41 0.30 . 1 . . . . . 29 GLU CG . 53425 1 389 . 1 . 1 29 29 GLU N N 15 124.12 0.20 . 1 . . . . . 29 GLU N . 53425 1 390 . 1 . 1 30 30 ARG H H 1 8.411 0.01 . 1 . . . . . 30 ARG H . 53425 1 391 . 1 . 1 30 30 ARG HA H 1 4.310 0.01 . 1 . . . . . 30 ARG HA . 53425 1 392 . 1 . 1 30 30 ARG HB2 H 1 1.895 0.01 . . . . . . . 30 ARG HB2 . 53425 1 393 . 1 . 1 30 30 ARG HB3 H 1 1.791 0.01 . . . . . . . 30 ARG HB3 . 53425 1 394 . 1 . 1 30 30 ARG HG2 H 1 1.645 0.01 . . . . . . . 30 ARG HG2 . 53425 1 395 . 1 . 1 30 30 ARG HG3 H 1 1.645 0.01 . . . . . . . 30 ARG HG3 . 53425 1 396 . 1 . 1 30 30 ARG HD2 H 1 3.194 0.01 . . . . . . . 30 ARG HD2 . 53425 1 397 . 1 . 1 30 30 ARG HD3 H 1 3.194 0.01 . . . . . . . 30 ARG HD3 . 53425 1 398 . 1 . 1 30 30 ARG HE H 1 7.205 0.01 . 1 . . . . . 30 ARG HE . 53425 1 399 . 1 . 1 30 30 ARG CA C 13 55.2 0.30 . 1 . . . . . 30 ARG CA . 53425 1 400 . 1 . 1 30 30 ARG CB C 13 30.67 0.30 . 1 . . . . . 30 ARG CB . 53425 1 401 . 1 . 1 30 30 ARG CG C 13 27.05 0.30 . 1 . . . . . 30 ARG CG . 53425 1 402 . 1 . 1 30 30 ARG CD C 13 43.23 0.30 . 1 . . . . . 30 ARG CD . 53425 1 403 . 1 . 1 30 30 ARG N N 15 120.76 0.20 . 1 . . . . . 30 ARG N . 53425 1 stop_ save_