data_5114 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5114 _Entry.Title ; Refined Structure and Metal Binding site of the Kalata B1 Peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-08-15 _Entry.Accession_date 2001-08-15 _Entry.Last_release_date 2001-08-15 _Entry.Original_release_date 2001-08-15 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 . _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 L. Skjeldal . . . . 5114 2 L. Gran . . . . 5114 3 K. Sletten . . . . 5114 4 B. Volkman . F. . . 5114 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5114 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 169 5114 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 . . 2002-04-08 . original BMRB . 5114 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1JJZ 'BMRB Entry Tracking System' 5114 PDB 1K48 'BMRB Entry Tracking System' 5114 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5114 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21885728 _Citation.DOI . _Citation.PubMed_ID 11888199 _Citation.Full_citation . _Citation.Title ; Refined Structure and Metal Binding Site of the Kalata B1 Peptide ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Arch. Biochem. Biophys.' _Citation.Journal_name_full . _Citation.Journal_volume 399 _Citation.Journal_issue 2 _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 142 _Citation.Page_last 148 _Citation.Year 2002 _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 L. Skjeldal . . . . 5114 1 2 L. Gran . . . . 5114 1 3 K. Sletten . . . . 5114 1 4 B. Volkman . F. . . 5114 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'cyclic peptide' 5114 1 cyclotide 5114 1 'disulfide pairing' 5114 1 uterotonic 5114 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_kalata_B1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_kalata_B1 _Assembly.Entry_ID 5114 _Assembly.ID 1 _Assembly.Name 'KALATA B1' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5114 1 stop_ 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 'kalata B1' 1 $kalata_B1 . . . native . . . . . 5114 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 6 6 SG . 1 . 1 CYS 27 27 SG . . . . . . . . . . . . 5114 1 2 disulfide single . 1 . 1 CYS 10 10 SG . 1 . 1 CYS 22 22 SG . . . . . . . . . . . . 5114 1 3 disulfide single . 1 . 1 CYS 15 15 SG . 1 . 1 CYS 20 20 SG . . . . . . . . . . . . 5114 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1JJZ . . . . . . 5114 1 yes PDB 1K48 . . . . . . 5114 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'KALATA B1' system 5114 1 'kalata B1' abbreviation 5114 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_kalata_B1 _Entity.Sf_category entity _Entity.Sf_framecode kalata_B1 _Entity.Entry_ID 5114 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'kalata B1' _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 ; NGLPVCGETCVGGTCNTPGC TCSWPVCTR ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 29 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 6627 . 'Kalata B1' . . . . . 82.76 29 100.00 100.00 2.11e-04 . . . . 5114 1 2 no PDB 1JJZ . 'Refined Structure And Disulfide Pairing Of The Kalata B1 Peptide' . . . . . 93.10 29 100.00 100.00 7.69e-06 . . . . 5114 1 3 no PDB 1K48 . 'Refined Structure And Disulfide Pairing Of The Kalata B1 Peptide' . . . . . 93.10 29 100.00 100.00 7.69e-06 . . . . 5114 1 4 no PDB 1KAL . 'Elucidation Of The Primary And Three-Dimensional Structure Of The Uterotonic Polypeptide Kalata B1' . . . . . 75.86 29 100.00 100.00 8.29e-03 . . . . 5114 1 5 no PDB 1NB1 . 'High Resolution Solution Structure Of Kalata B1' . . . . . 82.76 29 100.00 100.00 2.11e-04 . . . . 5114 1 6 no PDB 1ORX . 'Solution Structure Of The Acyclic Permutant Des-(24-28)- Kalata B1' . . . . . 79.31 24 100.00 100.00 1.30e-03 . . . . 5114 1 7 no PDB 1ZNU . 'Structure Of Cyclotide Kalata B1 In Dpc Micelles Solution' . . . . . 79.31 29 100.00 100.00 6.84e-04 . . . . 5114 1 8 no PIR A56283 . 'kalata B1 [validated] - Oldenlandia affinis' . . . . . 75.86 29 100.00 100.00 7.20e-03 . . . . 5114 1 9 no SWISS-PROT P83938 . Kalata-B4 . . . . . 96.55 29 100.00 100.00 1.22e-06 . . . . 5114 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'kalata B1' abbreviation 5114 1 'kalata B1' common 5114 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 8 ASN . 5114 1 2 9 GLY . 5114 1 3 10 LEU . 5114 1 4 11 PRO . 5114 1 5 12 VAL . 5114 1 6 13 CYS . 5114 1 7 14 GLY . 5114 1 8 15 GLU . 5114 1 9 16 THR . 5114 1 10 17 CYS . 5114 1 11 18 VAL . 5114 1 12 19 GLY . 5114 1 13 20 GLY . 5114 1 14 21 THR . 5114 1 15 22 CYS . 5114 1 16 23 ASN . 5114 1 17 24 THR . 5114 1 18 25 PRO . 5114 1 19 26 GLY . 5114 1 20 27 CYS . 5114 1 21 28 THR . 5114 1 22 29 CYS . 5114 1 23 30 SER . 5114 1 24 31 TRP . 5114 1 25 32 PRO . 5114 1 26 33 VAL . 5114 1 27 34 CYS . 5114 1 28 35 THR . 5114 1 29 36 ARG . 5114 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 . ASN 1 1 5114 1 . GLY 2 2 5114 1 . LEU 3 3 5114 1 . PRO 4 4 5114 1 . VAL 5 5 5114 1 . CYS 6 6 5114 1 . GLY 7 7 5114 1 . GLU 8 8 5114 1 . THR 9 9 5114 1 . CYS 10 10 5114 1 . VAL 11 11 5114 1 . GLY 12 12 5114 1 . GLY 13 13 5114 1 . THR 14 14 5114 1 . CYS 15 15 5114 1 . ASN 16 16 5114 1 . THR 17 17 5114 1 . PRO 18 18 5114 1 . GLY 19 19 5114 1 . CYS 20 20 5114 1 . THR 21 21 5114 1 . CYS 22 22 5114 1 . SER 23 23 5114 1 . TRP 24 24 5114 1 . PRO 25 25 5114 1 . VAL 26 26 5114 1 . CYS 27 27 5114 1 . THR 28 28 5114 1 . ARG 29 29 5114 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 5114 _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 $kalata_B1 . 60225 . . 'Oldenlandia affinis' 'Oldenlandia affinis' . . Eukaryota Viridiplantae Oldenlandia affinis . . . . . . . . . . . . . 5114 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 5114 _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 $kalata_B1 . 'purified from the natural source' . . . . . . . . . . . . . . . . 5114 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5114 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 'kalata B1' . . . 1 $kalata_B1 . . 5 . . mM . . . . 5114 1 2 H2O . . . . . . . 90 . . % . . . . 5114 1 3 D2O . . . . . . . 10 . . % . . . . 5114 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 5114 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 3 . n/a 5114 1 pressure 1 . atm 5114 1 temperature 298 . K 5114 1 stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 5114 _Software.ID 1 _Software.Type . _Software.Name DYANA _Software.Version 1.5 _Software.DOI . _Software.Details 'P. Guentert' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 5114 1 stop_ save_ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5114 _Software.ID 2 _Software.Type . _Software.Name xwinnmr _Software.Version 2.6 _Software.DOI . _Software.Details Bruker loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 5114 2 stop_ save_ save_Xeasy _Software.Sf_category software _Software.Sf_framecode Xeasy _Software.Entry_ID 5114 _Software.ID 3 _Software.Type . _Software.Name XEASY _Software.Version 1.3.11 _Software.DOI . _Software.Details 'C. Bartels' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5114 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5114 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5114 _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 NMR_spectrometer Bruker DMX . 750 . . . 5114 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 5114 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5114 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5114 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal . 1.0 . . . . . 5114 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_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 5114 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D NOESY' 1 $sample_1 . 5114 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.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 ASN H H 1 9.52 0.02 . 1 . . . . . 8 . . . 5114 1 2 . 1 1 1 1 ASN HA H 1 4.36 0.02 . 1 . . . . . 8 . . . 5114 1 3 . 1 1 1 1 ASN HB2 H 1 3.06 0.02 . 2 . . . . . 8 . . . 5114 1 4 . 1 1 1 1 ASN HB3 H 1 2.80 0.02 . 2 . . . . . 8 . . . 5114 1 5 . 1 1 1 1 ASN HD21 H 1 7.57 0.02 . 2 . . . . . 8 . . . 5114 1 6 . 1 1 1 1 ASN HD22 H 1 6.92 0.02 . 2 . . . . . 8 . . . 5114 1 7 . 1 1 2 2 GLY H H 1 8.72 0.02 . 1 . . . . . 9 . . . 5114 1 8 . 1 1 2 2 GLY HA2 H 1 4.20 0.02 . 2 . . . . . 9 . . . 5114 1 9 . 1 1 2 2 GLY HA3 H 1 3.56 0.02 . 2 . . . . . 9 . . . 5114 1 10 . 1 1 3 3 LEU H H 1 7.72 0.02 . 1 . . . . . 10 . . . 5114 1 11 . 1 1 3 3 LEU HA H 1 5.02 0.02 . 1 . . . . . 10 . . . 5114 1 12 . 1 1 3 3 LEU HB2 H 1 1.88 0.02 . 2 . . . . . 10 . . . 5114 1 13 . 1 1 3 3 LEU HB3 H 1 1.45 0.02 . 2 . . . . . 10 . . . 5114 1 14 . 1 1 3 3 LEU HG H 1 1.67 0.02 . 1 . . . . . 10 . . . 5114 1 15 . 1 1 3 3 LEU HD11 H 1 0.95 0.02 . 2 . . . . . 10 . . . 5114 1 16 . 1 1 3 3 LEU HD12 H 1 0.95 0.02 . 2 . . . . . 10 . . . 5114 1 17 . 1 1 3 3 LEU HD13 H 1 0.95 0.02 . 2 . . . . . 10 . . . 5114 1 18 . 1 1 3 3 LEU HD21 H 1 0.88 0.02 . 2 . . . . . 10 . . . 5114 1 19 . 1 1 3 3 LEU HD22 H 1 0.88 0.02 . 2 . . . . . 10 . . . 5114 1 20 . 1 1 3 3 LEU HD23 H 1 0.88 0.02 . 2 . . . . . 10 . . . 5114 1 21 . 1 1 4 4 PRO HA H 1 5.03 0.02 . 1 . . . . . 11 . . . 5114 1 22 . 1 1 4 4 PRO HB2 H 1 2.42 0.02 . 2 . . . . . 11 . . . 5114 1 23 . 1 1 4 4 PRO HB3 H 1 1.68 0.02 . 2 . . . . . 11 . . . 5114 1 24 . 1 1 4 4 PRO HG2 H 1 2.12 0.02 . 2 . . . . . 11 . . . 5114 1 25 . 1 1 4 4 PRO HG3 H 1 2.01 0.02 . 2 . . . . . 11 . . . 5114 1 26 . 1 1 4 4 PRO HD2 H 1 3.76 0.02 . 2 . . . . . 11 . . . 5114 1 27 . 1 1 4 4 PRO HD3 H 1 3.72 0.02 . 2 . . . . . 11 . . . 5114 1 28 . 1 1 5 5 VAL H H 1 8.10 0.02 . 1 . . . . . 12 . . . 5114 1 29 . 1 1 5 5 VAL HA H 1 4.63 0.02 . 1 . . . . . 12 . . . 5114 1 30 . 1 1 5 5 VAL HB H 1 2.55 0.02 . 1 . . . . . 12 . . . 5114 1 31 . 1 1 5 5 VAL HG11 H 1 0.85 0.02 . 2 . . . . . 12 . . . 5114 1 32 . 1 1 5 5 VAL HG12 H 1 0.85 0.02 . 2 . . . . . 12 . . . 5114 1 33 . 1 1 5 5 VAL HG13 H 1 0.85 0.02 . 2 . . . . . 12 . . . 5114 1 34 . 1 1 5 5 VAL HG21 H 1 0.80 0.02 . 2 . . . . . 12 . . . 5114 1 35 . 1 1 5 5 VAL HG22 H 1 0.80 0.02 . 2 . . . . . 12 . . . 5114 1 36 . 1 1 5 5 VAL HG23 H 1 0.80 0.02 . 2 . . . . . 12 . . . 5114 1 37 . 1 1 6 6 CYS H H 1 7.96 0.02 . 1 . . . . . 13 . . . 5114 1 38 . 1 1 6 6 CYS HA H 1 4.44 0.02 . 1 . . . . . 13 . . . 5114 1 39 . 1 1 6 6 CYS HB2 H 1 3.31 0.02 . 2 . . . . . 13 . . . 5114 1 40 . 1 1 6 6 CYS HB3 H 1 2.96 0.02 . 2 . . . . . 13 . . . 5114 1 41 . 1 1 7 7 GLY H H 1 8.49 0.02 . 1 . . . . . 14 . . . 5114 1 42 . 1 1 7 7 GLY HA2 H 1 3.81 0.02 . 2 . . . . . 14 . . . 5114 1 43 . 1 1 7 7 GLY HA3 H 1 3.71 0.02 . 2 . . . . . 14 . . . 5114 1 44 . 1 1 8 8 GLU H H 1 7.14 0.02 . 1 . . . . . 15 . . . 5114 1 45 . 1 1 8 8 GLU HA H 1 4.76 0.02 . 1 . . . . . 15 . . . 5114 1 46 . 1 1 8 8 GLU HB2 H 1 1.98 0.02 . 2 . . . . . 15 . . . 5114 1 47 . 1 1 8 8 GLU HB3 H 1 1.84 0.02 . 2 . . . . . 15 . . . 5114 1 48 . 1 1 8 8 GLU HG2 H 1 2.55 0.02 . 2 . . . . . 15 . . . 5114 1 49 . 1 1 8 8 GLU HG3 H 1 2.49 0.02 . 2 . . . . . 15 . . . 5114 1 50 . 1 1 9 9 THR H H 1 8.43 0.02 . 1 . . . . . 16 . . . 5114 1 51 . 1 1 9 9 THR HA H 1 4.53 0.02 . 1 . . . . . 16 . . . 5114 1 52 . 1 1 9 9 THR HB H 1 4.41 0.02 . 1 . . . . . 16 . . . 5114 1 53 . 1 1 9 9 THR HG21 H 1 1.11 0.02 . 1 . . . . . 16 . . . 5114 1 54 . 1 1 9 9 THR HG22 H 1 1.11 0.02 . 1 . . . . . 16 . . . 5114 1 55 . 1 1 9 9 THR HG23 H 1 1.11 0.02 . 1 . . . . . 16 . . . 5114 1 56 . 1 1 10 10 CYS H H 1 8.31 0.02 . 1 . . . . . 17 . . . 5114 1 57 . 1 1 10 10 CYS HA H 1 4.91 0.02 . 1 . . . . . 17 . . . 5114 1 58 . 1 1 10 10 CYS HB2 H 1 3.15 0.02 . 2 . . . . . 17 . . . 5114 1 59 . 1 1 10 10 CYS HB3 H 1 2.87 0.02 . 2 . . . . . 17 . . . 5114 1 60 . 1 1 11 11 VAL H H 1 8.51 0.02 . 1 . . . . . 18 . . . 5114 1 61 . 1 1 11 11 VAL HA H 1 3.81 0.02 . 1 . . . . . 18 . . . 5114 1 62 . 1 1 11 11 VAL HB H 1 2.00 0.02 . 1 . . . . . 18 . . . 5114 1 63 . 1 1 11 11 VAL HG11 H 1 0.99 0.02 . 2 . . . . . 18 . . . 5114 1 64 . 1 1 11 11 VAL HG12 H 1 0.99 0.02 . 2 . . . . . 18 . . . 5114 1 65 . 1 1 11 11 VAL HG13 H 1 0.99 0.02 . 2 . . . . . 18 . . . 5114 1 66 . 1 1 11 11 VAL HG21 H 1 0.91 0.02 . 2 . . . . . 18 . . . 5114 1 67 . 1 1 11 11 VAL HG22 H 1 0.91 0.02 . 2 . . . . . 18 . . . 5114 1 68 . 1 1 11 11 VAL HG23 H 1 0.91 0.02 . 2 . . . . . 18 . . . 5114 1 69 . 1 1 12 12 GLY H H 1 8.65 0.02 . 1 . . . . . 19 . . . 5114 1 70 . 1 1 12 12 GLY HA2 H 1 4.22 0.02 . 2 . . . . . 19 . . . 5114 1 71 . 1 1 12 12 GLY HA3 H 1 3.80 0.02 . 2 . . . . . 19 . . . 5114 1 72 . 1 1 13 13 GLY H H 1 8.18 0.02 . 1 . . . . . 20 . . . 5114 1 73 . 1 1 13 13 GLY HA2 H 1 4.38 0.02 . 2 . . . . . 20 . . . 5114 1 74 . 1 1 13 13 GLY HA3 H 1 4.00 0.02 . 2 . . . . . 20 . . . 5114 1 75 . 1 1 14 14 THR H H 1 7.82 0.02 . 1 . . . . . 21 . . . 5114 1 76 . 1 1 14 14 THR HA H 1 4.06 0.02 . 1 . . . . . 21 . . . 5114 1 77 . 1 1 14 14 THR HB H 1 4.68 0.02 . 1 . . . . . 21 . . . 5114 1 78 . 1 1 14 14 THR HG21 H 1 1.11 0.02 . 1 . . . . . 21 . . . 5114 1 79 . 1 1 14 14 THR HG22 H 1 1.11 0.02 . 1 . . . . . 21 . . . 5114 1 80 . 1 1 14 14 THR HG23 H 1 1.11 0.02 . 1 . . . . . 21 . . . 5114 1 81 . 1 1 15 15 CYS H H 1 8.68 0.02 . 1 . . . . . 22 . . . 5114 1 82 . 1 1 15 15 CYS HA H 1 4.67 0.02 . 1 . . . . . 22 . . . 5114 1 83 . 1 1 15 15 CYS HB2 H 1 3.00 0.02 . 2 . . . . . 22 . . . 5114 1 84 . 1 1 15 15 CYS HB3 H 1 2.73 0.02 . 2 . . . . . 22 . . . 5114 1 85 . 1 1 16 16 ASN H H 1 9.32 0.02 . 1 . . . . . 23 . . . 5114 1 86 . 1 1 16 16 ASN HA H 1 4.67 0.02 . 1 . . . . . 23 . . . 5114 1 87 . 1 1 16 16 ASN HB2 H 1 2.77 0.02 . 1 . . . . . 23 . . . 5114 1 88 . 1 1 16 16 ASN HB3 H 1 2.77 0.02 . 1 . . . . . 23 . . . 5114 1 89 . 1 1 16 16 ASN HD21 H 1 7.61 0.02 . 2 . . . . . 23 . . . 5114 1 90 . 1 1 16 16 ASN HD22 H 1 6.89 0.02 . 2 . . . . . 23 . . . 5114 1 91 . 1 1 17 17 THR H H 1 8.29 0.02 . 1 . . . . . 24 . . . 5114 1 92 . 1 1 17 17 THR HA H 1 4.47 0.02 . 1 . . . . . 24 . . . 5114 1 93 . 1 1 17 17 THR HB H 1 4.17 0.02 . 1 . . . . . 24 . . . 5114 1 94 . 1 1 17 17 THR HG21 H 1 1.30 0.02 . 1 . . . . . 24 . . . 5114 1 95 . 1 1 17 17 THR HG22 H 1 1.30 0.02 . 1 . . . . . 24 . . . 5114 1 96 . 1 1 17 17 THR HG23 H 1 1.30 0.02 . 1 . . . . . 24 . . . 5114 1 97 . 1 1 18 18 PRO HA H 1 4.23 0.02 . 1 . . . . . 25 . . . 5114 1 98 . 1 1 18 18 PRO HB2 H 1 2.29 0.02 . 2 . . . . . 25 . . . 5114 1 99 . 1 1 18 18 PRO HB3 H 1 1.87 0.02 . 2 . . . . . 25 . . . 5114 1 100 . 1 1 18 18 PRO HG2 H 1 2.11 0.02 . 2 . . . . . 25 . . . 5114 1 101 . 1 1 18 18 PRO HG3 H 1 1.97 0.02 . 2 . . . . . 25 . . . 5114 1 102 . 1 1 18 18 PRO HD2 H 1 4.11 0.02 . 2 . . . . . 25 . . . 5114 1 103 . 1 1 18 18 PRO HD3 H 1 3.67 0.02 . 2 . . . . . 25 . . . 5114 1 104 . 1 1 19 19 GLY H H 1 8.75 0.02 . 1 . . . . . 26 . . . 5114 1 105 . 1 1 19 19 GLY HA2 H 1 4.15 0.02 . 2 . . . . . 26 . . . 5114 1 106 . 1 1 19 19 GLY HA3 H 1 3.65 0.02 . 2 . . . . . 26 . . . 5114 1 107 . 1 1 20 20 CYS H H 1 7.66 0.02 . 1 . . . . . 27 . . . 5114 1 108 . 1 1 20 20 CYS HA H 1 5.29 0.02 . 1 . . . . . 27 . . . 5114 1 109 . 1 1 20 20 CYS HB2 H 1 3.78 0.02 . 2 . . . . . 27 . . . 5114 1 110 . 1 1 20 20 CYS HB3 H 1 2.58 0.02 . 2 . . . . . 27 . . . 5114 1 111 . 1 1 21 21 THR H H 1 9.48 0.02 . 1 . . . . . 28 . . . 5114 1 112 . 1 1 21 21 THR HA H 1 4.49 0.02 . 1 . . . . . 28 . . . 5114 1 113 . 1 1 21 21 THR HB H 1 4.00 0.02 . 1 . . . . . 28 . . . 5114 1 114 . 1 1 21 21 THR HG21 H 1 1.09 0.02 . 1 . . . . . 28 . . . 5114 1 115 . 1 1 21 21 THR HG22 H 1 1.09 0.02 . 1 . . . . . 28 . . . 5114 1 116 . 1 1 21 21 THR HG23 H 1 1.09 0.02 . 1 . . . . . 28 . . . 5114 1 117 . 1 1 22 22 CYS H H 1 8.92 0.02 . 1 . . . . . 29 . . . 5114 1 118 . 1 1 22 22 CYS HA H 1 4.56 0.02 . 1 . . . . . 29 . . . 5114 1 119 . 1 1 22 22 CYS HB2 H 1 3.08 0.02 . 2 . . . . . 29 . . . 5114 1 120 . 1 1 22 22 CYS HB3 H 1 2.78 0.02 . 2 . . . . . 29 . . . 5114 1 121 . 1 1 23 23 SER H H 1 8.92 0.02 . 1 . . . . . 30 . . . 5114 1 122 . 1 1 23 23 SER HA H 1 4.74 0.02 . 1 . . . . . 30 . . . 5114 1 123 . 1 1 23 23 SER HB2 H 1 3.81 0.02 . 1 . . . . . 30 . . . 5114 1 124 . 1 1 23 23 SER HB3 H 1 3.81 0.02 . 1 . . . . . 30 . . . 5114 1 125 . 1 1 24 24 TRP H H 1 7.94 0.02 . 1 . . . . . 31 . . . 5114 1 126 . 1 1 24 24 TRP HA H 1 4.02 0.02 . 1 . . . . . 31 . . . 5114 1 127 . 1 1 24 24 TRP HB2 H 1 3.21 0.02 . 1 . . . . . 31 . . . 5114 1 128 . 1 1 24 24 TRP HB3 H 1 3.21 0.02 . 1 . . . . . 31 . . . 5114 1 129 . 1 1 24 24 TRP HD1 H 1 7.26 0.02 . 1 . . . . . 31 . . . 5114 1 130 . 1 1 24 24 TRP HE3 H 1 7.39 0.02 . 1 . . . . . 31 . . . 5114 1 131 . 1 1 24 24 TRP HE1 H 1 10.38 0.02 . 1 . . . . . 31 . . . 5114 1 132 . 1 1 24 24 TRP HZ3 H 1 7.07 0.02 . 1 . . . . . 31 . . . 5114 1 133 . 1 1 24 24 TRP HZ2 H 1 7.47 0.02 . 1 . . . . . 31 . . . 5114 1 134 . 1 1 24 24 TRP HH2 H 1 7.16 0.02 . 1 . . . . . 31 . . . 5114 1 135 . 1 1 25 25 PRO HA H 1 3.38 0.02 . 1 . . . . . 32 . . . 5114 1 136 . 1 1 25 25 PRO HB2 H 1 1.64 0.02 . 2 . . . . . 32 . . . 5114 1 137 . 1 1 25 25 PRO HB3 H 1 -0.27 0.02 . 2 . . . . . 32 . . . 5114 1 138 . 1 1 25 25 PRO HG2 H 1 1.31 0.02 . 2 . . . . . 32 . . . 5114 1 139 . 1 1 25 25 PRO HG3 H 1 1.23 0.02 . 2 . . . . . 32 . . . 5114 1 140 . 1 1 25 25 PRO HD2 H 1 3.21 0.02 . 2 . . . . . 32 . . . 5114 1 141 . 1 1 25 25 PRO HD3 H 1 3.16 0.02 . 2 . . . . . 32 . . . 5114 1 142 . 1 1 26 26 VAL H H 1 8.25 0.02 . 1 . . . . . 33 . . . 5114 1 143 . 1 1 26 26 VAL HA H 1 4.18 0.02 . 1 . . . . . 33 . . . 5114 1 144 . 1 1 26 26 VAL HB H 1 1.88 0.02 . 1 . . . . . 33 . . . 5114 1 145 . 1 1 26 26 VAL HG11 H 1 0.81 0.02 . 2 . . . . . 33 . . . 5114 1 146 . 1 1 26 26 VAL HG12 H 1 0.81 0.02 . 2 . . . . . 33 . . . 5114 1 147 . 1 1 26 26 VAL HG13 H 1 0.81 0.02 . 2 . . . . . 33 . . . 5114 1 148 . 1 1 26 26 VAL HG21 H 1 0.78 0.02 . 2 . . . . . 33 . . . 5114 1 149 . 1 1 26 26 VAL HG22 H 1 0.78 0.02 . 2 . . . . . 33 . . . 5114 1 150 . 1 1 26 26 VAL HG23 H 1 0.78 0.02 . 2 . . . . . 33 . . . 5114 1 151 . 1 1 27 27 CYS H H 1 7.69 0.02 . 1 . . . . . 34 . . . 5114 1 152 . 1 1 27 27 CYS HA H 1 5.07 0.02 . 1 . . . . . 34 . . . 5114 1 153 . 1 1 27 27 CYS HB2 H 1 3.18 0.02 . 2 . . . . . 34 . . . 5114 1 154 . 1 1 27 27 CYS HB3 H 1 2.71 0.02 . 2 . . . . . 34 . . . 5114 1 155 . 1 1 28 28 THR H H 1 9.83 0.02 . 1 . . . . . 35 . . . 5114 1 156 . 1 1 28 28 THR HA H 1 5.03 0.02 . 1 . . . . . 35 . . . 5114 1 157 . 1 1 28 28 THR HB H 1 3.67 0.02 . 1 . . . . . 35 . . . 5114 1 158 . 1 1 28 28 THR HG21 H 1 0.84 0.02 . 1 . . . . . 35 . . . 5114 1 159 . 1 1 28 28 THR HG22 H 1 0.84 0.02 . 1 . . . . . 35 . . . 5114 1 160 . 1 1 28 28 THR HG23 H 1 0.84 0.02 . 1 . . . . . 35 . . . 5114 1 161 . 1 1 29 29 ARG H H 1 8.67 0.02 . 1 . . . . . 36 . . . 5114 1 162 . 1 1 29 29 ARG HA H 1 4.72 0.02 . 1 . . . . . 36 . . . 5114 1 163 . 1 1 29 29 ARG HB2 H 1 1.64 0.02 . 2 . . . . . 36 . . . 5114 1 164 . 1 1 29 29 ARG HB3 H 1 1.60 0.02 . 2 . . . . . 36 . . . 5114 1 165 . 1 1 29 29 ARG HG2 H 1 1.43 0.02 . 2 . . . . . 36 . . . 5114 1 166 . 1 1 29 29 ARG HG3 H 1 1.39 0.02 . 2 . . . . . 36 . . . 5114 1 167 . 1 1 29 29 ARG HD2 H 1 3.14 0.02 . 2 . . . . . 36 . . . 5114 1 168 . 1 1 29 29 ARG HD3 H 1 3.11 0.02 . 2 . . . . . 36 . . . 5114 1 169 . 1 1 29 29 ARG HE H 1 6.92 0.02 . 1 . . . . . 36 . . . 5114 1 stop_ save_