data_5495 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5495 _Entry.Title ; 1H chemical shift assignments for Psalmotoxin 1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-08-07 _Entry.Accession_date 2002-08-07 _Entry.Last_release_date 2003-07-30 _Entry.Original_release_date 2003-07-30 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Pierre Escoubas . . . 5495 2 Cedric Bernard . . . 5495 3 Gerard Lambeau . . . 5495 4 Michel Lazdunski . . . 5495 5 Herve Darbon . . . 5495 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5495 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 194 5495 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 . . 2003-07-30 2002-08-07 original author . 5495 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1LMM 'BMRB Entry Tracking System' 5495 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5495 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22709212 _Citation.DOI . _Citation.PubMed_ID 12824480 _Citation.Full_citation . _Citation.Title ; Recombinant Production and Solution Structure of PcTx1, the Specific Peptide Inhibitor of ASIC1a Proton-gated Cation Channels ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full . _Citation.Journal_volume 12 _Citation.Journal_issue 7 _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 1332 _Citation.Page_last 1343 _Citation.Year 2003 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Pierre Escoubas . . . 5495 1 2 Cedric Bernard . . . 5495 1 3 Gerard Lambeau . . . 5495 1 4 Michel Lazdunski . . . 5495 1 5 Herve Darbon . . . 5495 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID ASIC 5495 1 ICK 5495 1 'Spider toxin' 5495 1 'structure determination' 5495 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_PcTx1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_PcTx1 _Assembly.Entry_ID 5495 _Assembly.ID 1 _Assembly.Name psalmotoxin1 _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 5495 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 'psalmotoxin 1' 1 $PcTx1 . . . native . . . . . 5495 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . . CYS 3 3 SG . 1 . 1 CYS 18 18 SG . . . . . . . . . . 5495 1 2 disulfide single . 1 . . CYS 10 10 SG . 1 . 1 CYS 23 23 SG . . . . . . . . . . 5495 1 3 disulfide single . 1 . . CYS 17 17 SG . 1 . 1 CYS 33 33 SG . . . . . . . . . . 5495 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 . PDB 1LMM . . . . . . 5495 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID PcTx1 abbreviation 5495 1 psalmotoxin1 system 5495 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PcTx1 _Entity.Sf_category entity _Entity.Sf_framecode PcTx1 _Entity.Entry_ID 5495 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'psalmotoxin 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 ; EDCIPKWKGCVNRHGDCCEG LECWKRRRSFEVCVPKTPKT ; _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 40 _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 . _Entity.DB_query_revised_last_date 2015-01-28 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 16468 . PcTx1 . . . . . 100.00 41 100.00 100.00 9.59e-20 . . . . 5495 1 2 no BMRB 26504 . TRTX-Pc1a . . . . . 100.00 40 100.00 100.00 1.25e-19 . . . . 5495 1 3 no PDB 1LMM . "Solution Structure Of Psmalmotoxin 1, The First Characterized Specific Blocker Of Asic1a Na+ Channel" . . . . . 100.00 40 100.00 100.00 1.25e-19 . . . . 5495 1 4 no PDB 2KNI . "High-resolution Solution Structure Of The Asic1a Blocker Pctx1" . . . . . 100.00 41 100.00 100.00 9.59e-20 . . . . 5495 1 5 no PDB 3S3X . "Structure Of Chicken Acid-Sensing Ion Channel 1 At 3.0 A Resolution In Complex With Psalmotoxin" . . . . . 92.50 37 100.00 100.00 1.27e-17 . . . . 5495 1 6 no PDB 4FZ0 . "Crystal Structure Of Acid-Sensing Ion Channel In Complex With Psalmotoxin 1 At Low Ph" . . . . . 100.00 40 100.00 100.00 1.25e-19 . . . . 5495 1 7 no PDB 4FZ1 . "Crystal Structure Of Acid-Sensing Ion Channel In Complex With Psalmotoxin 1 At High Ph" . . . . . 100.00 40 100.00 100.00 1.25e-19 . . . . 5495 1 8 no SP P60514 . "RecName: Full=Pi-theraphotoxin-Pc1a; Short=Pi-TRTX-Pc1a; AltName: Full=PcTx1; AltName: Full=Psalmotoxin-1 [Psalmopoeus cambridg" . . . . . 100.00 40 100.00 100.00 1.25e-19 . . . . 5495 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID PcTx1 abbreviation 5495 1 'psalmotoxin 1' common 5495 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 . GLU . 5495 1 2 . ASP . 5495 1 3 . CYS . 5495 1 4 . ILE . 5495 1 5 . PRO . 5495 1 6 . LYS . 5495 1 7 . TRP . 5495 1 8 . LYS . 5495 1 9 . GLY . 5495 1 10 . CYS . 5495 1 11 . VAL . 5495 1 12 . ASN . 5495 1 13 . ARG . 5495 1 14 . HIS . 5495 1 15 . GLY . 5495 1 16 . ASP . 5495 1 17 . CYS . 5495 1 18 . CYS . 5495 1 19 . GLU . 5495 1 20 . GLY . 5495 1 21 . LEU . 5495 1 22 . GLU . 5495 1 23 . CYS . 5495 1 24 . TRP . 5495 1 25 . LYS . 5495 1 26 . ARG . 5495 1 27 . ARG . 5495 1 28 . ARG . 5495 1 29 . SER . 5495 1 30 . PHE . 5495 1 31 . GLU . 5495 1 32 . VAL . 5495 1 33 . CYS . 5495 1 34 . VAL . 5495 1 35 . PRO . 5495 1 36 . LYS . 5495 1 37 . THR . 5495 1 38 . PRO . 5495 1 39 . LYS . 5495 1 40 . THR . 5495 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 . GLU 1 1 5495 1 . ASP 2 2 5495 1 . CYS 3 3 5495 1 . ILE 4 4 5495 1 . PRO 5 5 5495 1 . LYS 6 6 5495 1 . TRP 7 7 5495 1 . LYS 8 8 5495 1 . GLY 9 9 5495 1 . CYS 10 10 5495 1 . VAL 11 11 5495 1 . ASN 12 12 5495 1 . ARG 13 13 5495 1 . HIS 14 14 5495 1 . GLY 15 15 5495 1 . ASP 16 16 5495 1 . CYS 17 17 5495 1 . CYS 18 18 5495 1 . GLU 19 19 5495 1 . GLY 20 20 5495 1 . LEU 21 21 5495 1 . GLU 22 22 5495 1 . CYS 23 23 5495 1 . TRP 24 24 5495 1 . LYS 25 25 5495 1 . ARG 26 26 5495 1 . ARG 27 27 5495 1 . ARG 28 28 5495 1 . SER 29 29 5495 1 . PHE 30 30 5495 1 . GLU 31 31 5495 1 . VAL 32 32 5495 1 . CYS 33 33 5495 1 . VAL 34 34 5495 1 . PRO 35 35 5495 1 . LYS 36 36 5495 1 . THR 37 37 5495 1 . PRO 38 38 5495 1 . LYS 39 39 5495 1 . THR 40 40 5495 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 5495 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $PcTx1 . . . . 'Psalmopoeus cambridgei' 'Psalmopoeus cambridgei' . . Eukaryota Metazoa Psalmopoeus cambridgei . . . . . . . . . . . . . . . . . . . . . 5495 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 5495 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $PcTx1 . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5495 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5495 _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 'psalmotoxin 1' . . . 1 $PcTx1 . . 2.9 . . mM . . . . 5495 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5495 _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* 3.0 . n/a 5495 1 temperature 300 . K 5495 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 5495 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 5495 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 5495 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 5495 _Experiment_list.ID 1 _Experiment_list.Details . 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 5495 _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 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5495 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5495 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_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 $sample_1 . 5495 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 GLU HA H 1 4.042 0.001 . 1 . . . . . . . . 5495 1 2 . 1 1 2 2 ASP H H 1 8.863 0.000 . 1 . . . . . . . . 5495 1 3 . 1 1 2 2 ASP HA H 1 4.748 0.001 . 1 . . . . . . . . 5495 1 4 . 1 1 2 2 ASP HB2 H 1 2.786 0.000 . 1 . . . . . . . . 5495 1 5 . 1 1 2 2 ASP HB3 H 1 2.573 0.000 . 1 . . . . . . . . 5495 1 6 . 1 1 3 3 CYS H H 1 8.377 0.000 . 1 . . . . . . . . 5495 1 7 . 1 1 3 3 CYS HA H 1 4.056 0.000 . 1 . . . . . . . . 5495 1 8 . 1 1 4 4 ILE H H 1 8.954 0.000 . 1 . . . . . . . . 5495 1 9 . 1 1 4 4 ILE HA H 1 4.282 0.000 . 1 . . . . . . . . 5495 1 10 . 1 1 4 4 ILE HB H 1 1.785 0.001 . 1 . . . . . . . . 5495 1 11 . 1 1 4 4 ILE HG21 H 1 0.886 0.025 . 1 . . . . . . . . 5495 1 12 . 1 1 4 4 ILE HG22 H 1 0.886 0.025 . 1 . . . . . . . . 5495 1 13 . 1 1 4 4 ILE HG23 H 1 0.886 0.025 . 1 . . . . . . . . 5495 1 14 . 1 1 4 4 ILE HD11 H 1 1.569 0.000 . 1 . . . . . . . . 5495 1 15 . 1 1 4 4 ILE HD12 H 1 1.569 0.000 . 1 . . . . . . . . 5495 1 16 . 1 1 4 4 ILE HD13 H 1 1.569 0.000 . 1 . . . . . . . . 5495 1 17 . 1 1 5 5 PRO HA H 1 4.302 0.000 . 1 . . . . . . . . 5495 1 18 . 1 1 5 5 PRO HG2 H 1 2.030 0.000 . 1 . . . . . . . . 5495 1 19 . 1 1 5 5 PRO HG3 H 1 1.754 0.000 . 1 . . . . . . . . 5495 1 20 . 1 1 5 5 PRO HD2 H 1 4.099 0.000 . 1 . . . . . . . . 5495 1 21 . 1 1 5 5 PRO HD3 H 1 3.593 0.000 . 1 . . . . . . . . 5495 1 22 . 1 1 6 6 LYS H H 1 7.619 0.000 . 1 . . . . . . . . 5495 1 23 . 1 1 6 6 LYS HA H 1 3.264 0.000 . 1 . . . . . . . . 5495 1 24 . 1 1 6 6 LYS HG2 H 1 0.649 0.000 . 1 . . . . . . . . 5495 1 25 . 1 1 6 6 LYS HG3 H 1 0.192 0.000 . 1 . . . . . . . . 5495 1 26 . 1 1 7 7 TRP H H 1 9.287 0.000 . 1 . . . . . . . . 5495 1 27 . 1 1 7 7 TRP HA H 1 4.230 0.001 . 1 . . . . . . . . 5495 1 28 . 1 1 7 7 TRP HD1 H 1 7.083 0.000 . 1 . . . . . . . . 5495 1 29 . 1 1 7 7 TRP HE1 H 1 10.206 0.001 . 1 . . . . . . . . 5495 1 30 . 1 1 7 7 TRP HH2 H 1 7.489 0.000 . 1 . . . . . . . . 5495 1 31 . 1 1 8 8 LYS H H 1 7.774 0.000 . 1 . . . . . . . . 5495 1 32 . 1 1 8 8 LYS HA H 1 4.706 0.000 . 1 . . . . . . . . 5495 1 33 . 1 1 8 8 LYS HB2 H 1 1.745 0.000 . 1 . . . . . . . . 5495 1 34 . 1 1 8 8 LYS HG2 H 1 1.502 0.000 . 1 . . . . . . . . 5495 1 35 . 1 1 8 8 LYS HG3 H 1 1.423 0.000 . 1 . . . . . . . . 5495 1 36 . 1 1 8 8 LYS HD2 H 1 2.001 0.000 . 1 . . . . . . . . 5495 1 37 . 1 1 8 8 LYS HD3 H 1 1.879 0.000 . 1 . . . . . . . . 5495 1 38 . 1 1 9 9 GLY H H 1 8.509 0.000 . 1 . . . . . . . . 5495 1 39 . 1 1 9 9 GLY HA2 H 1 4.666 0.001 . 1 . . . . . . . . 5495 1 40 . 1 1 9 9 GLY HA3 H 1 3.949 0.001 . 1 . . . . . . . . 5495 1 41 . 1 1 10 10 CYS H H 1 8.298 0.000 . 1 . . . . . . . . 5495 1 42 . 1 1 10 10 CYS HA H 1 4.900 0.000 . 1 . . . . . . . . 5495 1 43 . 1 1 10 10 CYS HB2 H 1 3.430 0.000 . 1 . . . . . . . . 5495 1 44 . 1 1 10 10 CYS HB3 H 1 3.159 0.000 . 1 . . . . . . . . 5495 1 45 . 1 1 11 11 VAL H H 1 7.900 0.000 . 1 . . . . . . . . 5495 1 46 . 1 1 11 11 VAL HA H 1 3.786 0.000 . 1 . . . . . . . . 5495 1 47 . 1 1 11 11 VAL HB H 1 1.993 0.000 . 1 . . . . . . . . 5495 1 48 . 1 1 11 11 VAL HG11 H 1 1.147 0.000 . 1 . . . . . . . . 5495 1 49 . 1 1 11 11 VAL HG12 H 1 1.147 0.000 . 1 . . . . . . . . 5495 1 50 . 1 1 11 11 VAL HG13 H 1 1.147 0.000 . 1 . . . . . . . . 5495 1 51 . 1 1 11 11 VAL HG21 H 1 0.922 0.000 . 1 . . . . . . . . 5495 1 52 . 1 1 11 11 VAL HG22 H 1 0.922 0.000 . 1 . . . . . . . . 5495 1 53 . 1 1 11 11 VAL HG23 H 1 0.922 0.000 . 1 . . . . . . . . 5495 1 54 . 1 1 12 12 ASN H H 1 8.925 0.000 . 1 . . . . . . . . 5495 1 55 . 1 1 12 12 ASN HA H 1 4.294 0.000 . 1 . . . . . . . . 5495 1 56 . 1 1 12 12 ASN HB2 H 1 3.048 0.000 . 1 . . . . . . . . 5495 1 57 . 1 1 12 12 ASN HB3 H 1 2.988 0.000 . 1 . . . . . . . . 5495 1 58 . 1 1 12 12 ASN HD21 H 1 7.613 0.000 . 1 . . . . . . . . 5495 1 59 . 1 1 12 12 ASN HD22 H 1 6.919 0.000 . 1 . . . . . . . . 5495 1 60 . 1 1 13 13 ARG H H 1 7.972 0.000 . 1 . . . . . . . . 5495 1 61 . 1 1 13 13 ARG HA H 1 4.614 0.000 . 1 . . . . . . . . 5495 1 62 . 1 1 13 13 ARG HG2 H 1 1.662 0.000 . 1 . . . . . . . . 5495 1 63 . 1 1 13 13 ARG HG3 H 1 1.486 0.000 . 1 . . . . . . . . 5495 1 64 . 1 1 13 13 ARG HD2 H 1 3.272 0.000 . 1 . . . . . . . . 5495 1 65 . 1 1 13 13 ARG HD3 H 1 3.039 0.000 . 1 . . . . . . . . 5495 1 66 . 1 1 13 13 ARG HE H 1 8.223 0.000 . 1 . . . . . . . . 5495 1 67 . 1 1 13 13 ARG HH21 H 1 6.946 0.000 . 1 . . . . . . . . 5495 1 68 . 1 1 13 13 ARG HH22 H 1 6.257 0.000 . 1 . . . . . . . . 5495 1 69 . 1 1 14 14 HIS H H 1 8.695 0.000 . 1 . . . . . . . . 5495 1 70 . 1 1 14 14 HIS HA H 1 4.595 0.001 . 1 . . . . . . . . 5495 1 71 . 1 1 14 14 HIS HD1 H 1 8.531 0.000 . 1 . . . . . . . . 5495 1 72 . 1 1 14 14 HIS HD2 H 1 7.924 0.606 . 1 . . . . . . . . 5495 1 73 . 1 1 14 14 HIS HE1 H 1 7.634 0.000 . 1 . . . . . . . . 5495 1 74 . 1 1 15 15 GLY H H 1 8.846 0.000 . 1 . . . . . . . . 5495 1 75 . 1 1 15 15 GLY HA2 H 1 4.467 0.000 . 1 . . . . . . . . 5495 1 76 . 1 1 15 15 GLY HA3 H 1 3.707 0.000 . 1 . . . . . . . . 5495 1 77 . 1 1 16 16 ASP H H 1 7.408 0.000 . 1 . . . . . . . . 5495 1 78 . 1 1 16 16 ASP HA H 1 4.917 0.000 . 1 . . . . . . . . 5495 1 79 . 1 1 16 16 ASP HB2 H 1 3.241 0.000 . 1 . . . . . . . . 5495 1 80 . 1 1 16 16 ASP HB3 H 1 2.677 0.000 . 1 . . . . . . . . 5495 1 81 . 1 1 17 17 CYS H H 1 8.618 0.000 . 1 . . . . . . . . 5495 1 82 . 1 1 17 17 CYS HA H 1 5.043 0.000 . 1 . . . . . . . . 5495 1 83 . 1 1 17 17 CYS HB2 H 1 2.966 0.000 . 1 . . . . . . . . 5495 1 84 . 1 1 17 17 CYS HB3 H 1 2.772 0.000 . 1 . . . . . . . . 5495 1 85 . 1 1 18 18 CYS H H 1 9.102 0.000 . 1 . . . . . . . . 5495 1 86 . 1 1 18 18 CYS HA H 1 4.451 0.000 . 1 . . . . . . . . 5495 1 87 . 1 1 18 18 CYS HB2 H 1 3.418 0.000 . 1 . . . . . . . . 5495 1 88 . 1 1 18 18 CYS HB3 H 1 2.499 0.000 . 1 . . . . . . . . 5495 1 89 . 1 1 19 19 GLU H H 1 8.221 0.000 . 1 . . . . . . . . 5495 1 90 . 1 1 19 19 GLU HA H 1 4.064 0.000 . 1 . . . . . . . . 5495 1 91 . 1 1 20 20 GLY H H 1 8.887 0.000 . 1 . . . . . . . . 5495 1 92 . 1 1 20 20 GLY HA2 H 1 4.243 0.000 . 1 . . . . . . . . 5495 1 93 . 1 1 20 20 GLY HA3 H 1 3.661 0.000 . 1 . . . . . . . . 5495 1 94 . 1 1 21 21 LEU H H 1 7.820 0.000 . 1 . . . . . . . . 5495 1 95 . 1 1 21 21 LEU HA H 1 5.135 0.000 . 1 . . . . . . . . 5495 1 96 . 1 1 21 21 LEU HB2 H 1 2.082 0.000 . 1 . . . . . . . . 5495 1 97 . 1 1 21 21 LEU HB3 H 1 0.965 0.000 . 1 . . . . . . . . 5495 1 98 . 1 1 21 21 LEU HG H 1 1.250 0.000 . 1 . . . . . . . . 5495 1 99 . 1 1 21 21 LEU HD11 H 1 0.650 0.000 . 1 . . . . . . . . 5495 1 100 . 1 1 21 21 LEU HD12 H 1 0.650 0.000 . 1 . . . . . . . . 5495 1 101 . 1 1 21 21 LEU HD13 H 1 0.650 0.000 . 1 . . . . . . . . 5495 1 102 . 1 1 21 21 LEU HD21 H 1 0.374 0.000 . 1 . . . . . . . . 5495 1 103 . 1 1 21 21 LEU HD22 H 1 0.374 0.000 . 1 . . . . . . . . 5495 1 104 . 1 1 21 21 LEU HD23 H 1 0.374 0.000 . 1 . . . . . . . . 5495 1 105 . 1 1 22 22 GLU H H 1 9.377 0.000 . 1 . . . . . . . . 5495 1 106 . 1 1 22 22 GLU HA H 1 4.670 0.000 . 1 . . . . . . . . 5495 1 107 . 1 1 22 22 GLU HB2 H 1 1.962 0.000 . 1 . . . . . . . . 5495 1 108 . 1 1 22 22 GLU HB3 H 1 1.813 0.000 . 1 . . . . . . . . 5495 1 109 . 1 1 23 23 CYS H H 1 8.935 0.000 . 1 . . . . . . . . 5495 1 110 . 1 1 23 23 CYS HA H 1 4.769 0.000 . 1 . . . . . . . . 5495 1 111 . 1 1 23 23 CYS HB2 H 1 3.144 0.000 . 1 . . . . . . . . 5495 1 112 . 1 1 23 23 CYS HB3 H 1 2.755 0.000 . 1 . . . . . . . . 5495 1 113 . 1 1 24 24 TRP H H 1 9.403 0.000 . 1 . . . . . . . . 5495 1 114 . 1 1 24 24 TRP HA H 1 4.872 0.000 . 1 . . . . . . . . 5495 1 115 . 1 1 24 24 TRP HB2 H 1 3.406 0.000 . 1 . . . . . . . . 5495 1 116 . 1 1 24 24 TRP HB3 H 1 3.019 0.000 . 1 . . . . . . . . 5495 1 117 . 1 1 24 24 TRP HD1 H 1 7.121 0.001 . 1 . . . . . . . . 5495 1 118 . 1 1 24 24 TRP HE1 H 1 10.179 0.000 . 1 . . . . . . . . 5495 1 119 . 1 1 24 24 TRP HZ2 H 1 7.147 0.000 . 1 . . . . . . . . 5495 1 120 . 1 1 24 24 TRP HH2 H 1 7.556 0.000 . 1 . . . . . . . . 5495 1 121 . 1 1 25 25 LYS H H 1 8.086 0.000 . 1 . . . . . . . . 5495 1 122 . 1 1 25 25 LYS HA H 1 4.184 0.001 . 1 . . . . . . . . 5495 1 123 . 1 1 26 26 ARG H H 1 7.601 0.000 . 1 . . . . . . . . 5495 1 124 . 1 1 26 26 ARG HA H 1 3.985 0.001 . 1 . . . . . . . . 5495 1 125 . 1 1 26 26 ARG HE H 1 7.016 0.000 . 1 . . . . . . . . 5495 1 126 . 1 1 27 27 ARG H H 1 8.381 0.000 . 1 . . . . . . . . 5495 1 127 . 1 1 27 27 ARG HA H 1 4.345 0.001 . 1 . . . . . . . . 5495 1 128 . 1 1 27 27 ARG HB2 H 1 1.874 0.004 . 1 . . . . . . . . 5495 1 129 . 1 1 27 27 ARG HB3 H 1 1.788 0.007 . 1 . . . . . . . . 5495 1 130 . 1 1 29 29 SER H H 1 8.023 0.000 . 1 . . . . . . . . 5495 1 131 . 1 1 29 29 SER HA H 1 4.373 0.000 . 1 . . . . . . . . 5495 1 132 . 1 1 29 29 SER HB2 H 1 3.756 0.000 . 1 . . . . . . . . 5495 1 133 . 1 1 29 29 SER HB3 H 1 3.613 0.002 . 1 . . . . . . . . 5495 1 134 . 1 1 30 30 PHE H H 1 7.862 0.000 . 1 . . . . . . . . 5495 1 135 . 1 1 30 30 PHE HA H 1 4.778 0.000 . 1 . . . . . . . . 5495 1 136 . 1 1 30 30 PHE HB2 H 1 3.178 0.003 . 1 . . . . . . . . 5495 1 137 . 1 1 30 30 PHE HB3 H 1 3.049 0.001 . 1 . . . . . . . . 5495 1 138 . 1 1 30 30 PHE HZ H 1 7.293 0.000 . 1 . . . . . . . . 5495 1 139 . 1 1 31 31 GLU H H 1 8.579 0.000 . 1 . . . . . . . . 5495 1 140 . 1 1 31 31 GLU HA H 1 4.279 0.000 . 1 . . . . . . . . 5495 1 141 . 1 1 31 31 GLU HG2 H 1 1.636 0.001 . 1 . . . . . . . . 5495 1 142 . 1 1 31 31 GLU HG3 H 1 1.446 0.001 . 1 . . . . . . . . 5495 1 143 . 1 1 32 32 VAL H H 1 8.365 0.001 . 1 . . . . . . . . 5495 1 144 . 1 1 32 32 VAL HA H 1 5.053 0.000 . 1 . . . . . . . . 5495 1 145 . 1 1 32 32 VAL HB H 1 1.776 0.000 . 1 . . . . . . . . 5495 1 146 . 1 1 32 32 VAL HG11 H 1 0.893 0.000 . 1 . . . . . . . . 5495 1 147 . 1 1 32 32 VAL HG12 H 1 0.893 0.000 . 1 . . . . . . . . 5495 1 148 . 1 1 32 32 VAL HG13 H 1 0.893 0.000 . 1 . . . . . . . . 5495 1 149 . 1 1 32 32 VAL HG21 H 1 0.825 0.000 . 1 . . . . . . . . 5495 1 150 . 1 1 32 32 VAL HG22 H 1 0.825 0.000 . 1 . . . . . . . . 5495 1 151 . 1 1 32 32 VAL HG23 H 1 0.825 0.000 . 1 . . . . . . . . 5495 1 152 . 1 1 33 33 CYS H H 1 8.219 0.000 . 1 . . . . . . . . 5495 1 153 . 1 1 33 33 CYS HA H 1 5.121 0.000 . 1 . . . . . . . . 5495 1 154 . 1 1 33 33 CYS HB2 H 1 2.960 0.000 . 1 . . . . . . . . 5495 1 155 . 1 1 33 33 CYS HB3 H 1 2.537 0.000 . 1 . . . . . . . . 5495 1 156 . 1 1 34 34 VAL H H 1 9.563 0.000 . 1 . . . . . . . . 5495 1 157 . 1 1 34 34 VAL HA H 1 4.503 0.004 . 1 . . . . . . . . 5495 1 158 . 1 1 34 34 VAL HB H 1 2.159 0.005 . 1 . . . . . . . . 5495 1 159 . 1 1 34 34 VAL HG11 H 1 1.031 0.003 . 1 . . . . . . . . 5495 1 160 . 1 1 34 34 VAL HG12 H 1 1.031 0.003 . 1 . . . . . . . . 5495 1 161 . 1 1 34 34 VAL HG13 H 1 1.031 0.003 . 1 . . . . . . . . 5495 1 162 . 1 1 34 34 VAL HG21 H 1 0.831 0.003 . 1 . . . . . . . . 5495 1 163 . 1 1 34 34 VAL HG22 H 1 0.831 0.003 . 1 . . . . . . . . 5495 1 164 . 1 1 34 34 VAL HG23 H 1 0.831 0.003 . 1 . . . . . . . . 5495 1 165 . 1 1 35 35 PRO HA H 1 4.362 0.000 . 1 . . . . . . . . 5495 1 166 . 1 1 35 35 PRO HB2 H 1 2.239 0.000 . 1 . . . . . . . . 5495 1 167 . 1 1 35 35 PRO HB3 H 1 1.803 0.000 . 1 . . . . . . . . 5495 1 168 . 1 1 35 35 PRO HG2 H 1 2.093 0.000 . 1 . . . . . . . . 5495 1 169 . 1 1 35 35 PRO HG3 H 1 1.561 0.001 . 1 . . . . . . . . 5495 1 170 . 1 1 35 35 PRO HD2 H 1 3.447 0.000 . 1 . . . . . . . . 5495 1 171 . 1 1 35 35 PRO HD3 H 1 2.768 0.000 . 1 . . . . . . . . 5495 1 172 . 1 1 36 36 LYS H H 1 8.024 0.000 . 1 . . . . . . . . 5495 1 173 . 1 1 36 36 LYS HA H 1 4.141 0.000 . 1 . . . . . . . . 5495 1 174 . 1 1 36 36 LYS HB2 H 1 1.660 0.000 . 1 . . . . . . . . 5495 1 175 . 1 1 36 36 LYS HB3 H 1 1.441 0.001 . 1 . . . . . . . . 5495 1 176 . 1 1 36 36 LYS HG2 H 1 1.248 0.000 . 1 . . . . . . . . 5495 1 177 . 1 1 36 36 LYS HG3 H 1 1.162 0.000 . 1 . . . . . . . . 5495 1 178 . 1 1 37 37 THR H H 1 8.277 0.000 . 1 . . . . . . . . 5495 1 179 . 1 1 37 37 THR HA H 1 4.509 0.001 . 1 . . . . . . . . 5495 1 180 . 1 1 37 37 THR HB H 1 4.079 0.000 . 1 . . . . . . . . 5495 1 181 . 1 1 37 37 THR HG21 H 1 1.173 0.000 . 1 . . . . . . . . 5495 1 182 . 1 1 37 37 THR HG22 H 1 1.173 0.000 . 1 . . . . . . . . 5495 1 183 . 1 1 37 37 THR HG23 H 1 1.173 0.000 . 1 . . . . . . . . 5495 1 184 . 1 1 38 38 PRO HA H 1 4.389 0.001 . 1 . . . . . . . . 5495 1 185 . 1 1 38 38 PRO HD2 H 1 3.820 0.000 . 1 . . . . . . . . 5495 1 186 . 1 1 38 38 PRO HD3 H 1 3.656 0.000 . 1 . . . . . . . . 5495 1 187 . 1 1 39 39 LYS H H 1 8.523 0.000 . 1 . . . . . . . . 5495 1 188 . 1 1 39 39 LYS HA H 1 4.062 0.005 . 1 . . . . . . . . 5495 1 189 . 1 1 40 40 THR H H 1 7.772 0.000 . 1 . . . . . . . . 5495 1 190 . 1 1 40 40 THR HA H 1 4.228 0.000 . 1 . . . . . . . . 5495 1 191 . 1 1 40 40 THR HB H 1 4.167 0.000 . 1 . . . . . . . . 5495 1 192 . 1 1 40 40 THR HG21 H 1 1.140 0.000 . 1 . . . . . . . . 5495 1 193 . 1 1 40 40 THR HG22 H 1 1.140 0.000 . 1 . . . . . . . . 5495 1 194 . 1 1 40 40 THR HG23 H 1 1.140 0.000 . 1 . . . . . . . . 5495 1 stop_ save_