data_15130 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15130 _Entry.Title ; CA Chemical Shift Assignments for alpha-bungarotoxin (pH6.0) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-02-09 _Entry.Accession_date 2007-02-09 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Vincenzo Venditti . . . 15130 2 Andrea Bernini . . . 15130 3 Alfonso 'De Simone' . . . 15130 4 Ottavia Spiga . . . 15130 5 Filippo Prischi . . . 15130 6 Neri Niccolai . . . 15130 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15130 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 74 15130 '1H chemical shifts' 78 15130 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2008-07-02 2007-02-09 update BMRB 'complete entry citation' 15130 1 . . 2007-03-06 2007-02-09 original author 'original release' 15130 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 15130 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17336923 _Citation.Full_citation . _Citation.Title 'MMD and NMR studies of alpha-bungarotoxin surface accessibility' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. Biophys. Res. Commun.' _Citation.Journal_name_full . _Citation.Journal_volume 356 _Citation.Journal_issue 1 _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 114 _Citation.Page_last 117 _Citation.Year 2007 _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 Vincenzo Venditti . . . 15130 1 2 Andrea Bernini . . . 15130 1 3 Alfonso 'De Simone' . . . 15130 1 4 Ottavia Spiga . . . 15130 1 5 Filippo Prischi . . . 15130 1 6 Neri Niccolai . . . 15130 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15130 _Assembly.ID 1 _Assembly.Name alpha-BTX _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 alpha-BTX 1 $alpha-BTX A . yes native no no . . . 15130 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 alpha-BTX 1 CYS 3 3 SG . 1 alpha-BTX 1 CYS 23 23 SG . . 3 3 SG . . 23 23 SG 15130 1 2 disulfide single . 1 alpha-BTX 1 CYS 16 16 SG . 1 alpha-BTX 1 CYS 44 44 SG . . 16 16 SG . . 44 44 SG 15130 1 3 disulfide single . 1 alpha-BTX 1 CYS 29 29 SG . 1 alpha-BTX 1 CYS 33 33 SG . . 29 29 SG . . 33 33 SG 15130 1 4 disulfide single . 1 alpha-BTX 1 CYS 48 48 SG . 1 alpha-BTX 1 CYS 59 59 SG . . 48 48 SG . . 59 59 SG 15130 1 5 disulfide single . 1 alpha-BTX 1 CYS 60 60 SG . 1 alpha-BTX 1 CYS 65 65 SG . . 60 60 SG . . 65 65 SG 15130 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_alpha-BTX _Entity.Sf_category entity _Entity.Sf_framecode alpha-BTX _Entity.Entry_ID 15130 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name alpha-BTX _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 ; IVCHTTATSPISAVTCPPGE NLCYRKMWCDAFCSSRGKVV ELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 74 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _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 2015-11-26 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 4195 . alpha-Bungarotoxin . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 2 no PDB 1ABT . "Nmr Solution Structure Of An Alpha-Bungarotoxin(Slash) Nicotinic Receptor Peptide Complex" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 3 no PDB 1BXP . "Solution Nmr Structure Of The Complex Of Alpha-Bungarotoxin With A Library Derived Peptide, 20 Structures" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 4 no PDB 1HAA . "A Beta-Hairpin Structure In A 13-Mer Peptide That Binds A-Bungarotoxin With High Affinity And Neutralizes Its Toxicity" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 5 no PDB 1HAJ . "A Beta-hairpin Structure In A 13-mer Peptide That Binds A-bungarotoxin With High Affinity And Neutralizes Its Toxicity" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 6 no PDB 1HC9 . "A-Bungarotoxin Complexed With High Affinity Peptide" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 7 no PDB 1HOY . "Nmr Structure Of The Complex Between A-Bungarotoxin And A Mimotope Of The Nicotinic Acetilcholine Receptor" . . . . . 98.65 74 100.00 100.00 1.45e-44 . . . . 15130 1 8 no PDB 1IDG . "The Nmr Solution Structure Of The Complex Formed Between Alpha-Bungarotoxin And An 18mer Cognate Peptide" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 9 no PDB 1IDH . "The Nmr Solution Structure Of The Complex Formed Between Alpha-Bungarotoxin And An 18mer Cognate Peptide" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 10 no PDB 1IDI . "The Nmr Solution Structure Of Alpha-Bungarotoxin" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 11 no PDB 1IDL . "The Nmr Solution Structure Of Alpha-Bungarotoxin" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 12 no PDB 1IK8 . "Nmr Structure Of Alpha-Bungarotoxin" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 13 no PDB 1IKC . "Nmr Structure Of Alpha-Bungarotoxin" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 14 no PDB 1JBD . "Nmr Structure Of The Complex Between Alpha-Bungarotoxin And A Mimotope Of The Nicotinic Acetilcholine Receptor" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 15 no PDB 1KC4 . "Nmr Structural Analysis Of The Complex Formed Between Alpha- Bungarotoxin And The Principal Alpha-Neurotoxin Binding Sequence O" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 16 no PDB 1KFH . "Solution Structure Of Alpha-Bungarotoxin By Nmr Spectroscopy" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 17 no PDB 1KL8 . "Nmr Structural Analysis Of The Complex Formed Between Alpha- Bungarotoxin And The Principal Alpha-Neurotoxin Binding Sequence O" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 18 no PDB 1L4W . "Nmr Structure Of An Achr-Peptide (Torpedo Californica, Alpha-Subunit Residues 182-202) In Complex With Alpha- Bungarotoxin" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 19 no PDB 1LJZ . "Nmr Structure Of An Achr-peptide (torpedo Californica, Alpha-subunit Residues 182-202) In Complex With Alpha-bungarotoxin" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 20 no PDB 1RGJ . "Nmr Structure Of The Complex Between Alpha-Bungarotoxin And Mimotope Of The Nicotinic Acetilcholine Receptor With Enhanced Acti" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 21 no PDB 2BTX . "Solution Nmr Structure Of The Complex Of Alpha-Bungarotoxin With A Library Derived Peptide, Nmr, Minimized Average Structure" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 22 no PDB 2QC1 . "Crystal Structure Of The Extracellular Domain Of The Nicotinic Acetylcholine Receptor 1 Subunit Bound To Alpha-Bungarotoxin At " . . . . . 100.00 74 98.65 98.65 9.07e-45 . . . . 15130 1 23 no PDB 4HQP . "Alpha7 Nicotinic Receptor Chimera And Its Complex With Alpha Bungarotoxin" . . . . . 98.65 73 98.63 98.63 6.90e-44 . . . . 15130 1 24 no PDB 4UY2 . "Crystal Structure Of The Complex Of The Extracellular Domain Of Human Alpha9 Nachr With Alpha-bungarotoxin." . . . . . 100.00 74 98.65 98.65 9.07e-45 . . . . 15130 1 25 no EMBL CAA63045 . "alpha-bungarotoxin [Bungarus multicinctus]" . . . . . 100.00 74 100.00 100.00 2.11e-45 . . . . 15130 1 26 no EMBL CAB50692 . "snake venom [Bungarus multicinctus]" . . . . . 100.00 95 98.65 98.65 1.70e-45 . . . . 15130 1 27 no EMBL CAB51841 . "alpha-bungarotoxin (V31) [Bungarus multicinctus]" . . . . . 100.00 95 98.65 98.65 1.65e-45 . . . . 15130 1 28 no EMBL CAB51842 . "alpha-bungarotoxin (A31) [Bungarus multicinctus]" . . . . . 100.00 95 100.00 100.00 5.26e-46 . . . . 15130 1 29 no EMBL CAB51843 . "alpha-bungarotoxin (V31) [Bungarus multicinctus]" . . . . . 100.00 95 98.65 98.65 1.65e-45 . . . . 15130 1 30 no GB AAC83981 . "alpha-bungarotoxin precursor [Bungarus multicinctus]" . . . . . 100.00 95 100.00 100.00 5.26e-46 . . . . 15130 1 31 no GB AAC83982 . "alpha-bungarotoxin [Bungarus multicinctus]" . . . . . 100.00 74 98.65 100.00 6.33e-45 . . . . 15130 1 32 no GB AAC83983 . "alpha-bungarotoxin isoform R2 [Bungarus multicinctus]" . . . . . 100.00 74 98.65 100.00 6.33e-45 . . . . 15130 1 33 no GB AAC83984 . "alpha-bungarotoxin isoform R3 [Bungarus multicinctus]" . . . . . 100.00 74 98.65 100.00 6.33e-45 . . . . 15130 1 34 no GB AAC83985 . "alpha-bungarotoxin isoform R4 [Bungarus multicinctus]" . . . . . 100.00 74 97.30 100.00 3.53e-44 . . . . 15130 1 35 no SP P60615 . "RecName: Full=Alpha-bungarotoxin isoform A31; Short=Alpha-BTX A31; Short=Alpha-Bgt(A31); Short=BGTX A31; AltName: Full=Long neu" . . . . . 100.00 95 100.00 100.00 5.26e-46 . . . . 15130 1 36 no SP P60616 . "RecName: Full=Alpha-bungarotoxin isoform V31; Short=Alpha-BTX V31; Short=Alpha-Bgt(V31); Short=BGTX V31; AltName: Full=Long neu" . . . . . 100.00 95 98.65 98.65 1.65e-45 . . . . 15130 1 37 no SP Q7T3J2 . "RecName: Full=Alpha-elapitoxin-Bm2a; Short=Alpha-EPTX-Bm2a; AltName: Full=Alpha-bungarotoxin, isoform A31; Flags: Precursor" . . . . . 100.00 95 100.00 100.00 5.26e-46 . . . . 15130 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 . ILE . 15130 1 2 . VAL . 15130 1 3 . CYS . 15130 1 4 . HIS . 15130 1 5 . THR . 15130 1 6 . THR . 15130 1 7 . ALA . 15130 1 8 . THR . 15130 1 9 . SER . 15130 1 10 . PRO . 15130 1 11 . ILE . 15130 1 12 . SER . 15130 1 13 . ALA . 15130 1 14 . VAL . 15130 1 15 . THR . 15130 1 16 . CYS . 15130 1 17 . PRO . 15130 1 18 . PRO . 15130 1 19 . GLY . 15130 1 20 . GLU . 15130 1 21 . ASN . 15130 1 22 . LEU . 15130 1 23 . CYS . 15130 1 24 . TYR . 15130 1 25 . ARG . 15130 1 26 . LYS . 15130 1 27 . MET . 15130 1 28 . TRP . 15130 1 29 . CYS . 15130 1 30 . ASP . 15130 1 31 . ALA . 15130 1 32 . PHE . 15130 1 33 . CYS . 15130 1 34 . SER . 15130 1 35 . SER . 15130 1 36 . ARG . 15130 1 37 . GLY . 15130 1 38 . LYS . 15130 1 39 . VAL . 15130 1 40 . VAL . 15130 1 41 . GLU . 15130 1 42 . LEU . 15130 1 43 . GLY . 15130 1 44 . CYS . 15130 1 45 . ALA . 15130 1 46 . ALA . 15130 1 47 . THR . 15130 1 48 . CYS . 15130 1 49 . PRO . 15130 1 50 . SER . 15130 1 51 . LYS . 15130 1 52 . LYS . 15130 1 53 . PRO . 15130 1 54 . TYR . 15130 1 55 . GLU . 15130 1 56 . GLU . 15130 1 57 . VAL . 15130 1 58 . THR . 15130 1 59 . CYS . 15130 1 60 . CYS . 15130 1 61 . SER . 15130 1 62 . THR . 15130 1 63 . ASP . 15130 1 64 . LYS . 15130 1 65 . CYS . 15130 1 66 . ASN . 15130 1 67 . PRO . 15130 1 68 . HIS . 15130 1 69 . PRO . 15130 1 70 . LYS . 15130 1 71 . GLN . 15130 1 72 . ARG . 15130 1 73 . PRO . 15130 1 74 . GLY . 15130 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 . ILE 1 1 15130 1 . VAL 2 2 15130 1 . CYS 3 3 15130 1 . HIS 4 4 15130 1 . THR 5 5 15130 1 . THR 6 6 15130 1 . ALA 7 7 15130 1 . THR 8 8 15130 1 . SER 9 9 15130 1 . PRO 10 10 15130 1 . ILE 11 11 15130 1 . SER 12 12 15130 1 . ALA 13 13 15130 1 . VAL 14 14 15130 1 . THR 15 15 15130 1 . CYS 16 16 15130 1 . PRO 17 17 15130 1 . PRO 18 18 15130 1 . GLY 19 19 15130 1 . GLU 20 20 15130 1 . ASN 21 21 15130 1 . LEU 22 22 15130 1 . CYS 23 23 15130 1 . TYR 24 24 15130 1 . ARG 25 25 15130 1 . LYS 26 26 15130 1 . MET 27 27 15130 1 . TRP 28 28 15130 1 . CYS 29 29 15130 1 . ASP 30 30 15130 1 . ALA 31 31 15130 1 . PHE 32 32 15130 1 . CYS 33 33 15130 1 . SER 34 34 15130 1 . SER 35 35 15130 1 . ARG 36 36 15130 1 . GLY 37 37 15130 1 . LYS 38 38 15130 1 . VAL 39 39 15130 1 . VAL 40 40 15130 1 . GLU 41 41 15130 1 . LEU 42 42 15130 1 . GLY 43 43 15130 1 . CYS 44 44 15130 1 . ALA 45 45 15130 1 . ALA 46 46 15130 1 . THR 47 47 15130 1 . CYS 48 48 15130 1 . PRO 49 49 15130 1 . SER 50 50 15130 1 . LYS 51 51 15130 1 . LYS 52 52 15130 1 . PRO 53 53 15130 1 . TYR 54 54 15130 1 . GLU 55 55 15130 1 . GLU 56 56 15130 1 . VAL 57 57 15130 1 . THR 58 58 15130 1 . CYS 59 59 15130 1 . CYS 60 60 15130 1 . SER 61 61 15130 1 . THR 62 62 15130 1 . ASP 63 63 15130 1 . LYS 64 64 15130 1 . CYS 65 65 15130 1 . ASN 66 66 15130 1 . PRO 67 67 15130 1 . HIS 68 68 15130 1 . PRO 69 69 15130 1 . LYS 70 70 15130 1 . GLN 71 71 15130 1 . ARG 72 72 15130 1 . PRO 73 73 15130 1 . GLY 74 74 15130 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 15130 _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 $alpha-BTX . . organism . 'Bungarus multicinctus' . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15130 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 15130 _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 $alpha-BTX . 'obtained from a vendor' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15130 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15130 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% 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 alpha-BTX 'natural abundance' . . 1 $alpha-BTX . . 1.0 . . mM . . . . 15130 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 15130 _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 6.0 . pH 15130 1 pressure 1 . atm 15130 1 temperature 303 . K 15130 1 stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 15130 _Software.ID 1 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 15130 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15130 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 15130 _Software.ID 2 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 15130 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 15130 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 15130 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 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 15130 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 600 . . . 15130 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 15130 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-13C HSQC-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15130 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 15130 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 TSP 'methyl carbons' . . . . ppm 0 internal direct 1 . . . . . . . . . 15130 1 H 1 TSP 'methyl protons' . . . . ppm 0 internal direct 1 . . . . . . . . . 15130 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 15130 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-13C HSQC-TOCSY' . . . 15130 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 ILE HA H 1 4.196 0.02 . 1 . . . . 1 ILE HA . 15130 1 2 . 1 1 1 1 ILE CA C 13 65.733 0.02 . 1 . . . . 1 ILE CA . 15130 1 3 . 1 1 2 2 VAL HA H 1 4.997 0.02 . 1 . . . . 2 VAL HA . 15130 1 4 . 1 1 2 2 VAL CA C 13 60.347 0.02 . 1 . . . . 2 VAL CA . 15130 1 5 . 1 1 3 3 CYS HA H 1 5.070 0.02 . 1 . . . . 3 CYS HA . 15130 1 6 . 1 1 3 3 CYS CA C 13 51.712 0.02 . 1 . . . . 3 CYS CA . 15130 1 7 . 1 1 4 4 HIS HA H 1 5.176 0.02 . 1 . . . . 4 HIS HA . 15130 1 8 . 1 1 4 4 HIS CA C 13 52.996 0.02 . 1 . . . . 4 HIS CA . 15130 1 9 . 1 1 5 5 THR HA H 1 5.193 0.02 . 1 . . . . 5 THR HA . 15130 1 10 . 1 1 5 5 THR CA C 13 58.268 0.02 . 1 . . . . 5 THR CA . 15130 1 11 . 1 1 6 6 THR HA H 1 4.417 0.02 . 1 . . . . 6 THR HA . 15130 1 12 . 1 1 6 6 THR CA C 13 56.186 0.02 . 1 . . . . 6 THR CA . 15130 1 13 . 1 1 7 7 ALA HA H 1 4.339 0.02 . 1 . . . . 7 ALA HA . 15130 1 14 . 1 1 7 7 ALA CA C 13 54.134 0.02 . 1 . . . . 7 ALA CA . 15130 1 15 . 1 1 8 8 THR HA H 1 4.513 0.02 . 1 . . . . 8 THR HA . 15130 1 16 . 1 1 8 8 THR CA C 13 58.982 0.02 . 1 . . . . 8 THR CA . 15130 1 17 . 1 1 9 9 SER HA H 1 4.607 0.02 . 1 . . . . 9 SER HA . 15130 1 18 . 1 1 9 9 SER CA C 13 54.371 0.02 . 1 . . . . 9 SER CA . 15130 1 19 . 1 1 10 10 PRO HA H 1 4.884 0.02 . 1 . . . . 10 PRO HA . 15130 1 20 . 1 1 10 10 PRO CA C 13 63.282 0.02 . 1 . . . . 10 PRO CA . 15130 1 21 . 1 1 11 11 ILE HA H 1 4.158 0.02 . 1 . . . . 11 ILE HA . 15130 1 22 . 1 1 11 11 ILE CA C 13 63.760 0.02 . 1 . . . . 11 ILE CA . 15130 1 23 . 1 1 12 12 SER HA H 1 4.929 0.02 . 1 . . . . 12 SER HA . 15130 1 24 . 1 1 12 12 SER CA C 13 57.139 0.02 . 1 . . . . 12 SER CA . 15130 1 25 . 1 1 13 13 ALA HA H 1 5.189 0.02 . 1 . . . . 13 ALA HA . 15130 1 26 . 1 1 13 13 ALA CA C 13 50.516 0.02 . 1 . . . . 13 ALA CA . 15130 1 27 . 1 1 14 14 VAL HA H 1 4.677 0.02 . 1 . . . . 14 VAL HA . 15130 1 28 . 1 1 14 14 VAL CA C 13 58.810 0.02 . 1 . . . . 14 VAL CA . 15130 1 29 . 1 1 15 15 THR HA H 1 4.462 0.02 . 1 . . . . 15 THR HA . 15130 1 30 . 1 1 15 15 THR CA C 13 63.526 0.02 . 1 . . . . 15 THR CA . 15130 1 31 . 1 1 16 16 CYS HA H 1 4.861 0.02 . 1 . . . . 16 CYS HA . 15130 1 32 . 1 1 16 16 CYS CA C 13 53.344 0.02 . 1 . . . . 16 CYS CA . 15130 1 33 . 1 1 17 17 PRO HA H 1 4.726 0.02 . 1 . . . . 17 PRO HA . 15130 1 34 . 1 1 17 17 PRO CA C 13 62.220 0.02 . 1 . . . . 17 PRO CA . 15130 1 35 . 1 1 18 18 PRO HA H 1 4.296 0.02 . 1 . . . . 18 PRO HA . 15130 1 36 . 1 1 18 18 PRO CA C 13 64.235 0.02 . 1 . . . . 18 PRO CA . 15130 1 37 . 1 1 19 19 GLY HA2 H 1 3.662 0.02 . 2 . . . . 19 GLY HA2 . 15130 1 38 . 1 1 19 19 GLY HA3 H 1 4.287 0.02 . 2 . . . . 19 GLY HA3 . 15130 1 39 . 1 1 19 19 GLY CA C 13 44.960 0.02 . 1 . . . . 19 GLY CA . 15130 1 40 . 1 1 20 20 GLU HA H 1 4.254 0.02 . 1 . . . . 20 GLU HA . 15130 1 41 . 1 1 20 20 GLU CA C 13 44.963 0.02 . 1 . . . . 20 GLU CA . 15130 1 42 . 1 1 21 21 ASN HA H 1 4.985 0.02 . 1 . . . . 21 ASN HA . 15130 1 43 . 1 1 21 21 ASN CA C 13 53.123 0.02 . 1 . . . . 21 ASN CA . 15130 1 44 . 1 1 22 22 LEU HA H 1 5.013 0.02 . 1 . . . . 22 LEU HA . 15130 1 45 . 1 1 22 22 LEU CA C 13 54.746 0.02 . 1 . . . . 22 LEU CA . 15130 1 46 . 1 1 23 23 CYS HA H 1 5.979 0.02 . 1 . . . . 23 CYS HA . 15130 1 47 . 1 1 23 23 CYS CA C 13 51.932 0.02 . 1 . . . . 23 CYS CA . 15130 1 48 . 1 1 24 24 TYR HA H 1 6.005 0.02 . 1 . . . . 24 TYR HA . 15130 1 49 . 1 1 24 24 TYR CA C 13 56.021 0.02 . 1 . . . . 24 TYR CA . 15130 1 50 . 1 1 25 25 ARG HA H 1 5.244 0.02 . 1 . . . . 25 ARG HA . 15130 1 51 . 1 1 25 25 ARG CA C 13 54.938 0.02 . 1 . . . . 25 ARG CA . 15130 1 52 . 1 1 26 26 LYS HA H 1 5.864 0.02 . 1 . . . . 26 LYS HA . 15130 1 53 . 1 1 26 26 LYS CA C 13 54.699 0.02 . 1 . . . . 26 LYS CA . 15130 1 54 . 1 1 27 27 MET HA H 1 6.119 0.02 . 1 . . . . 27 MET HA . 15130 1 55 . 1 1 27 27 MET CA C 13 54.465 0.02 . 1 . . . . 27 MET CA . 15130 1 56 . 1 1 28 28 TRP HA H 1 5.257 0.02 . 1 . . . . 28 TRP HA . 15130 1 57 . 1 1 28 28 TRP CA C 13 57.448 0.02 . 1 . . . . 28 TRP CA . 15130 1 58 . 1 1 29 29 CYS HA H 1 5.120 0.02 . 1 . . . . 29 CYS HA . 15130 1 59 . 1 1 29 29 CYS CA C 13 52.457 0.02 . 1 . . . . 29 CYS CA . 15130 1 60 . 1 1 30 30 ASP HA H 1 4.895 0.02 . 1 . . . . 30 ASP HA . 15130 1 61 . 1 1 30 30 ASP CA C 13 52.627 0.02 . 1 . . . . 30 ASP CA . 15130 1 62 . 1 1 31 31 ALA HA H 1 4.055 0.02 . 1 . . . . 31 ALA HA . 15130 1 63 . 1 1 31 31 ALA CA C 13 54.461 0.02 . 1 . . . . 31 ALA CA . 15130 1 64 . 1 1 32 32 PHE HA H 1 4.852 0.02 . 1 . . . . 32 PHE HA . 15130 1 65 . 1 1 32 32 PHE CA C 13 57.203 0.02 . 1 . . . . 32 PHE CA . 15130 1 66 . 1 1 33 33 CYS HA H 1 4.132 0.02 . 1 . . . . 33 CYS HA . 15130 1 67 . 1 1 33 33 CYS CA C 13 56.214 0.02 . 1 . . . . 33 CYS CA . 15130 1 68 . 1 1 34 34 SER HA H 1 4.288 0.02 . 1 . . . . 34 SER HA . 15130 1 69 . 1 1 34 34 SER CA C 13 60.992 0.02 . 1 . . . . 34 SER CA . 15130 1 70 . 1 1 35 35 SER HA H 1 4.690 0.02 . 1 . . . . 35 SER HA . 15130 1 71 . 1 1 35 35 SER CA C 13 58.997 0.02 . 1 . . . . 35 SER CA . 15130 1 72 . 1 1 36 36 ARG HA H 1 4.590 0.02 . 1 . . . . 36 ARG HA . 15130 1 73 . 1 1 36 36 ARG CA C 13 56.498 0.02 . 1 . . . . 36 ARG CA . 15130 1 74 . 1 1 37 37 GLY HA2 H 1 3.936 0.02 . 2 . . . . 37 GLY HA2 . 15130 1 75 . 1 1 37 37 GLY HA3 H 1 4.363 0.02 . 2 . . . . 37 GLY HA3 . 15130 1 76 . 1 1 37 37 GLY CA C 13 44.050 0.02 . 1 . . . . 37 GLY CA . 15130 1 77 . 1 1 38 38 LYS HA H 1 4.181 0.02 . 1 . . . . 38 LYS HA . 15130 1 78 . 1 1 38 38 LYS CA C 13 59.855 0.02 . 1 . . . . 38 LYS CA . 15130 1 79 . 1 1 39 39 VAL HA H 1 3.587 0.02 . 1 . . . . 39 VAL HA . 15130 1 80 . 1 1 39 39 VAL CA C 13 62.992 0.02 . 1 . . . . 39 VAL CA . 15130 1 81 . 1 1 40 40 VAL HA H 1 4.704 0.02 . 1 . . . . 40 VAL HA . 15130 1 82 . 1 1 40 40 VAL CA C 13 60.744 0.02 . 1 . . . . 40 VAL CA . 15130 1 83 . 1 1 41 41 GLU HA H 1 5.022 0.02 . 1 . . . . 41 GLU HA . 15130 1 84 . 1 1 41 41 GLU CA C 13 53.913 0.02 . 1 . . . . 41 GLU CA . 15130 1 85 . 1 1 42 42 LEU HA H 1 5.065 0.02 . 1 . . . . 42 LEU HA . 15130 1 86 . 1 1 42 42 LEU CA C 13 57.752 0.02 . 1 . . . . 42 LEU CA . 15130 1 87 . 1 1 43 43 GLY HA2 H 1 4.060 0.02 . 2 . . . . 43 GLY HA2 . 15130 1 88 . 1 1 43 43 GLY HA3 H 1 4.310 0.02 . 2 . . . . 43 GLY HA3 . 15130 1 89 . 1 1 43 43 GLY CA C 13 46.883 0.02 . 1 . . . . 43 GLY CA . 15130 1 90 . 1 1 44 44 CYS HA H 1 5.624 0.02 . 1 . . . . 44 CYS HA . 15130 1 91 . 1 1 44 44 CYS CA C 13 56.257 0.02 . 1 . . . . 44 CYS CA . 15130 1 92 . 1 1 45 45 ALA HA H 1 4.565 0.02 . 1 . . . . 45 ALA HA . 15130 1 93 . 1 1 45 45 ALA CA C 13 52.292 0.02 . 1 . . . . 45 ALA CA . 15130 1 94 . 1 1 46 46 ALA HA H 1 4.864 0.02 . 1 . . . . 46 ALA HA . 15130 1 95 . 1 1 46 46 ALA CA C 13 57.282 0.02 . 1 . . . . 46 ALA CA . 15130 1 96 . 1 1 47 47 THR HA H 1 4.330 0.02 . 1 . . . . 47 THR HA . 15130 1 97 . 1 1 47 47 THR CA C 13 59.579 0.02 . 1 . . . . 47 THR CA . 15130 1 98 . 1 1 48 48 CYS HA H 1 4.552 0.02 . 1 . . . . 48 CYS HA . 15130 1 99 . 1 1 48 48 CYS CA C 13 53.416 0.02 . 1 . . . . 48 CYS CA . 15130 1 100 . 1 1 49 49 PRO HA H 1 4.092 0.02 . 1 . . . . 49 PRO HA . 15130 1 101 . 1 1 49 49 PRO CA C 13 58.124 0.02 . 1 . . . . 49 PRO CA . 15130 1 102 . 1 1 50 50 SER HA H 1 4.204 0.02 . 1 . . . . 50 SER HA . 15130 1 103 . 1 1 50 50 SER CA C 13 58.239 0.02 . 1 . . . . 50 SER CA . 15130 1 104 . 1 1 51 51 LYS HA H 1 4.417 0.02 . 1 . . . . 51 LYS HA . 15130 1 105 . 1 1 51 51 LYS CA C 13 55.821 0.02 . 1 . . . . 51 LYS CA . 15130 1 106 . 1 1 52 52 LYS HA H 1 4.500 0.02 . 1 . . . . 52 LYS HA . 15130 1 107 . 1 1 52 52 LYS CA C 13 54.592 0.02 . 1 . . . . 52 LYS CA . 15130 1 108 . 1 1 53 53 PRO HA H 1 4.204 0.02 . 1 . . . . 53 PRO HA . 15130 1 109 . 1 1 53 53 PRO CA C 13 58.239 0.02 . 1 . . . . 53 PRO CA . 15130 1 110 . 1 1 54 54 TYR HA H 1 4.671 0.02 . 1 . . . . 54 TYR HA . 15130 1 111 . 1 1 54 54 TYR CA C 13 56.680 0.02 . 1 . . . . 54 TYR CA . 15130 1 112 . 1 1 55 55 GLU HA H 1 5.090 0.02 . 1 . . . . 55 GLU HA . 15130 1 113 . 1 1 55 55 GLU CA C 13 55.120 0.02 . 1 . . . . 55 GLU CA . 15130 1 114 . 1 1 56 56 GLU HA H 1 4.776 0.02 . 1 . . . . 56 GLU HA . 15130 1 115 . 1 1 56 56 GLU CA C 13 55.392 0.02 . 1 . . . . 56 GLU CA . 15130 1 116 . 1 1 57 57 VAL HA H 1 5.375 0.02 . 1 . . . . 57 VAL HA . 15130 1 117 . 1 1 57 57 VAL CA C 13 61.358 0.02 . 1 . . . . 57 VAL CA . 15130 1 118 . 1 1 58 58 THR HA H 1 4.767 0.02 . 1 . . . . 58 THR HA . 15130 1 119 . 1 1 58 58 THR CA C 13 61.259 0.02 . 1 . . . . 58 THR CA . 15130 1 120 . 1 1 59 59 CYS HA H 1 5.650 0.02 . 1 . . . . 59 CYS HA . 15130 1 121 . 1 1 59 59 CYS CA C 13 54.680 0.02 . 1 . . . . 59 CYS CA . 15130 1 122 . 1 1 60 60 CYS HA H 1 5.136 0.02 . 1 . . . . 60 CYS HA . 15130 1 123 . 1 1 60 60 CYS CA C 13 54.949 0.02 . 1 . . . . 60 CYS CA . 15130 1 124 . 1 1 61 61 SER HA H 1 4.958 0.02 . 1 . . . . 61 SER HA . 15130 1 125 . 1 1 61 61 SER CA C 13 58.136 0.02 . 1 . . . . 61 SER CA . 15130 1 126 . 1 1 62 62 THR HA H 1 4.772 0.02 . 1 . . . . 62 THR HA . 15130 1 127 . 1 1 62 62 THR CA C 13 60.105 0.02 . 1 . . . . 62 THR CA . 15130 1 128 . 1 1 63 63 ASP HA H 1 4.819 0.02 . 1 . . . . 63 ASP HA . 15130 1 129 . 1 1 63 63 ASP CA C 13 55.876 0.02 . 1 . . . . 63 ASP CA . 15130 1 130 . 1 1 64 64 LYS HA H 1 3.202 0.02 . 1 . . . . 64 LYS HA . 15130 1 131 . 1 1 64 64 LYS CA C 13 58.594 0.02 . 1 . . . . 64 LYS CA . 15130 1 132 . 1 1 65 65 CYS HA H 1 4.564 0.02 . 1 . . . . 65 CYS HA . 15130 1 133 . 1 1 65 65 CYS CA C 13 57.393 0.02 . 1 . . . . 65 CYS CA . 15130 1 134 . 1 1 66 66 ASN HA H 1 4.969 0.02 . 1 . . . . 66 ASN HA . 15130 1 135 . 1 1 66 66 ASN CA C 13 52.078 0.02 . 1 . . . . 66 ASN CA . 15130 1 136 . 1 1 67 67 PRO HA H 1 3.674 0.02 . 1 . . . . 67 PRO HA . 15130 1 137 . 1 1 67 67 PRO CA C 13 64.534 0.02 . 1 . . . . 67 PRO CA . 15130 1 138 . 1 1 68 68 HIS HA H 1 4.103 0.02 . 1 . . . . 68 HIS HA . 15130 1 139 . 1 1 68 68 HIS CA C 13 56.134 0.02 . 1 . . . . 68 HIS CA . 15130 1 140 . 1 1 69 69 PRO HA H 1 4.338 0.02 . 1 . . . . 69 PRO HA . 15130 1 141 . 1 1 69 69 PRO CA C 13 64.508 0.02 . 1 . . . . 69 PRO CA . 15130 1 142 . 1 1 70 70 LYS HA H 1 4.410 0.02 . 1 . . . . 70 LYS HA . 15130 1 143 . 1 1 70 70 LYS CA C 13 56.186 0.02 . 1 . . . . 70 LYS CA . 15130 1 144 . 1 1 71 71 GLN HA H 1 4.258 0.02 . 1 . . . . 71 GLN HA . 15130 1 145 . 1 1 71 71 GLN CA C 13 56.031 0.02 . 1 . . . . 71 GLN CA . 15130 1 146 . 1 1 72 72 ARG HA H 1 4.623 0.02 . 1 . . . . 72 ARG HA . 15130 1 147 . 1 1 72 72 ARG CA C 13 54.112 0.02 . 1 . . . . 72 ARG CA . 15130 1 148 . 1 1 73 73 PRO HA H 1 4.458 0.02 . 1 . . . . 73 PRO HA . 15130 1 149 . 1 1 73 73 PRO CA C 13 63.526 0.02 . 1 . . . . 73 PRO CA . 15130 1 150 . 1 1 74 74 GLY HA2 H 1 3.770 0.02 . 2 . . . . 74 GLY HA2 . 15130 1 151 . 1 1 74 74 GLY HA3 H 1 3.772 0.02 . 2 . . . . 74 GLY HA3 . 15130 1 152 . 1 1 74 74 GLY CA C 13 46.185 0.02 . 1 . . . . 74 GLY CA . 15130 1 stop_ save_