data_4477 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4477 _Entry.Title ; Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1998-12-22 _Entry.Accession_date 1999-12-06 _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 . _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 C. Antz . . . 4477 2 T. Bauer . . . 4477 3 H. Kalbacher . . . 4477 4 R. Frank . . . 4477 5 M. Covarrubias . . . 4477 6 H. Kalbitzer . R. . 4477 7 J. Ruppersberg . P. . 4477 8 T. Baukrowitz . . . 4477 9 B. Fakler . . . 4477 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4477 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 189 4477 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 3 . . 2008-07-11 1998-12-23 update BMRB 'Updating non-standard residue' 4477 2 . . 2008-03-24 . update BMRB . 4477 1 . . 2002-06-07 1998-12-23 original author . 4477 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4476 'SER 8 phosphorylated' 4477 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4477 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9000078 _Citation.Full_citation . _Citation.Title ; NMR structure of inactivation gates from mammalian voltage-dependent potassium channels ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full . _Citation.Journal_volume 385 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 272 _Citation.Page_last 275 _Citation.Year 1997 _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 C. Antz . . . 4477 1 2 M. Geyer . . . 4477 1 3 B. Fakler . . . 4477 1 4 M. Schott . K. . 4477 1 5 H. Guy . R. . 4477 1 6 R. Frank . . . 4477 1 7 J. Ruppersberg . P. . 4477 1 8 H. Kalbitzer . R. . 4477 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'potassium channel' 4477 1 'inactivation gate' 4477 1 phosphorylation 4477 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_potassium_channel _Assembly.Sf_category assembly _Assembly.Sf_framecode system_potassium_channel _Assembly.Entry_ID 4477 _Assembly.ID 1 _Assembly.Name 'Potassium channel' _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 'not reported' _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 4477 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 'Potassium channel' 1 $Potassium_channel . . . native . . . . . 4477 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Potassium channel' system 4477 1 'Potassium channel' abbreviation 4477 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Potassium_channel _Entity.Sf_category entity _Entity.Sf_framecode Potassium_channel _Entity.Entry_ID 4477 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Potassium channel' _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 ; MISSVCVSSYRGRKXGNKPP XKTCLKEEMA ; _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 30 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2013-11-03 loop_ _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 no PDB 1B4I . "Control Of K+ Channel Gating By Protein Phosphorylation: Str Switches Of The Inactivation Gate, Nmr, 22 Structures" . . . . . 100.00 30 100.00 100.00 2.69e-10 . . . . 4477 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Potassium channel' common 4477 1 S8S(phosphor.) variant 4477 1 'Potassium channel' abbreviation 4477 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 . MET . 4477 1 2 . ILE . 4477 1 3 . SER . 4477 1 4 . SER . 4477 1 5 . VAL . 4477 1 6 . CYS . 4477 1 7 . VAL . 4477 1 8 . SER . 4477 1 9 . SER . 4477 1 10 . TYR . 4477 1 11 . ARG . 4477 1 12 . GLY . 4477 1 13 . ARG . 4477 1 14 . LYS . 4477 1 15 . SEP . 4477 1 16 . GLY . 4477 1 17 . ASN . 4477 1 18 . LYS . 4477 1 19 . PRO . 4477 1 20 . PRO . 4477 1 21 . SEP . 4477 1 22 . LYS . 4477 1 23 . THR . 4477 1 24 . CYS . 4477 1 25 . LEU . 4477 1 26 . LYS . 4477 1 27 . GLU . 4477 1 28 . GLU . 4477 1 29 . MET . 4477 1 30 . ALA . 4477 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 . MET 1 1 4477 1 . ILE 2 2 4477 1 . SER 3 3 4477 1 . SER 4 4 4477 1 . VAL 5 5 4477 1 . CYS 6 6 4477 1 . VAL 7 7 4477 1 . SER 8 8 4477 1 . SER 9 9 4477 1 . TYR 10 10 4477 1 . ARG 11 11 4477 1 . GLY 12 12 4477 1 . ARG 13 13 4477 1 . LYS 14 14 4477 1 . SEP 15 15 4477 1 . GLY 16 16 4477 1 . ASN 17 17 4477 1 . LYS 18 18 4477 1 . PRO 19 19 4477 1 . PRO 20 20 4477 1 . SEP 21 21 4477 1 . LYS 22 22 4477 1 . THR 23 23 4477 1 . CYS 24 24 4477 1 . LEU 25 25 4477 1 . LYS 26 26 4477 1 . GLU 27 27 4477 1 . GLU 28 28 4477 1 . MET 29 29 4477 1 . ALA 30 30 4477 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 4477 _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 $Potassium_channel . 562 . . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 4477 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 4477 _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 $Potassium_channel . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4477 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_SEP _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_SEP _Chem_comp.Entry_ID 4477 _Chem_comp.ID SEP _Chem_comp.Provenance . _Chem_comp.Name PHOSPHOSERINE _Chem_comp.Type 'L-peptide linking' _Chem_comp.BMRB_code . _Chem_comp.PDB_code SEP _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code S _Chem_comp.Three_letter_code SEP _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID SER _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms PHOSPHONOSERINE _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C3 H8 N O6 P' _Chem_comp.Formula_weight 185.072 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1BX6 _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 13:28:27 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID O=P(O)(O)OCC(C(=O)O)N SMILES ACDLabs 10.04 4477 SEP N[C@@H](CO[P](O)(O)=O)C(O)=O SMILES_CANONICAL CACTVS 3.341 4477 SEP N[CH](CO[P](O)(O)=O)C(O)=O SMILES CACTVS 3.341 4477 SEP C([C@@H](C(=O)O)N)OP(=O)(O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4477 SEP C(C(C(=O)O)N)OP(=O)(O)O SMILES 'OpenEye OEToolkits' 1.5.0 4477 SEP InChI=1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 InChI InChI 1.03 4477 SEP BZQFBWGGLXLEPQ-REOHCLBHSA-N InChIKey InChI 1.03 4477 SEP stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID O-phosphono-L-serine 'SYSTEMATIC NAME' ACDLabs 10.04 4477 SEP '(2S)-2-amino-3-phosphonooxy-propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4477 SEP stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N . N . . N . . N 0 . . . . no no . . . . 12.751 . 44.134 . -4.949 . 1.855 0.421 1.751 1 . 4477 SEP CA . CA . . C . . S 0 . . . . no no . . . . 12.373 . 44.600 . -6.265 . 0.401 0.620 1.687 2 . 4477 SEP CB . CB . . C . . N 0 . . . . no no . . . . 11.077 . 45.353 . -6.305 . -0.139 0.015 0.391 3 . 4477 SEP OG . OG . . O . . N 0 . . . . no no . . . . 10.895 . 45.809 . -7.608 . 0.477 0.655 -0.727 4 . 4477 SEP C . C . . C . . N 0 . . . . no no . . . . 13.435 . 45.364 . -6.941 . -0.249 -0.053 2.867 5 . 4477 SEP O . O . . O . . N 0 . . . . no no . . . . 14.373 . 45.871 . -6.303 . 0.254 -1.038 3.354 6 . 4477 SEP OXT . OXT . . O . . N 0 . . . . no yes . . . . 13.281 . 45.410 . -8.244 . -1.389 0.439 3.377 7 . 4477 SEP P . P . . P . . N 0 . . . . no no . . . . 9.607 . 45.328 . -8.384 . -0.135 -0.027 -2.050 8 . 4477 SEP O1P . O1P . . O . . N 0 . . . . no no . . . . 9.500 . 46.086 . -9.633 . -1.601 0.172 -2.074 9 . 4477 SEP O2P . O2P . . O . . N 0 . . . . no no . . . . 9.829 . 43.907 . -8.669 . 0.520 0.649 -3.356 10 . 4477 SEP O3P . O3P . . O . . N 0 . . . . no no . . . . 8.402 . 45.541 . -7.535 . 0.191 -1.603 -2.041 11 . 4477 SEP H . H . . H . . N 0 . . . . no no . . . . 13.632 . 43.621 . -4.921 . 2.237 0.796 0.895 12 . 4477 SEP H2 . H2 . . H . . N 0 . . . . no yes . . . . 12.001 . 43.575 . -4.540 . 2.013 -0.574 1.727 13 . 4477 SEP HA . HA . . H . . N 0 . . . . no no . . . . 12.213 . 43.656 . -6.837 . 0.179 1.687 1.711 14 . 4477 SEP HB2 . HB2 . . H . . N 0 . . . . no no . . . . 10.214 . 44.753 . -5.930 . 0.082 -1.051 0.367 15 . 4477 SEP HB3 . HB3 . . H . . N 0 . . . . no no . . . . 11.026 . 46.170 . -5.548 . -1.218 0.163 0.344 16 . 4477 SEP HXT . HXT . . H . . N 0 . . . . no yes . . . . 13.966 . 45.902 . -8.680 . -1.807 0.006 4.134 17 . 4477 SEP HOP2 . HOP2 . . H . . N 0 . . . . no no . . . . 9.054 . 43.617 . -9.135 . 0.127 0.212 -4.124 18 . 4477 SEP HOP3 . HOP3 . . H . . N 0 . . . . no no . . . . 7.627 . 45.251 . -8.001 . 1.154 -1.689 -2.025 19 . 4477 SEP stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 4477 SEP 2 . SING N H no N 2 . 4477 SEP 3 . SING N H2 no N 3 . 4477 SEP 4 . SING CA CB no N 4 . 4477 SEP 5 . SING CA C no N 5 . 4477 SEP 6 . SING CA HA no N 6 . 4477 SEP 7 . SING CB OG no N 7 . 4477 SEP 8 . SING CB HB2 no N 8 . 4477 SEP 9 . SING CB HB3 no N 9 . 4477 SEP 10 . SING OG P no N 10 . 4477 SEP 11 . DOUB C O no N 11 . 4477 SEP 12 . SING C OXT no N 12 . 4477 SEP 13 . SING OXT HXT no N 13 . 4477 SEP 14 . DOUB P O1P no N 14 . 4477 SEP 15 . SING P O2P no N 15 . 4477 SEP 16 . SING P O3P no N 16 . 4477 SEP 17 . SING O2P HOP2 no N 17 . 4477 SEP 18 . SING O3P HOP3 no N 18 . 4477 SEP stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4477 _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 'Potassium channel' . . . 1 $Potassium_channel . . . . . . . . . . 4477 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 4477 _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 3.37 . n/a 4477 1 temperature 283 . K 4477 1 stop_ save_ save_sample_cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_2 _Sample_condition_list.Entry_ID 4477 _Sample_condition_list.ID 2 _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 6.8 . n/a 4477 2 temperature 283 . K 4477 2 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 4477 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer . _NMR_spectrometer.Model . _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength . save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4477 _NMR_spectrometer_list.ID 1 save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4477 _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 . . 1 $NMR_applied_experiment . . . . . . . . 1 $sample_1 . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4477 1 stop_ save_ save_NMR_applied_experiment _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_applied_experiment _NMR_spec_expt.Entry_ID 4477 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_ref _Chem_shift_reference.Entry_ID 4477 _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 . . . . . . . . . . . . . . 1 $entry_citation . . 1 $entry_citation 4477 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_chem_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4477 _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 $chem_shift_ref _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 . 4477 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 MET HA H 1 4.18 . . . . . . . . . . . 4477 1 2 . 1 1 1 1 MET HB2 H 1 2.18 . . . . . . . . . . . 4477 1 3 . 1 1 1 1 MET HB3 H 1 2.18 . . . . . . . . . . . 4477 1 4 . 1 1 1 1 MET HG2 H 1 2.59 . . . . . . . . . . . 4477 1 5 . 1 1 1 1 MET HG3 H 1 2.61 . . . . . . . . . . . 4477 1 6 . 1 1 2 2 ILE H H 1 8.74 . . . . . . . . . . . 4477 1 7 . 1 1 2 2 ILE HA H 1 4.29 . . . . . . . . . . . 4477 1 8 . 1 1 2 2 ILE HB H 1 1.88 . . . . . . . . . . . 4477 1 9 . 1 1 2 2 ILE HG21 H 1 1.23 . . . . . . . . . . . 4477 1 10 . 1 1 2 2 ILE HG22 H 1 1.23 . . . . . . . . . . . 4477 1 11 . 1 1 2 2 ILE HG23 H 1 1.23 . . . . . . . . . . . 4477 1 12 . 1 1 2 2 ILE HD11 H 1 1.52 . . . . . . . . . . . 4477 1 13 . 1 1 2 2 ILE HD12 H 1 1.52 . . . . . . . . . . . 4477 1 14 . 1 1 2 2 ILE HD13 H 1 1.52 . . . . . . . . . . . 4477 1 15 . 1 1 2 2 ILE HG12 H 1 0.89 . . . . . . . . . . . 4477 1 16 . 1 1 2 2 ILE HG13 H 1 0.96 . . . . . . . . . . . 4477 1 17 . 1 1 3 3 SER H H 1 8.64 . . . . . . . . . . . 4477 1 18 . 1 1 3 3 SER HA H 1 4.53 . . . . . . . . . . . 4477 1 19 . 1 1 3 3 SER HB2 H 1 3.88 . . . . . . . . . . . 4477 1 20 . 1 1 3 3 SER HB3 H 1 3.88 . . . . . . . . . . . 4477 1 21 . 1 1 4 4 SER H H 1 8.56 . . . . . . . . . . . 4477 1 22 . 1 1 4 4 SER HA H 1 4.51 . . . . . . . . . . . 4477 1 23 . 1 1 4 4 SER HB2 H 1 3.89 . . . . . . . . . . . 4477 1 24 . 1 1 4 4 SER HB3 H 1 3.89 . . . . . . . . . . . 4477 1 25 . 1 1 5 5 VAL H H 1 8.25 . . . . . . . . . . . 4477 1 26 . 1 1 5 5 VAL HA H 1 4.16 . . . . . . . . . . . 4477 1 27 . 1 1 5 5 VAL HB H 1 2.08 . . . . . . . . . . . 4477 1 28 . 1 1 5 5 VAL HG11 H 1 0.95 . . . . . . . . . . . 4477 1 29 . 1 1 5 5 VAL HG12 H 1 0.95 . . . . . . . . . . . 4477 1 30 . 1 1 5 5 VAL HG13 H 1 0.95 . . . . . . . . . . . 4477 1 31 . 1 1 5 5 VAL HG21 H 1 0.95 . . . . . . . . . . . 4477 1 32 . 1 1 5 5 VAL HG22 H 1 0.95 . . . . . . . . . . . 4477 1 33 . 1 1 5 5 VAL HG23 H 1 0.95 . . . . . . . . . . . 4477 1 34 . 1 1 6 6 CYS H H 1 8.58 . . . . . . . . . . . 4477 1 35 . 1 1 6 6 CYS HA H 1 4.56 . . . . . . . . . . . 4477 1 36 . 1 1 6 6 CYS HB2 H 1 2.91 . . . . . . . . . . . 4477 1 37 . 1 1 6 6 CYS HB3 H 1 2.91 . . . . . . . . . . . 4477 1 38 . 1 1 7 7 VAL H H 1 8.49 . . . . . . . . . . . 4477 1 39 . 1 1 7 7 VAL HA H 1 4.16 . . . . . . . . . . . 4477 1 40 . 1 1 7 7 VAL HB H 1 2.13 . . . . . . . . . . . 4477 1 41 . 1 1 7 7 VAL HG11 H 1 0.97 . . . . . . . . . . . 4477 1 42 . 1 1 7 7 VAL HG12 H 1 0.97 . . . . . . . . . . . 4477 1 43 . 1 1 7 7 VAL HG13 H 1 0.97 . . . . . . . . . . . 4477 1 44 . 1 1 7 7 VAL HG21 H 1 0.97 . . . . . . . . . . . 4477 1 45 . 1 1 7 7 VAL HG22 H 1 0.97 . . . . . . . . . . . 4477 1 46 . 1 1 7 7 VAL HG23 H 1 0.97 . . . . . . . . . . . 4477 1 47 . 1 1 8 8 SER H H 1 8.52 . . . . . . . . . . . 4477 1 48 . 1 1 8 8 SER HA H 1 4.49 . . . . . . . . . . . 4477 1 49 . 1 1 8 8 SER HB2 H 1 3.84 . . . . . . . . . . . 4477 1 50 . 1 1 8 8 SER HB3 H 1 3.92 . . . . . . . . . . . 4477 1 51 . 1 1 9 9 SER H H 1 8.40 . . . . . . . . . . . 4477 1 52 . 1 1 9 9 SER HA H 1 4.45 . . . . . . . . . . . 4477 1 53 . 1 1 9 9 SER HB2 H 1 3.84 . . . . . . . . . . . 4477 1 54 . 1 1 9 9 SER HB3 H 1 3.87 . . . . . . . . . . . 4477 1 55 . 1 1 10 10 TYR H H 1 8.30 . . . . . . . . . . . 4477 1 56 . 1 1 10 10 TYR HA H 1 4.55 . . . . . . . . . . . 4477 1 57 . 1 1 10 10 TYR HB2 H 1 3.03 . . . . . . . . . . . 4477 1 58 . 1 1 10 10 TYR HB3 H 1 3.03 . . . . . . . . . . . 4477 1 59 . 1 1 10 10 TYR HD1 H 1 7.13 . . . . . . . . . . . 4477 1 60 . 1 1 10 10 TYR HD2 H 1 7.13 . . . . . . . . . . . 4477 1 61 . 1 1 10 10 TYR HE1 H 1 6.83 . . . . . . . . . . . 4477 1 62 . 1 1 10 10 TYR HE2 H 1 6.82 . . . . . . . . . . . 4477 1 63 . 1 1 11 11 ARG H H 1 8.33 . . . . . . . . . . . 4477 1 64 . 1 1 11 11 ARG HA H 1 4.28 . . . . . . . . . . . 4477 1 65 . 1 1 11 11 ARG HB2 H 1 1.69 . . . . . . . . . . . 4477 1 66 . 1 1 11 11 ARG HB3 H 1 1.84 . . . . . . . . . . . 4477 1 67 . 1 1 11 11 ARG HG2 H 1 1.57 . . . . . . . . . . . 4477 1 68 . 1 1 11 11 ARG HG3 H 1 1.57 . . . . . . . . . . . 4477 1 69 . 1 1 11 11 ARG HE H 1 7.21 . . . . . . . . . . . 4477 1 70 . 1 1 11 11 ARG HH21 H 1 6.52 . . . . . . . . . . . 4477 1 71 . 1 1 11 11 ARG HH22 H 1 6.52 . . . . . . . . . . . 4477 1 72 . 1 1 11 11 ARG HD2 H 1 3.19 . . . . . . . . . . . 4477 1 73 . 1 1 11 11 ARG HD3 H 1 3.19 . . . . . . . . . . . 4477 1 74 . 1 1 11 11 ARG HH11 H 1 6.88 . . . . . . . . . . . 4477 1 75 . 1 1 11 11 ARG HH12 H 1 6.88 . . . . . . . . . . . 4477 1 76 . 1 1 12 12 GLY H H 1 7.78 . . . . . . . . . . . 4477 1 77 . 1 1 12 12 GLY HA2 H 1 3.90 . . . . . . . . . . . 4477 1 78 . 1 1 12 12 GLY HA3 H 1 3.90 . . . . . . . . . . . 4477 1 79 . 1 1 13 13 ARG H H 1 8.26 . . . . . . . . . . . 4477 1 80 . 1 1 13 13 ARG HA H 1 4.37 . . . . . . . . . . . 4477 1 81 . 1 1 13 13 ARG HB2 H 1 1.78 . . . . . . . . . . . 4477 1 82 . 1 1 13 13 ARG HB3 H 1 1.89 . . . . . . . . . . . 4477 1 83 . 1 1 13 13 ARG HG2 H 1 1.65 . . . . . . . . . . . 4477 1 84 . 1 1 13 13 ARG HG3 H 1 1.65 . . . . . . . . . . . 4477 1 85 . 1 1 13 13 ARG HD2 H 1 3.21 . . . . . . . . . . . 4477 1 86 . 1 1 13 13 ARG HD3 H 1 3.21 . . . . . . . . . . . 4477 1 87 . 1 1 13 13 ARG HH11 H 1 7.32 . . . . . . . . . . . 4477 1 88 . 1 1 13 13 ARG HH12 H 1 7.32 . . . . . . . . . . . 4477 1 89 . 1 1 13 13 ARG HH21 H 1 6.52 . . . . . . . . . . . 4477 1 90 . 1 1 13 13 ARG HH22 H 1 6.88 . . . . . . . . . . . 4477 1 91 . 1 1 14 14 LYS H H 1 8.70 . . . . . . . . . . . 4477 1 92 . 1 1 14 14 LYS HA H 1 4.36 . . . . . . . . . . . 4477 1 93 . 1 1 14 14 LYS HB2 H 1 1.81 . . . . . . . . . . . 4477 1 94 . 1 1 14 14 LYS HB3 H 1 1.88 . . . . . . . . . . . 4477 1 95 . 1 1 14 14 LYS HG2 H 1 1.46 . . . . . . . . . . . 4477 1 96 . 1 1 14 14 LYS HG3 H 1 1.46 . . . . . . . . . . . 4477 1 97 . 1 1 14 14 LYS HZ1 H 1 7.59 . . . . . . . . . . . 4477 1 98 . 1 1 14 14 LYS HZ2 H 1 7.59 . . . . . . . . . . . 4477 1 99 . 1 1 14 14 LYS HZ3 H 1 7.59 . . . . . . . . . . . 4477 1 100 . 1 1 14 14 LYS HD2 H 1 1.70 . . . . . . . . . . . 4477 1 101 . 1 1 14 14 LYS HD3 H 1 1.70 . . . . . . . . . . . 4477 1 102 . 1 1 14 14 LYS HE2 H 1 3.00 . . . . . . . . . . . 4477 1 103 . 1 1 14 14 LYS HE3 H 1 3.00 . . . . . . . . . . . 4477 1 104 . 1 1 15 15 SEP H H 1 8.63 . . . . . . . . . . . 4477 1 105 . 1 1 15 15 SEP HA H 1 4.58 . . . . . . . . . . . 4477 1 106 . 1 1 15 15 SEP HB2 H 1 4.16 . . . . . . . . . . . 4477 1 107 . 1 1 15 15 SEP HB3 H 1 4.16 . . . . . . . . . . . 4477 1 108 . 1 1 16 16 GLY H H 1 8.48 . . . . . . . . . . . 4477 1 109 . 1 1 16 16 GLY HA2 H 1 3.99 . . . . . . . . . . . 4477 1 110 . 1 1 16 16 GLY HA3 H 1 3.99 . . . . . . . . . . . 4477 1 111 . 1 1 17 17 ASN H H 1 8.39 . . . . . . . . . . . 4477 1 112 . 1 1 17 17 ASN HA H 1 4.71 . . . . . . . . . . . 4477 1 113 . 1 1 17 17 ASN HB2 H 1 2.73 . . . . . . . . . . . 4477 1 114 . 1 1 17 17 ASN HB3 H 1 2.81 . . . . . . . . . . . 4477 1 115 . 1 1 17 17 ASN HD21 H 1 7.00 . . . . . . . . . . . 4477 1 116 . 1 1 17 17 ASN HD22 H 1 7.69 . . . . . . . . . . . 4477 1 117 . 1 1 18 18 LYS H H 1 8.41 . . . . . . . . . . . 4477 1 118 . 1 1 18 18 LYS HA H 1 4.61 . . . . . . . . . . . 4477 1 119 . 1 1 18 18 LYS HB2 H 1 1.73 . . . . . . . . . . . 4477 1 120 . 1 1 18 18 LYS HB3 H 1 1.81 . . . . . . . . . . . 4477 1 121 . 1 1 18 18 LYS HG2 H 1 1.48 . . . . . . . . . . . 4477 1 122 . 1 1 18 18 LYS HG3 H 1 1.48 . . . . . . . . . . . 4477 1 123 . 1 1 18 18 LYS HZ1 H 1 7.59 . . . . . . . . . . . 4477 1 124 . 1 1 18 18 LYS HZ2 H 1 7.59 . . . . . . . . . . . 4477 1 125 . 1 1 18 18 LYS HZ3 H 1 7.59 . . . . . . . . . . . 4477 1 126 . 1 1 18 18 LYS HD2 H 1 1.70 . . . . . . . . . . . 4477 1 127 . 1 1 18 18 LYS HD3 H 1 1.70 . . . . . . . . . . . 4477 1 128 . 1 1 18 18 LYS HE2 H 1 3.01 . . . . . . . . . . . 4477 1 129 . 1 1 18 18 LYS HE3 H 1 3.01 . . . . . . . . . . . 4477 1 130 . 1 1 19 19 PRO HA H 1 4.73 . . . . . . . . . . . 4477 1 131 . 1 1 19 19 PRO HB2 H 1 2.05 . . . . . . . . . . . 4477 1 132 . 1 1 19 19 PRO HB3 H 1 2.37 . . . . . . . . . . . 4477 1 133 . 1 1 19 19 PRO HG2 H 1 1.92 . . . . . . . . . . . 4477 1 134 . 1 1 19 19 PRO HG3 H 1 1.92 . . . . . . . . . . . 4477 1 135 . 1 1 19 19 PRO HD2 H 1 3.62 . . . . . . . . . . . 4477 1 136 . 1 1 19 19 PRO HD3 H 1 3.88 . . . . . . . . . . . 4477 1 137 . 1 1 20 20 PRO HA H 1 4.47 . . . . . . . . . . . 4477 1 138 . 1 1 20 20 PRO HB2 H 1 2.07 . . . . . . . . . . . 4477 1 139 . 1 1 20 20 PRO HB3 H 1 2.36 . . . . . . . . . . . 4477 1 140 . 1 1 20 20 PRO HG2 H 1 1.97 . . . . . . . . . . . 4477 1 141 . 1 1 20 20 PRO HG3 H 1 1.97 . . . . . . . . . . . 4477 1 142 . 1 1 20 20 PRO HD2 H 1 3.67 . . . . . . . . . . . 4477 1 143 . 1 1 20 20 PRO HD3 H 1 3.84 . . . . . . . . . . . 4477 1 144 . 1 1 21 21 SEP H H 1 8.80 . . . . . . . . . . . 4477 1 145 . 1 1 21 21 SEP HA H 1 4.55 . . . . . . . . . . . 4477 1 146 . 1 1 21 21 SEP HB2 H 1 4.16 . . . . . . . . . . . 4477 1 147 . 1 1 21 21 SEP HB3 H 1 4.16 . . . . . . . . . . . 4477 1 148 . 1 1 22 22 LYS H H 1 8.46 . . . . . . . . . . . 4477 1 149 . 1 1 22 22 LYS HA H 1 4.45 . . . . . . . . . . . 4477 1 150 . 1 1 22 22 LYS HB2 H 1 1.81 . . . . . . . . . . . 4477 1 151 . 1 1 22 22 LYS HB3 H 1 1.90 . . . . . . . . . . . 4477 1 152 . 1 1 22 22 LYS HG2 H 1 1.47 . . . . . . . . . . . 4477 1 153 . 1 1 22 22 LYS HG3 H 1 1.47 . . . . . . . . . . . 4477 1 154 . 1 1 22 22 LYS HZ1 H 1 7.59 . . . . . . . . . . . 4477 1 155 . 1 1 22 22 LYS HZ2 H 1 7.59 . . . . . . . . . . . 4477 1 156 . 1 1 22 22 LYS HZ3 H 1 7.59 . . . . . . . . . . . 4477 1 157 . 1 1 22 22 LYS HD2 H 1 1.71 . . . . . . . . . . . 4477 1 158 . 1 1 22 22 LYS HD3 H 1 1.71 . . . . . . . . . . . 4477 1 159 . 1 1 22 22 LYS HE2 H 1 3.01 . . . . . . . . . . . 4477 1 160 . 1 1 22 22 LYS HE3 H 1 3.01 . . . . . . . . . . . 4477 1 161 . 1 1 23 23 THR H H 1 8.24 . . . . . . . . . . . 4477 1 162 . 1 1 23 23 THR HA H 1 4.31 . . . . . . . . . . . 4477 1 163 . 1 1 23 23 THR HB H 1 4.20 . . . . . . . . . . . 4477 1 164 . 1 1 23 23 THR HG21 H 1 1.22 . . . . . . . . . . . 4477 1 165 . 1 1 23 23 THR HG22 H 1 1.22 . . . . . . . . . . . 4477 1 166 . 1 1 23 23 THR HG23 H 1 1.22 . . . . . . . . . . . 4477 1 167 . 1 1 24 24 CYS H H 1 8.47 . . . . . . . . . . . 4477 1 168 . 1 1 24 24 CYS HA H 1 4.54 . . . . . . . . . . . 4477 1 169 . 1 1 24 24 CYS HB2 H 1 2.96 . . . . . . . . . . . 4477 1 170 . 1 1 24 24 CYS HB3 H 1 2.96 . . . . . . . . . . . 4477 1 171 . 1 1 25 25 LEU H H 1 8.44 . . . . . . . . . . . 4477 1 172 . 1 1 25 25 LEU HA H 1 4.34 . . . . . . . . . . . 4477 1 173 . 1 1 25 25 LEU HB2 H 1 1.67 . . . . . . . . . . . 4477 1 174 . 1 1 25 25 LEU HB3 H 1 1.67 . . . . . . . . . . . 4477 1 175 . 1 1 25 25 LEU HG H 1 1.61 . . . . . . . . . . . 4477 1 176 . 1 1 25 25 LEU HD11 H 1 0.89 . . . . . . . . . . . 4477 1 177 . 1 1 25 25 LEU HD12 H 1 0.89 . . . . . . . . . . . 4477 1 178 . 1 1 25 25 LEU HD13 H 1 0.89 . . . . . . . . . . . 4477 1 179 . 1 1 25 25 LEU HD21 H 1 0.95 . . . . . . . . . . . 4477 1 180 . 1 1 25 25 LEU HD22 H 1 0.95 . . . . . . . . . . . 4477 1 181 . 1 1 25 25 LEU HD23 H 1 0.95 . . . . . . . . . . . 4477 1 182 . 1 1 26 26 LYS H H 1 8.38 . . . . . . . . . . . 4477 1 183 . 1 1 26 26 LYS HA H 1 4.28 . . . . . . . . . . . 4477 1 184 . 1 1 26 26 LYS HB2 H 1 1.81 . . . . . . . . . . . 4477 1 185 . 1 1 26 26 LYS HB3 H 1 1.81 . . . . . . . . . . . 4477 1 186 . 1 1 26 26 LYS HG2 H 1 1.46 . . . . . . . . . . . 4477 1 187 . 1 1 26 26 LYS HG3 H 1 1.46 . . . . . . . . . . . 4477 1 188 . 1 1 26 26 LYS HZ1 H 1 7.59 . . . . . . . . . . . 4477 1 189 . 1 1 26 26 LYS HZ2 H 1 7.59 . . . . . . . . . . . 4477 1 190 . 1 1 26 26 LYS HZ3 H 1 7.59 . . . . . . . . . . . 4477 1 191 . 1 1 26 26 LYS HD2 H 1 1.70 . . . . . . . . . . . 4477 1 192 . 1 1 26 26 LYS HD3 H 1 1.70 . . . . . . . . . . . 4477 1 193 . 1 1 26 26 LYS HE2 H 1 3.00 . . . . . . . . . . . 4477 1 194 . 1 1 26 26 LYS HE3 H 1 3.00 . . . . . . . . . . . 4477 1 195 . 1 1 27 27 GLU H H 1 8.38 . . . . . . . . . . . 4477 1 196 . 1 1 27 27 GLU HA H 1 4.33 . . . . . . . . . . . 4477 1 197 . 1 1 27 27 GLU HB2 H 1 2.02 . . . . . . . . . . . 4477 1 198 . 1 1 27 27 GLU HB3 H 1 2.11 . . . . . . . . . . . 4477 1 199 . 1 1 27 27 GLU HG2 H 1 2.47 . . . . . . . . . . . 4477 1 200 . 1 1 27 27 GLU HG3 H 1 2.47 . . . . . . . . . . . 4477 1 201 . 1 1 28 28 GLU H H 1 8.47 . . . . . . . . . . . 4477 1 202 . 1 1 28 28 GLU HA H 1 4.43 . . . . . . . . . . . 4477 1 203 . 1 1 28 28 GLU HB2 H 1 2.03 . . . . . . . . . . . 4477 1 204 . 1 1 28 28 GLU HB3 H 1 2.14 . . . . . . . . . . . 4477 1 205 . 1 1 28 28 GLU HG2 H 1 2.47 . . . . . . . . . . . 4477 1 206 . 1 1 28 28 GLU HG3 H 1 2.47 . . . . . . . . . . . 4477 1 207 . 1 1 29 29 MET H H 1 8.46 . . . . . . . . . . . 4477 1 208 . 1 1 29 29 MET HA H 1 4.46 . . . . . . . . . . . 4477 1 209 . 1 1 29 29 MET HB2 H 1 2.05 . . . . . . . . . . . 4477 1 210 . 1 1 29 29 MET HB3 H 1 2.13 . . . . . . . . . . . 4477 1 211 . 1 1 29 29 MET HG2 H 1 2.58 . . . . . . . . . . . 4477 1 212 . 1 1 29 29 MET HG3 H 1 2.66 . . . . . . . . . . . 4477 1 213 . 1 1 30 30 ALA H H 1 8.35 . . . . . . . . . . . 4477 1 214 . 1 1 30 30 ALA HA H 1 4.29 . . . . . . . . . . . 4477 1 215 . 1 1 30 30 ALA HB1 H 1 1.43 . . . . . . . . . . . 4477 1 216 . 1 1 30 30 ALA HB2 H 1 1.43 . . . . . . . . . . . 4477 1 217 . 1 1 30 30 ALA HB3 H 1 1.43 . . . . . . . . . . . 4477 1 stop_ save_