data_18287 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18287 _Entry.Title ; Backbone and sidechain 1H chemical shifts for PAP248-286 (SEVI) in solution at pH 6 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-02-21 _Entry.Accession_date 2012-02-21 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _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 Nataliya Popovych . . . 18287 2 Jeffrey Brender . R. . 18287 3 Ronald Soong . . . 18287 4 Subramanian Vivekanandan . . . 18287 5 Kevin Hartman . . . 18287 6 Venkatesha Basrur . . . 18287 7 Peter MacDonald . M. . 18287 8 Ayyalusamy Ramamoorthy . . . 18287 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18287 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 230 18287 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 . . 2012-05-10 2012-02-22 update BMRB 'update entry citation' 18287 1 . . 2012-03-22 2012-02-22 original author 'original release' 18287 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 17193 'PAP248-286 in SDS' 18287 BMRB 17346 'PAP248-286 in 50% TFE' 18287 PDB 2L3H 'PAP248-286 in SDS' 18287 PDB 2L77 'PAP248-286 in 50% TFE' 18287 PDB 2L79 'PAP248-286 in 30% TFE' 18287 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18287 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22360607 _Citation.Full_citation . _Citation.Title 'Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Phys. Chem. B' _Citation.Journal_name_full 'The journal of physical chemistry. B' _Citation.Journal_volume 116 _Citation.Journal_issue 11 _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 3650 _Citation.Page_last 3658 _Citation.Year 2012 _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 Nataliya Popovych . . . 18287 1 2 Jeffrey Brender . R. . 18287 1 3 Ronald Soong . . . 18287 1 4 Subramanian Vivekanandan . . . 18287 1 5 Kevin Hartman . . . 18287 1 6 Venkatesha Basrur . . . 18287 1 7 Peter Macdonald . M. . 18287 1 8 Ayyalusamy Ramamoorthy . . . 18287 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Amyloid 18287 1 EGCG 18287 1 'Prostatic Acid Phosphatase' 18287 1 SEVI 18287 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18287 _Assembly.ID 1 _Assembly.Name PAP248-286 _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 PAP248-286 1 $PAP248-286 A . yes native no no . . . 18287 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PAP248-286 _Entity.Sf_category entity _Entity.Sf_framecode PAP248-286 _Entity.Entry_ID 18287 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name PAP248-286 _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 ; GIHKQKEKSRLQGGVLVNEI LNHMKRATQIPSYKKLIMY ; _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 39 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _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 2015-11-25 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 17193 . PAP248-286 . . . . . 100.00 39 100.00 100.00 3.57e-18 . . . . 18287 1 2 no BMRB 17346 . entity . . . . . 100.00 39 100.00 100.00 3.57e-18 . . . . 18287 1 3 no BMRB 17347 . entity . . . . . 100.00 39 100.00 100.00 3.57e-18 . . . . 18287 1 4 no BMRB 17924 . SEVI . . . . . 100.00 39 100.00 100.00 3.57e-18 . . . . 18287 1 5 no BMRB 17925 . SEVI . . . . . 100.00 39 100.00 100.00 3.57e-18 . . . . 18287 1 6 no PDB 1CVI . "Crystal Structure Of Human Prostatic Acid Phosphatase" . . . . . 100.00 342 100.00 100.00 2.98e-17 . . . . 18287 1 7 no PDB 1ND5 . "Crystal Structures Of Human Prostatic Acid Phosphatase In Complex With A Phosphate Ion And Alpha-Benzylaminobenzylphosphonic Ac" . . . . . 100.00 354 100.00 100.00 2.87e-17 . . . . 18287 1 8 no PDB 1ND6 . "Crystal Structures Of Human Prostatic Acid Phosphatase In Complex With A Phosphate Ion And Alpha-Benzylaminobenzylphosphonic Ac" . . . . . 100.00 354 100.00 100.00 2.87e-17 . . . . 18287 1 9 no PDB 2HPA . "Structural Origins Of L(+)-Tartrate Inhibition Of Human Prostatic Acid Phosphatase" . . . . . 100.00 342 100.00 100.00 2.98e-17 . . . . 18287 1 10 no PDB 2L3H . "Nmr Structure In A Membrane Environment Reveals Putative Amyloidogenic Regions Of The Sevi Precursor Peptide Pap248-286" . . . . . 97.44 39 100.00 100.00 3.55e-17 . . . . 18287 1 11 no PDB 2L77 . "Solution Nmr Structure Of Pap248-286 In 50% Tfe" . . . . . 97.44 39 100.00 100.00 3.55e-17 . . . . 18287 1 12 no PDB 2L79 . "Solution Nmr Structure Of Pap248-286 In 30% Tfe" . . . . . 97.44 39 100.00 100.00 3.55e-17 . . . . 18287 1 13 no DBJ BAD89417 . "Acid phosphatase prostate nirs variant 1 [Homo sapiens]" . . . . . 100.00 353 100.00 100.00 5.65e-18 . . . . 18287 1 14 no DBJ BAG62248 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 353 100.00 100.00 5.65e-18 . . . . 18287 1 15 no EMBL CAA36422 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 4.48e-18 . . . . 18287 1 16 no EMBL CAA37673 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 8.16e-18 . . . . 18287 1 17 no GB AAA60021 . "prostatic acid phosphatase [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 1.50e-17 . . . . 18287 1 18 no GB AAA60022 . "acid phosphatase [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 1.01e-17 . . . . 18287 1 19 no GB AAA69694 . "acid phosphatase [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 1.50e-17 . . . . 18287 1 20 no GB AAB60640 . "prostatic acid phosphatase [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 1.50e-17 . . . . 18287 1 21 no GB AAH07460 . "ACPP protein [Homo sapiens]" . . . . . 100.00 418 100.00 100.00 2.10e-17 . . . . 18287 1 22 no REF NP_001090 . "prostatic acid phosphatase isoform PAP precursor [Homo sapiens]" . . . . . 100.00 386 100.00 100.00 1.50e-17 . . . . 18287 1 23 no REF NP_001127666 . "prostatic acid phosphatase isoform TM-PAP precursor [Homo sapiens]" . . . . . 100.00 418 100.00 100.00 2.17e-17 . . . . 18287 1 24 no REF NP_001278966 . "prostatic acid phosphatase isoform 3 [Homo sapiens]" . . . . . 100.00 353 100.00 100.00 5.65e-18 . . . . 18287 1 25 no REF XP_001115549 . "PREDICTED: prostatic acid phosphatase [Macaca mulatta]" . . . . . 100.00 418 97.44 100.00 2.19e-17 . . . . 18287 1 26 no REF XP_001148736 . "PREDICTED: prostatic acid phosphatase [Pan troglodytes]" . . . . . 100.00 418 97.44 97.44 1.00e-16 . . . . 18287 1 27 no SP P15309 . "RecName: Full=Prostatic acid phosphatase; Short=PAP; AltName: Full=5'-nucleotidase; Short=5'-NT; AltName: Full=Ecto-5'-nucleoti" . . . . . 100.00 386 100.00 100.00 1.50e-17 . . . . 18287 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'normal function unknown, forms amyloid known to enhance HIV infection' 18287 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 . GLY . 18287 1 2 . ILE . 18287 1 3 . HIS . 18287 1 4 . LYS . 18287 1 5 . GLN . 18287 1 6 . LYS . 18287 1 7 . GLU . 18287 1 8 . LYS . 18287 1 9 . SER . 18287 1 10 . ARG . 18287 1 11 . LEU . 18287 1 12 . GLN . 18287 1 13 . GLY . 18287 1 14 . GLY . 18287 1 15 . VAL . 18287 1 16 . LEU . 18287 1 17 . VAL . 18287 1 18 . ASN . 18287 1 19 . GLU . 18287 1 20 . ILE . 18287 1 21 . LEU . 18287 1 22 . ASN . 18287 1 23 . HIS . 18287 1 24 . MET . 18287 1 25 . LYS . 18287 1 26 . ARG . 18287 1 27 . ALA . 18287 1 28 . THR . 18287 1 29 . GLN . 18287 1 30 . ILE . 18287 1 31 . PRO . 18287 1 32 . SER . 18287 1 33 . TYR . 18287 1 34 . LYS . 18287 1 35 . LYS . 18287 1 36 . LEU . 18287 1 37 . ILE . 18287 1 38 . MET . 18287 1 39 . TYR . 18287 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 . GLY 1 1 18287 1 . ILE 2 2 18287 1 . HIS 3 3 18287 1 . LYS 4 4 18287 1 . GLN 5 5 18287 1 . LYS 6 6 18287 1 . GLU 7 7 18287 1 . LYS 8 8 18287 1 . SER 9 9 18287 1 . ARG 10 10 18287 1 . LEU 11 11 18287 1 . GLN 12 12 18287 1 . GLY 13 13 18287 1 . GLY 14 14 18287 1 . VAL 15 15 18287 1 . LEU 16 16 18287 1 . VAL 17 17 18287 1 . ASN 18 18 18287 1 . GLU 19 19 18287 1 . ILE 20 20 18287 1 . LEU 21 21 18287 1 . ASN 22 22 18287 1 . HIS 23 23 18287 1 . MET 24 24 18287 1 . LYS 25 25 18287 1 . ARG 26 26 18287 1 . ALA 27 27 18287 1 . THR 28 28 18287 1 . GLN 29 29 18287 1 . ILE 30 30 18287 1 . PRO 31 31 18287 1 . SER 32 32 18287 1 . TYR 33 33 18287 1 . LYS 34 34 18287 1 . LYS 35 35 18287 1 . LEU 36 36 18287 1 . ILE 37 37 18287 1 . MET 38 38 18287 1 . TYR 39 39 18287 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 18287 _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 $PAP248-286 . 9606 organism . 'Homo sapiens' Humans . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18287 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 18287 _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 $PAP248-286 . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . 'chemical synthesized' . . 18287 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18287 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '50 mM sodium phosphate pH 6' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 PAP248-286 'natural abundance' . . 1 $PAP248-286 . . 0.3 . . mM . . . . 18287 1 2 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 18287 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18287 1 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18287 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 18287 _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 'ionic strength' 50 . mM 18287 1 pH 6 . pH 18287 1 pressure 1 . atm 18287 1 temperature 273 . K 18287 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 18287 _Software.ID 1 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 18287 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18287 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18287 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 18287 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18287 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 18287 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 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 18287 _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 . 900 . . . 18287 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 18287 _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-1H TOCSY' no 1 . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18287 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 18287 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details 'referenced to tetramethylsilane' 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 internal direct 1 . . . . . . . . . 18287 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 18287 _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-1H TOCSY' . . . 18287 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 2 2 ILE H H 1 7.956 0.015 . 1 . . . . 2 I H . 18287 1 2 . 1 1 2 2 ILE HA H 1 4.341 0.015 . 1 . . . . 2 I HA . 18287 1 3 . 1 1 2 2 ILE HB H 1 1.806 0.015 . 1 . . . . 2 I HB . 18287 1 4 . 1 1 2 2 ILE HD11 H 1 0.919 0.015 . 1 . . . . 2 I HD1 . 18287 1 5 . 1 1 2 2 ILE HD12 H 1 0.919 0.015 . 1 . . . . 2 I HD1 . 18287 1 6 . 1 1 2 2 ILE HD13 H 1 0.919 0.015 . 1 . . . . 2 I HD1 . 18287 1 7 . 1 1 3 3 HIS H H 1 8.075 0.015 . 1 . . . . 3 H H . 18287 1 8 . 1 1 3 3 HIS HB3 H 1 3.041 0.015 . 2 . . . . 3 H HB3 . 18287 1 9 . 1 1 4 4 LYS H H 1 8.442 0.015 . 1 . . . . 4 K H . 18287 1 10 . 1 1 4 4 LYS HA H 1 4.316 0.015 . 1 . . . . 4 K HA . 18287 1 11 . 1 1 4 4 LYS HB2 H 1 1.892 0.015 . 2 . . . . 4 K HB2 . 18287 1 12 . 1 1 4 4 LYS HB3 H 1 1.830 0.015 . 2 . . . . 4 K HB3 . 18287 1 13 . 1 1 4 4 LYS HG2 H 1 1.504 0.015 . 2 . . . . 4 K QG . 18287 1 14 . 1 1 4 4 LYS HG3 H 1 1.504 0.015 . 2 . . . . 4 K QG . 18287 1 15 . 1 1 4 4 LYS HD2 H 1 1.758 0.015 . 2 . . . . 4 K QD . 18287 1 16 . 1 1 4 4 LYS HD3 H 1 1.758 0.015 . 2 . . . . 4 K QD . 18287 1 17 . 1 1 5 5 GLN H H 1 8.479 0.015 . 1 . . . . 5 Q H . 18287 1 18 . 1 1 5 5 GLN HA H 1 4.343 0.015 . 1 . . . . 5 Q HA . 18287 1 19 . 1 1 5 5 GLN HB2 H 1 2.108 0.015 . 2 . . . . 5 Q HB2 . 18287 1 20 . 1 1 5 5 GLN HB3 H 1 2.015 0.015 . 2 . . . . 5 Q HB3 . 18287 1 21 . 1 1 5 5 GLN HG2 H 1 2.344 0.015 . 2 . . . . 5 Q QG . 18287 1 22 . 1 1 5 5 GLN HG3 H 1 2.344 0.015 . 2 . . . . 5 Q QG . 18287 1 23 . 1 1 6 6 LYS H H 1 8.421 0.015 . 1 . . . . 6 K H . 18287 1 24 . 1 1 6 6 LYS HA H 1 4.353 0.015 . 1 . . . . 6 K HA . 18287 1 25 . 1 1 6 6 LYS HB2 H 1 1.915 0.015 . 2 . . . . 6 K HB2 . 18287 1 26 . 1 1 6 6 LYS HB3 H 1 1.832 0.015 . 2 . . . . 6 K HB3 . 18287 1 27 . 1 1 6 6 LYS HG2 H 1 1.495 0.015 . 2 . . . . 6 K QG . 18287 1 28 . 1 1 6 6 LYS HG3 H 1 1.495 0.015 . 2 . . . . 6 K QG . 18287 1 29 . 1 1 6 6 LYS HD2 H 1 1.748 0.015 . 2 . . . . 6 K QD . 18287 1 30 . 1 1 6 6 LYS HD3 H 1 1.748 0.015 . 2 . . . . 6 K QD . 18287 1 31 . 1 1 7 7 GLU H H 1 8.309 0.015 . 1 . . . . 7 E H . 18287 1 32 . 1 1 7 7 GLU HG2 H 1 2.239 0.015 . 2 . . . . 7 E QG . 18287 1 33 . 1 1 7 7 GLU HG3 H 1 2.239 0.015 . 2 . . . . 7 E QG . 18287 1 34 . 1 1 8 8 LYS H H 1 8.399 0.015 . 1 . . . . 8 K H . 18287 1 35 . 1 1 8 8 LYS HA H 1 4.432 0.015 . 1 . . . . 8 K HA . 18287 1 36 . 1 1 8 8 LYS HB2 H 1 1.940 0.015 . 2 . . . . 8 K HB2 . 18287 1 37 . 1 1 8 8 LYS HB3 H 1 1.825 0.015 . 2 . . . . 8 K HB3 . 18287 1 38 . 1 1 8 8 LYS HD2 H 1 1.691 0.015 . 2 . . . . 8 K QD . 18287 1 39 . 1 1 8 8 LYS HD3 H 1 1.691 0.015 . 2 . . . . 8 K QD . 18287 1 40 . 1 1 9 9 SER H H 1 8.259 0.015 . 1 . . . . 9 S H . 18287 1 41 . 1 1 9 9 SER HA H 1 4.400 0.015 . 1 . . . . 9 S HA . 18287 1 42 . 1 1 9 9 SER HB2 H 1 3.911 0.015 . 2 . . . . 9 S HB2 . 18287 1 43 . 1 1 9 9 SER HB3 H 1 3.873 0.015 . 2 . . . . 9 S HB3 . 18287 1 44 . 1 1 10 10 ARG H H 1 7.993 0.015 . 1 . . . . 10 R H . 18287 1 45 . 1 1 10 10 ARG HA H 1 4.626 0.015 . 1 . . . . 10 R HA . 18287 1 46 . 1 1 10 10 ARG HB2 H 1 1.832 0.015 . 2 . . . . 10 R QB . 18287 1 47 . 1 1 10 10 ARG HB3 H 1 1.832 0.015 . 2 . . . . 10 R QB . 18287 1 48 . 1 1 10 10 ARG HG2 H 1 1.703 0.015 . 2 . . . . 10 R QG . 18287 1 49 . 1 1 10 10 ARG HG3 H 1 1.703 0.015 . 2 . . . . 10 R QG . 18287 1 50 . 1 1 10 10 ARG HD2 H 1 3.094 0.015 . 2 . . . . 10 R QD . 18287 1 51 . 1 1 10 10 ARG HD3 H 1 3.094 0.015 . 2 . . . . 10 R QD . 18287 1 52 . 1 1 10 10 ARG HE H 1 7.169 0.015 . 1 . . . . 10 R HE . 18287 1 53 . 1 1 11 11 LEU H H 1 8.208 0.015 . 1 . . . . 11 L H . 18287 1 54 . 1 1 11 11 LEU HA H 1 4.425 0.015 . 1 . . . . 11 L HA . 18287 1 55 . 1 1 11 11 LEU HB2 H 1 1.696 0.015 . 2 . . . . 11 L HB2 . 18287 1 56 . 1 1 11 11 LEU HB3 H 1 1.632 0.015 . 2 . . . . 11 L HB3 . 18287 1 57 . 1 1 12 12 GLN H H 1 8.373 0.015 . 1 . . . . 12 Q H . 18287 1 58 . 1 1 12 12 GLN HA H 1 4.425 0.015 . 1 . . . . 12 Q HA . 18287 1 59 . 1 1 12 12 GLN HB2 H 1 2.186 0.015 . 2 . . . . 12 Q HB2 . 18287 1 60 . 1 1 12 12 GLN HB3 H 1 2.061 0.015 . 2 . . . . 12 Q HB3 . 18287 1 61 . 1 1 12 12 GLN HG2 H 1 2.424 0.015 . 2 . . . . 12 Q QG . 18287 1 62 . 1 1 12 12 GLN HG3 H 1 2.424 0.015 . 2 . . . . 12 Q QG . 18287 1 63 . 1 1 13 13 GLY H H 1 8.450 0.015 . 1 . . . . 13 G H . 18287 1 64 . 1 1 13 13 GLY HA2 H 1 4.033 0.015 . 2 . . . . 13 G QA . 18287 1 65 . 1 1 13 13 GLY HA3 H 1 4.033 0.015 . 2 . . . . 13 G QA . 18287 1 66 . 1 1 14 14 GLY H H 1 8.273 0.015 . 1 . . . . 14 G H . 18287 1 67 . 1 1 14 14 GLY HA2 H 1 4.028 0.015 . 2 . . . . 14 G QA . 18287 1 68 . 1 1 14 14 GLY HA3 H 1 4.028 0.015 . 2 . . . . 14 G QA . 18287 1 69 . 1 1 15 15 VAL H H 1 7.927 0.015 . 1 . . . . 15 V H . 18287 1 70 . 1 1 15 15 VAL HA H 1 4.187 0.015 . 1 . . . . 15 V HA . 18287 1 71 . 1 1 15 15 VAL HB H 1 2.132 0.015 . 1 . . . . 15 V HB . 18287 1 72 . 1 1 15 15 VAL HG11 H 1 0.983 0.015 . 2 . . . . 15 V QG . 18287 1 73 . 1 1 15 15 VAL HG12 H 1 0.983 0.015 . 2 . . . . 15 V QG . 18287 1 74 . 1 1 15 15 VAL HG13 H 1 0.983 0.015 . 2 . . . . 15 V QG . 18287 1 75 . 1 1 15 15 VAL HG21 H 1 0.983 0.015 . 2 . . . . 15 V QG . 18287 1 76 . 1 1 15 15 VAL HG22 H 1 0.983 0.015 . 2 . . . . 15 V QG . 18287 1 77 . 1 1 15 15 VAL HG23 H 1 0.983 0.015 . 2 . . . . 15 V QG . 18287 1 78 . 1 1 16 16 LEU H H 1 8.326 0.015 . 1 . . . . 16 L H . 18287 1 79 . 1 1 16 16 LEU HA H 1 4.480 0.015 . 1 . . . . 16 L HA . 18287 1 80 . 1 1 16 16 LEU HB2 H 1 1.700 0.015 . 2 . . . . 16 L HB2 . 18287 1 81 . 1 1 16 16 LEU HB3 H 1 1.645 0.015 . 2 . . . . 16 L HB3 . 18287 1 82 . 1 1 16 16 LEU HG H 1 1.467 0.015 . 1 . . . . 16 L HG . 18287 1 83 . 1 1 17 17 VAL H H 1 8.101 0.015 . 1 . . . . 17 V H . 18287 1 84 . 1 1 17 17 VAL HA H 1 4.118 0.015 . 1 . . . . 17 V HA . 18287 1 85 . 1 1 17 17 VAL HB H 1 2.130 0.015 . 1 . . . . 17 V HB . 18287 1 86 . 1 1 17 17 VAL HG11 H 1 0.991 0.015 . 2 . . . . 17 V QG . 18287 1 87 . 1 1 17 17 VAL HG12 H 1 0.991 0.015 . 2 . . . . 17 V QG . 18287 1 88 . 1 1 17 17 VAL HG13 H 1 0.991 0.015 . 2 . . . . 17 V QG . 18287 1 89 . 1 1 17 17 VAL HG21 H 1 0.991 0.015 . 2 . . . . 17 V QG . 18287 1 90 . 1 1 17 17 VAL HG22 H 1 0.991 0.015 . 2 . . . . 17 V QG . 18287 1 91 . 1 1 17 17 VAL HG23 H 1 0.991 0.015 . 2 . . . . 17 V QG . 18287 1 92 . 1 1 18 18 ASN H H 1 8.410 0.015 . 1 . . . . 18 N H . 18287 1 93 . 1 1 18 18 ASN HA H 1 4.715 0.015 . 1 . . . . 18 N HA . 18287 1 94 . 1 1 18 18 ASN HB2 H 1 2.883 0.015 . 2 . . . . 18 N HB2 . 18287 1 95 . 1 1 18 18 ASN HB3 H 1 2.805 0.015 . 2 . . . . 18 N HB3 . 18287 1 96 . 1 1 19 19 GLU H H 1 8.346 0.015 . 1 . . . . 19 E H . 18287 1 97 . 1 1 19 19 GLU HA H 1 4.312 0.015 . 1 . . . . 19 E HA . 18287 1 98 . 1 1 19 19 GLU HB2 H 1 2.108 0.015 . 2 . . . . 19 E HB2 . 18287 1 99 . 1 1 19 19 GLU HB3 H 1 2.034 0.015 . 2 . . . . 19 E HB3 . 18287 1 100 . 1 1 19 19 GLU HG2 H 1 2.329 0.015 . 2 . . . . 19 E HG2 . 18287 1 101 . 1 1 19 19 GLU HG3 H 1 2.271 0.015 . 2 . . . . 19 E HG3 . 18287 1 102 . 1 1 20 20 ILE H H 1 8.046 0.015 . 1 . . . . 20 I H . 18287 1 103 . 1 1 20 20 ILE HA H 1 4.258 0.015 . 1 . . . . 20 I HA . 18287 1 104 . 1 1 20 20 ILE HB H 1 1.948 0.015 . 1 . . . . 20 I HB . 18287 1 105 . 1 1 20 20 ILE HG12 H 1 1.262 0.015 . 2 . . . . 20 I HG12 . 18287 1 106 . 1 1 20 20 ILE HG21 H 1 1.554 0.015 . 1 . . . . 20 I HG22 . 18287 1 107 . 1 1 20 20 ILE HG22 H 1 1.554 0.015 . 1 . . . . 20 I HG22 . 18287 1 108 . 1 1 20 20 ILE HG23 H 1 1.554 0.015 . 1 . . . . 20 I HG22 . 18287 1 109 . 1 1 21 21 LEU H H 1 8.076 0.015 . 1 . . . . 21 L H . 18287 1 110 . 1 1 21 21 LEU HA H 1 4.329 0.015 . 1 . . . . 21 L HA . 18287 1 111 . 1 1 21 21 LEU HB2 H 1 1.700 0.015 . 2 . . . . 21 L QB . 18287 1 112 . 1 1 21 21 LEU HB3 H 1 1.700 0.015 . 2 . . . . 21 L QB . 18287 1 113 . 1 1 21 21 LEU HG H 1 1.584 0.015 . 1 . . . . 21 L HG . 18287 1 114 . 1 1 21 21 LEU HD11 H 1 0.943 0.015 . 2 . . . . 21 L QD . 18287 1 115 . 1 1 21 21 LEU HD12 H 1 0.943 0.015 . 2 . . . . 21 L QD . 18287 1 116 . 1 1 21 21 LEU HD13 H 1 0.943 0.015 . 2 . . . . 21 L QD . 18287 1 117 . 1 1 21 21 LEU HD21 H 1 0.943 0.015 . 2 . . . . 21 L QD . 18287 1 118 . 1 1 21 21 LEU HD22 H 1 0.943 0.015 . 2 . . . . 21 L QD . 18287 1 119 . 1 1 21 21 LEU HD23 H 1 0.943 0.015 . 2 . . . . 21 L QD . 18287 1 120 . 1 1 22 22 ASN H H 1 8.211 0.015 . 1 . . . . 22 N H . 18287 1 121 . 1 1 22 22 ASN HB2 H 1 2.837 0.015 . 2 . . . . 22 N QB . 18287 1 122 . 1 1 22 22 ASN HB3 H 1 2.837 0.015 . 2 . . . . 22 N QB . 18287 1 123 . 1 1 23 23 HIS H H 1 8.573 0.015 . 1 . . . . 23 H H . 18287 1 124 . 1 1 23 23 HIS HA H 1 4.787 0.015 . 1 . . . . 23 H HA . 18287 1 125 . 1 1 23 23 HIS HB2 H 1 3.261 0.015 . 2 . . . . 23 H HB2 . 18287 1 126 . 1 1 23 23 HIS HB3 H 1 3.171 0.015 . 2 . . . . 23 H HB3 . 18287 1 127 . 1 1 23 23 HIS HD2 H 1 7.231 0.015 . 1 . . . . 23 H HD2 . 18287 1 128 . 1 1 23 23 HIS HE1 H 1 8.320 0.015 . 1 . . . . 23 H HE1 . 18287 1 129 . 1 1 24 24 MET H H 1 8.164 0.015 . 1 . . . . 24 M H . 18287 1 130 . 1 1 24 24 MET HA H 1 4.460 0.015 . 1 . . . . 24 M HA . 18287 1 131 . 1 1 24 24 MET HB3 H 1 2.099 0.015 . 2 . . . . 24 M HB3 . 18287 1 132 . 1 1 24 24 MET HG2 H 1 2.637 0.015 . 2 . . . . 24 M HG2 . 18287 1 133 . 1 1 24 24 MET HG3 H 1 2.553 0.015 . 2 . . . . 24 M HG3 . 18287 1 134 . 1 1 24 24 MET HE1 H 1 2.156 0.015 . 1 . . . . 24 M QE . 18287 1 135 . 1 1 24 24 MET HE2 H 1 2.156 0.015 . 1 . . . . 24 M QE . 18287 1 136 . 1 1 24 24 MET HE3 H 1 2.156 0.015 . 1 . . . . 24 M QE . 18287 1 137 . 1 1 25 25 LYS H H 1 8.204 0.015 . 1 . . . . 25 K H . 18287 1 138 . 1 1 25 25 LYS HB2 H 1 1.832 0.015 . 2 . . . . 25 K HB2 . 18287 1 139 . 1 1 25 25 LYS HG2 H 1 1.464 0.015 . 2 . . . . 25 K QG . 18287 1 140 . 1 1 25 25 LYS HG3 H 1 1.464 0.015 . 2 . . . . 25 K QG . 18287 1 141 . 1 1 26 26 ARG H H 1 8.230 0.015 . 1 . . . . 26 R H . 18287 1 142 . 1 1 26 26 ARG HA H 1 4.379 0.015 . 1 . . . . 26 R HA . 18287 1 143 . 1 1 26 26 ARG HB2 H 1 1.925 0.015 . 2 . . . . 26 R HB2 . 18287 1 144 . 1 1 26 26 ARG HB3 H 1 1.821 0.015 . 2 . . . . 26 R HB3 . 18287 1 145 . 1 1 26 26 ARG HG2 H 1 1.702 0.015 . 2 . . . . 26 R QG . 18287 1 146 . 1 1 26 26 ARG HG3 H 1 1.702 0.015 . 2 . . . . 26 R QG . 18287 1 147 . 1 1 27 27 ALA H H 1 7.986 0.015 . 1 . . . . 27 A H . 18287 1 148 . 1 1 27 27 ALA HA H 1 4.282 0.015 . 1 . . . . 27 A HA . 18287 1 149 . 1 1 27 27 ALA HB1 H 1 1.366 0.015 . 1 . . . . 27 A QB . 18287 1 150 . 1 1 27 27 ALA HB2 H 1 1.366 0.015 . 1 . . . . 27 A QB . 18287 1 151 . 1 1 27 27 ALA HB3 H 1 1.366 0.015 . 1 . . . . 27 A QB . 18287 1 152 . 1 1 28 28 THR H H 1 8.049 0.015 . 1 . . . . 28 T H . 18287 1 153 . 1 1 28 28 THR HA H 1 4.348 0.015 . 1 . . . . 28 T HA . 18287 1 154 . 1 1 28 28 THR HB H 1 4.099 0.015 . 1 . . . . 28 T HB . 18287 1 155 . 1 1 28 28 THR HG21 H 1 1.256 0.015 . 1 . . . . 28 T HG2 . 18287 1 156 . 1 1 28 28 THR HG22 H 1 1.256 0.015 . 1 . . . . 28 T HG2 . 18287 1 157 . 1 1 28 28 THR HG23 H 1 1.256 0.015 . 1 . . . . 28 T HG2 . 18287 1 158 . 1 1 29 29 GLN H H 1 8.307 0.015 . 1 . . . . 29 Q H . 18287 1 159 . 1 1 29 29 GLN HA H 1 4.442 0.015 . 1 . . . . 29 Q HA . 18287 1 160 . 1 1 29 29 GLN HB2 H 1 2.119 0.015 . 2 . . . . 29 Q HB2 . 18287 1 161 . 1 1 29 29 GLN HB3 H 1 2.024 0.015 . 2 . . . . 29 Q HB3 . 18287 1 162 . 1 1 29 29 GLN HG2 H 1 2.387 0.015 . 2 . . . . 29 Q QG . 18287 1 163 . 1 1 29 29 GLN HG3 H 1 2.387 0.015 . 2 . . . . 29 Q QG . 18287 1 164 . 1 1 30 30 ILE H H 1 8.187 0.015 . 1 . . . . 30 I H . 18287 1 165 . 1 1 30 30 ILE HA H 1 4.507 0.015 . 1 . . . . 30 I HA . 18287 1 166 . 1 1 30 30 ILE HB H 1 1.915 0.015 . 1 . . . . 30 I HB . 18287 1 167 . 1 1 30 30 ILE HG12 H 1 1.228 0.015 . 2 . . . . 30 I HG12 . 18287 1 168 . 1 1 30 30 ILE HG13 H 1 1.001 0.015 . 2 . . . . 30 I HG13 . 18287 1 169 . 1 1 30 30 ILE HG21 H 1 1.551 0.015 . 1 . . . . 30 I HG22 . 18287 1 170 . 1 1 30 30 ILE HG22 H 1 1.551 0.015 . 1 . . . . 30 I HG22 . 18287 1 171 . 1 1 30 30 ILE HG23 H 1 1.551 0.015 . 1 . . . . 30 I HG22 . 18287 1 172 . 1 1 30 30 ILE HD11 H 1 0.909 0.015 . 1 . . . . 30 I HD1 . 18287 1 173 . 1 1 30 30 ILE HD12 H 1 0.909 0.015 . 1 . . . . 30 I HD1 . 18287 1 174 . 1 1 30 30 ILE HD13 H 1 0.909 0.015 . 1 . . . . 30 I HD1 . 18287 1 175 . 1 1 31 31 PRO HB2 H 1 2.295 0.015 . 2 . . . . 31 P HB2 . 18287 1 176 . 1 1 31 31 PRO HB3 H 1 2.050 0.015 . 2 . . . . 31 P HB3 . 18287 1 177 . 1 1 31 31 PRO HG2 H 1 1.792 0.015 . 2 . . . . 31 P QG . 18287 1 178 . 1 1 31 31 PRO HG3 H 1 1.792 0.015 . 2 . . . . 31 P QG . 18287 1 179 . 1 1 31 31 PRO HD2 H 1 3.950 0.015 . 2 . . . . 31 P HD2 . 18287 1 180 . 1 1 31 31 PRO HD3 H 1 3.730 0.015 . 2 . . . . 31 P HD3 . 18287 1 181 . 1 1 32 32 SER H H 1 8.307 0.015 . 1 . . . . 32 S H . 18287 1 182 . 1 1 32 32 SER HA H 1 4.541 0.015 . 1 . . . . 32 S HA . 18287 1 183 . 1 1 32 32 SER HB2 H 1 3.925 0.015 . 2 . . . . 32 S QB . 18287 1 184 . 1 1 32 32 SER HB3 H 1 3.925 0.015 . 2 . . . . 32 S QB . 18287 1 185 . 1 1 33 33 TYR H H 1 7.820 0.015 . 1 . . . . 33 Y H . 18287 1 186 . 1 1 33 33 TYR HA H 1 4.448 0.015 . 1 . . . . 33 Y HA . 18287 1 187 . 1 1 33 33 TYR HB2 H 1 3.163 0.015 . 2 . . . . 33 Y HB2 . 18287 1 188 . 1 1 33 33 TYR HB3 H 1 2.909 0.015 . 2 . . . . 33 Y HB3 . 18287 1 189 . 1 1 34 34 LYS H H 1 8.203 0.015 . 1 . . . . 34 K H . 18287 1 190 . 1 1 34 34 LYS HA H 1 4.342 0.015 . 1 . . . . 34 K HA . 18287 1 191 . 1 1 34 34 LYS HG2 H 1 1.527 0.015 . 2 . . . . 34 K QG . 18287 1 192 . 1 1 34 34 LYS HG3 H 1 1.527 0.015 . 2 . . . . 34 K QG . 18287 1 193 . 1 1 35 35 LYS H H 1 8.068 0.015 . 1 . . . . 35 K H . 18287 1 194 . 1 1 35 35 LYS HA H 1 4.310 0.015 . 1 . . . . 35 K HA . 18287 1 195 . 1 1 35 35 LYS HB2 H 1 1.865 0.015 . 2 . . . . 35 K HB2 . 18287 1 196 . 1 1 35 35 LYS HB3 H 1 1.778 0.015 . 2 . . . . 35 K HB3 . 18287 1 197 . 1 1 35 35 LYS HG2 H 1 1.436 0.015 . 2 . . . . 35 K QG . 18287 1 198 . 1 1 35 35 LYS HG3 H 1 1.436 0.015 . 2 . . . . 35 K QG . 18287 1 199 . 1 1 36 36 LEU H H 1 8.156 0.015 . 1 . . . . 36 L H . 18287 1 200 . 1 1 36 36 LEU HA H 1 4.406 0.015 . 1 . . . . 36 L HA . 18287 1 201 . 1 1 36 36 LEU HB2 H 1 1.637 0.015 . 2 . . . . 36 L QB . 18287 1 202 . 1 1 36 36 LEU HB3 H 1 1.637 0.015 . 2 . . . . 36 L QB . 18287 1 203 . 1 1 36 36 LEU HD11 H 1 0.910 0.015 . 2 . . . . 36 L QD . 18287 1 204 . 1 1 36 36 LEU HD12 H 1 0.910 0.015 . 2 . . . . 36 L QD . 18287 1 205 . 1 1 36 36 LEU HD13 H 1 0.910 0.015 . 2 . . . . 36 L QD . 18287 1 206 . 1 1 36 36 LEU HD21 H 1 0.910 0.015 . 2 . . . . 36 L QD . 18287 1 207 . 1 1 36 36 LEU HD22 H 1 0.910 0.015 . 2 . . . . 36 L QD . 18287 1 208 . 1 1 36 36 LEU HD23 H 1 0.910 0.015 . 2 . . . . 36 L QD . 18287 1 209 . 1 1 37 37 ILE H H 1 7.994 0.015 . 1 . . . . 37 I H . 18287 1 210 . 1 1 37 37 ILE HA H 1 4.174 0.015 . 1 . . . . 37 I HA . 18287 1 211 . 1 1 37 37 ILE HB H 1 1.833 0.015 . 1 . . . . 37 I HB . 18287 1 212 . 1 1 37 37 ILE HG12 H 1 1.182 0.015 . 2 . . . . 37 I HG12 . 18287 1 213 . 1 1 37 37 ILE HG13 H 1 0.887 0.015 . 2 . . . . 37 I HG12 . 18287 1 214 . 1 1 37 37 ILE HG21 H 1 1.476 0.015 . 1 . . . . 37 I HG22 . 18287 1 215 . 1 1 37 37 ILE HG22 H 1 1.476 0.015 . 1 . . . . 37 I HG22 . 18287 1 216 . 1 1 37 37 ILE HG23 H 1 1.476 0.015 . 1 . . . . 37 I HG22 . 18287 1 217 . 1 1 37 37 ILE HD11 H 1 0.805 0.015 . 1 . . . . 37 I HD1 . 18287 1 218 . 1 1 37 37 ILE HD12 H 1 0.805 0.015 . 1 . . . . 37 I HD1 . 18287 1 219 . 1 1 37 37 ILE HD13 H 1 0.805 0.015 . 1 . . . . 37 I HD1 . 18287 1 220 . 1 1 38 38 MET H H 1 8.206 0.015 . 1 . . . . 38 M H . 18287 1 221 . 1 1 38 38 MET HA H 1 4.523 0.015 . 1 . . . . 38 M HA . 18287 1 222 . 1 1 38 38 MET HB2 H 1 2.071 0.015 . 2 . . . . 38 M HB2 . 18287 1 223 . 1 1 38 38 MET HB3 H 1 1.928 0.015 . 2 . . . . 38 M HB3 . 18287 1 224 . 1 1 38 38 MET HG2 H 1 2.571 0.015 . 2 . . . . 38 M HG2 . 18287 1 225 . 1 1 38 38 MET HG3 H 1 2.487 0.015 . 2 . . . . 38 M HG3 . 18287 1 226 . 1 1 39 39 TYR H H 1 7.643 0.015 . 1 . . . . 39 Y H . 18287 1 227 . 1 1 39 39 TYR HA H 1 4.445 0.015 . 1 . . . . 39 Y HA . 18287 1 228 . 1 1 39 39 TYR HB2 H 1 3.153 0.015 . 2 . . . . 39 Y HB2 . 18287 1 229 . 1 1 39 39 TYR HB3 H 1 2.925 0.015 . 2 . . . . 39 Y HB3 . 18287 1 stop_ save_