data_5318 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5318 _Entry.Title ; Backbone and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-03-13 _Entry.Accession_date 2002-03-13 _Entry.Last_release_date 2002-05-01 _Entry.Original_release_date 2002-05-01 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Julie Forman-Kay . D . 5318 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5318 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 98 5318 '1H chemical shifts' 98 5318 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-05-01 2002-03-13 original author . 5318 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5310 'Protein in complex form with a PDGFR-derived phosphopeptide.' 5318 PDB 2PLD 'BMRB Entry Tracking System' 5318 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5318 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8181064 _Citation.Full_citation . _Citation.Title ; Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Cell _Citation.Journal_name_full . _Citation.Journal_volume 77 _Citation.Journal_issue 3 _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 461 _Citation.Page_last 472 _Citation.Year 1994 _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 Steve Pascal . M. . 5318 1 2 Gerry Gish . . . 5318 1 3 Toshio Yamazaki . . . 5318 1 4 Alex Singer . U. . 5318 1 5 Steven Shoelson . E. . 5318 1 6 Tony Pawson . . . 5318 1 7 Lewis Kay . E. . 5318 1 8 Julie Forman-Kay . D. . 5318 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5318 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 88156963 _Citation.Full_citation ; Stahl ML, Ferenz CR, Kelleher KL, Kriz RW, Knopf JL. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature. 1988 Mar 17;332(6161):269-72. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5318 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 93213786 _Citation.Full_citation ; Piccione E, Case RD, Domchek SM, Hu P, Chaudhuri M, Backer JM, Schlessinger J, Shoelson SE. Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding. Biochemistry. 1993 Apr 6;32(13):3197-202. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5318 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Brunger, A.T. (1992) X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR (New Haven, Connecticut: Yale University Press). ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 5318 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 90212257 _Citation.Full_citation ; Miguel Giacchella R. [The history of the discovery of anesthesia. Progress is the attainment of utopia] Rev Soc Odontol La Plata. 1988 Apr;1(1):29-30. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_PLCC_SH2 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_PLCC_SH2 _Assembly.Entry_ID 5318 _Assembly.ID 1 _Assembly.Name 'phospholipase C gamma-1 C-terminal SH2 domain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 3.1.4.3 _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID complex 5318 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 'PLCC SH2 domain' 1 $PLCC_SH2 . . . native . . . . . 5318 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 2PLD . . . . . . 5318 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'phospholipase C gamma-1 C-terminal SH2 domain' system 5318 1 'PLCC SH2' abbreviation 5318 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Binds cell surface receptors and participates in intracellular signalling.' 5318 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PLCC_SH2 _Entity.Sf_category entity _Entity.Sf_framecode PLCC_SH2 _Entity.Entry_ID 5318 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'PLCC SH2' _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 ; GSPGIHESKEWYHASLTRAQ AEHMLMRVPRDGAFLVRKRN EPNSYAISFRAEGKIKHCRV QQEGQTVMLGNSEFDSLVDL ISYYEKHPLYRKMKLRYPIN EENSS ; _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 105 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _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 ; Residues 663 to 759 of PLC gamma-1, with five add'l N-term and three add'l C-term residues. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 2FCI . "Structural Basis For The Requirement Of Two Phosphotyrosines In Signaling Mediated By Syk Tyrosine Kinase" . . . . . 100.00 105 100.00 100.00 5.26e-72 . . . . 5318 1 2 no PDB 2PLD . "Nuclear Magnetic Resonance Structure Of An Sh2 Domain Of Phospholipase C-gamma1 Complexed With A High Affinity Binding Peptide" . . . . . 100.00 105 100.00 100.00 5.26e-72 . . . . 5318 1 3 no PDB 2PLE . "Nuclear Magnetic Resonance Structure Of An Sh2 Domain Of Phospholipase C-Gamma1 Complexed With A High Affinity Binding Peptide" . . . . . 100.00 105 100.00 100.00 5.26e-72 . . . . 5318 1 4 no PDB 4K44 . "Auto-inhibition And Phosphorylation-induced Activation Of Plc-gamma Isozymes" . . . . . 91.43 106 100.00 100.00 5.46e-65 . . . . 5318 1 5 no PDB 4K45 . "Auto-inhibition And Phosphorylation-induced Activation Of Plc-gamma Isozymes" . . . . . 91.43 106 100.00 100.00 5.46e-65 . . . . 5318 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'PLCC SH2' abbreviation 5318 1 'PLCC SH2' common 5318 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 . 5318 1 2 . SER . 5318 1 3 . PRO . 5318 1 4 . GLY . 5318 1 5 . ILE . 5318 1 6 . HIS . 5318 1 7 . GLU . 5318 1 8 . SER . 5318 1 9 . LYS . 5318 1 10 . GLU . 5318 1 11 . TRP . 5318 1 12 . TYR . 5318 1 13 . HIS . 5318 1 14 . ALA . 5318 1 15 . SER . 5318 1 16 . LEU . 5318 1 17 . THR . 5318 1 18 . ARG . 5318 1 19 . ALA . 5318 1 20 . GLN . 5318 1 21 . ALA . 5318 1 22 . GLU . 5318 1 23 . HIS . 5318 1 24 . MET . 5318 1 25 . LEU . 5318 1 26 . MET . 5318 1 27 . ARG . 5318 1 28 . VAL . 5318 1 29 . PRO . 5318 1 30 . ARG . 5318 1 31 . ASP . 5318 1 32 . GLY . 5318 1 33 . ALA . 5318 1 34 . PHE . 5318 1 35 . LEU . 5318 1 36 . VAL . 5318 1 37 . ARG . 5318 1 38 . LYS . 5318 1 39 . ARG . 5318 1 40 . ASN . 5318 1 41 . GLU . 5318 1 42 . PRO . 5318 1 43 . ASN . 5318 1 44 . SER . 5318 1 45 . TYR . 5318 1 46 . ALA . 5318 1 47 . ILE . 5318 1 48 . SER . 5318 1 49 . PHE . 5318 1 50 . ARG . 5318 1 51 . ALA . 5318 1 52 . GLU . 5318 1 53 . GLY . 5318 1 54 . LYS . 5318 1 55 . ILE . 5318 1 56 . LYS . 5318 1 57 . HIS . 5318 1 58 . CYS . 5318 1 59 . ARG . 5318 1 60 . VAL . 5318 1 61 . GLN . 5318 1 62 . GLN . 5318 1 63 . GLU . 5318 1 64 . GLY . 5318 1 65 . GLN . 5318 1 66 . THR . 5318 1 67 . VAL . 5318 1 68 . MET . 5318 1 69 . LEU . 5318 1 70 . GLY . 5318 1 71 . ASN . 5318 1 72 . SER . 5318 1 73 . GLU . 5318 1 74 . PHE . 5318 1 75 . ASP . 5318 1 76 . SER . 5318 1 77 . LEU . 5318 1 78 . VAL . 5318 1 79 . ASP . 5318 1 80 . LEU . 5318 1 81 . ILE . 5318 1 82 . SER . 5318 1 83 . TYR . 5318 1 84 . TYR . 5318 1 85 . GLU . 5318 1 86 . LYS . 5318 1 87 . HIS . 5318 1 88 . PRO . 5318 1 89 . LEU . 5318 1 90 . TYR . 5318 1 91 . ARG . 5318 1 92 . LYS . 5318 1 93 . MET . 5318 1 94 . LYS . 5318 1 95 . LEU . 5318 1 96 . ARG . 5318 1 97 . TYR . 5318 1 98 . PRO . 5318 1 99 . ILE . 5318 1 100 . ASN . 5318 1 101 . GLU . 5318 1 102 . GLU . 5318 1 103 . ASN . 5318 1 104 . SER . 5318 1 105 . SER . 5318 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 5318 1 . SER 2 2 5318 1 . PRO 3 3 5318 1 . GLY 4 4 5318 1 . ILE 5 5 5318 1 . HIS 6 6 5318 1 . GLU 7 7 5318 1 . SER 8 8 5318 1 . LYS 9 9 5318 1 . GLU 10 10 5318 1 . TRP 11 11 5318 1 . TYR 12 12 5318 1 . HIS 13 13 5318 1 . ALA 14 14 5318 1 . SER 15 15 5318 1 . LEU 16 16 5318 1 . THR 17 17 5318 1 . ARG 18 18 5318 1 . ALA 19 19 5318 1 . GLN 20 20 5318 1 . ALA 21 21 5318 1 . GLU 22 22 5318 1 . HIS 23 23 5318 1 . MET 24 24 5318 1 . LEU 25 25 5318 1 . MET 26 26 5318 1 . ARG 27 27 5318 1 . VAL 28 28 5318 1 . PRO 29 29 5318 1 . ARG 30 30 5318 1 . ASP 31 31 5318 1 . GLY 32 32 5318 1 . ALA 33 33 5318 1 . PHE 34 34 5318 1 . LEU 35 35 5318 1 . VAL 36 36 5318 1 . ARG 37 37 5318 1 . LYS 38 38 5318 1 . ARG 39 39 5318 1 . ASN 40 40 5318 1 . GLU 41 41 5318 1 . PRO 42 42 5318 1 . ASN 43 43 5318 1 . SER 44 44 5318 1 . TYR 45 45 5318 1 . ALA 46 46 5318 1 . ILE 47 47 5318 1 . SER 48 48 5318 1 . PHE 49 49 5318 1 . ARG 50 50 5318 1 . ALA 51 51 5318 1 . GLU 52 52 5318 1 . GLY 53 53 5318 1 . LYS 54 54 5318 1 . ILE 55 55 5318 1 . LYS 56 56 5318 1 . HIS 57 57 5318 1 . CYS 58 58 5318 1 . ARG 59 59 5318 1 . VAL 60 60 5318 1 . GLN 61 61 5318 1 . GLN 62 62 5318 1 . GLU 63 63 5318 1 . GLY 64 64 5318 1 . GLN 65 65 5318 1 . THR 66 66 5318 1 . VAL 67 67 5318 1 . MET 68 68 5318 1 . LEU 69 69 5318 1 . GLY 70 70 5318 1 . ASN 71 71 5318 1 . SER 72 72 5318 1 . GLU 73 73 5318 1 . PHE 74 74 5318 1 . ASP 75 75 5318 1 . SER 76 76 5318 1 . LEU 77 77 5318 1 . VAL 78 78 5318 1 . ASP 79 79 5318 1 . LEU 80 80 5318 1 . ILE 81 81 5318 1 . SER 82 82 5318 1 . TYR 83 83 5318 1 . TYR 84 84 5318 1 . GLU 85 85 5318 1 . LYS 86 86 5318 1 . HIS 87 87 5318 1 . PRO 88 88 5318 1 . LEU 89 89 5318 1 . TYR 90 90 5318 1 . ARG 91 91 5318 1 . LYS 92 92 5318 1 . MET 93 93 5318 1 . LYS 94 94 5318 1 . LEU 95 95 5318 1 . ARG 96 96 5318 1 . TYR 97 97 5318 1 . PRO 98 98 5318 1 . ILE 99 99 5318 1 . ASN 100 100 5318 1 . GLU 101 101 5318 1 . GLU 102 102 5318 1 . ASN 103 103 5318 1 . SER 104 104 5318 1 . SER 105 105 5318 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 5318 _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 $PLCC_SH2 . 9913 organism . 'Bos taurus' Cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 5318 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 5318 _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 $PLCC_SH2 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 . . . . . . . . . . . . . . . . . . . '50 mg protein/L of E.coli culture.' . . 5318 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5318 _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 'PLCC SH2' '[U-99% 15N]' . . 1 $PLCC_SH2 . . 1.5 . . mM . . . . 5318 1 2 'sodium phosphate' . . . . . . . 100 . . mM . . . . 5318 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5318 _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 6.4 0.2 n/a 5318 1 temperature 303 1 K 5318 1 stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 5318 _Software.ID 1 _Software.Name X-PLOR _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'combined distance geometry-simulated annealing calculations' 5318 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref_3 5318 1 stop_ save_ save_STEREOSEARCH _Software.Sf_category software _Software.Sf_framecode STEREOSEARCH _Software.Entry_ID 5318 _Software.ID 2 _Software.Name STEREOSEARCH _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'extraction of torsion angle restraint values' 5318 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 5 $ref_4 5318 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 5318 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITY _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5318 _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 Varian UNITY . 500 . . . 5318 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 5318 _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 '3D 13C- or 15N-edited NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 2 '3D 15N-edited TOCSY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 3 'CN NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 4 HBCBCA(CO)NNH . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 5 HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 6 (HB)CB(CGCD)HD . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 7 (HB)CB(CGCDCE)HE . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 8 'HMQC J' . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5318 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5318 _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 water protons . . . . ppm 4.725 internal direct 1.0 internal cylindrical parallel . . temperature . . . 5318 1 N 15 urea 'amino nitrogens' . . . . ppm 78.98 external direct 1.0 external cylindrical parallel . . . . . . 5318 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5318 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details 'Some protons (e.g Arg Nh) unobservable due to line broadening or overlap with similar species.' _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 . 5318 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 4 4 GLY H H 1 8.45 0.02 . 1 . . . . . . . . 5318 1 2 . 1 1 4 4 GLY N N 15 109.28 0.02 . 1 . . . . . . . . 5318 1 3 . 1 1 5 5 ILE H H 1 8.03 0.02 . 1 . . . . . . . . 5318 1 4 . 1 1 5 5 ILE N N 15 120.52 0.02 . 1 . . . . . . . . 5318 1 5 . 1 1 6 6 HIS H H 1 8.20 0.02 . 1 . . . . . . . . 5318 1 6 . 1 1 6 6 HIS N N 15 119.89 0.02 . 1 . . . . . . . . 5318 1 7 . 1 1 7 7 GLU H H 1 7.66 0.02 . 1 . . . . . . . . 5318 1 8 . 1 1 7 7 GLU N N 15 120.01 0.02 . 1 . . . . . . . . 5318 1 9 . 1 1 8 8 SER H H 1 7.54 0.02 . 1 . . . . . . . . 5318 1 10 . 1 1 8 8 SER N N 15 113.73 0.02 . 1 . . . . . . . . 5318 1 11 . 1 1 9 9 LYS H H 1 7.63 0.02 . 1 . . . . . . . . 5318 1 12 . 1 1 9 9 LYS N N 15 122.10 0.02 . 1 . . . . . . . . 5318 1 13 . 1 1 10 10 GLU H H 1 8.67 0.02 . 1 . . . . . . . . 5318 1 14 . 1 1 10 10 GLU N N 15 120.51 0.02 . 1 . . . . . . . . 5318 1 15 . 1 1 11 11 TRP H H 1 6.21 0.02 . 1 . . . . . . . . 5318 1 16 . 1 1 11 11 TRP N N 15 109.55 0.02 . 1 . . . . . . . . 5318 1 17 . 1 1 12 12 TYR H H 1 7.67 0.02 . 1 . . . . . . . . 5318 1 18 . 1 1 12 12 TYR N N 15 123.60 0.02 . 1 . . . . . . . . 5318 1 19 . 1 1 13 13 HIS H H 1 8.55 0.02 . 1 . . . . . . . . 5318 1 20 . 1 1 13 13 HIS N N 15 127.82 0.02 . 1 . . . . . . . . 5318 1 21 . 1 1 14 14 ALA H H 1 8.19 0.02 . 1 . . . . . . . . 5318 1 22 . 1 1 14 14 ALA N N 15 125.09 0.02 . 1 . . . . . . . . 5318 1 23 . 1 1 15 15 SER H H 1 8.20 0.02 . 1 . . . . . . . . 5318 1 24 . 1 1 15 15 SER N N 15 111.59 0.02 . 1 . . . . . . . . 5318 1 25 . 1 1 16 16 LEU H H 1 7.95 0.02 . 1 . . . . . . . . 5318 1 26 . 1 1 16 16 LEU N N 15 126.36 0.02 . 1 . . . . . . . . 5318 1 27 . 1 1 17 17 THR H H 1 8.67 0.02 . 1 . . . . . . . . 5318 1 28 . 1 1 17 17 THR N N 15 116.94 0.02 . 1 . . . . . . . . 5318 1 29 . 1 1 18 18 ARG H H 1 9.08 0.02 . 1 . . . . . . . . 5318 1 30 . 1 1 18 18 ARG N N 15 122.59 0.02 . 1 . . . . . . . . 5318 1 31 . 1 1 19 19 ALA H H 1 8.32 0.02 . 1 . . . . . . . . 5318 1 32 . 1 1 19 19 ALA N N 15 119.72 0.02 . 1 . . . . . . . . 5318 1 33 . 1 1 20 20 GLN H H 1 7.73 0.02 . 1 . . . . . . . . 5318 1 34 . 1 1 20 20 GLN N N 15 118.26 0.02 . 1 . . . . . . . . 5318 1 35 . 1 1 21 21 ALA H H 1 8.58 0.02 . 1 . . . . . . . . 5318 1 36 . 1 1 21 21 ALA N N 15 122.72 0.02 . 1 . . . . . . . . 5318 1 37 . 1 1 22 22 GLU H H 1 8.45 0.02 . 1 . . . . . . . . 5318 1 38 . 1 1 22 22 GLU N N 15 116.54 0.02 . 1 . . . . . . . . 5318 1 39 . 1 1 23 23 HIS H H 1 7.92 0.02 . 1 . . . . . . . . 5318 1 40 . 1 1 23 23 HIS N N 15 116.93 0.02 . 1 . . . . . . . . 5318 1 41 . 1 1 24 24 MET H H 1 7.90 0.02 . 1 . . . . . . . . 5318 1 42 . 1 1 24 24 MET N N 15 117.99 0.02 . 1 . . . . . . . . 5318 1 43 . 1 1 25 25 LEU H H 1 7.98 0.02 . 1 . . . . . . . . 5318 1 44 . 1 1 25 25 LEU N N 15 117.80 0.02 . 1 . . . . . . . . 5318 1 45 . 1 1 26 26 MET H H 1 7.99 0.02 . 1 . . . . . . . . 5318 1 46 . 1 1 26 26 MET N N 15 118.71 0.02 . 1 . . . . . . . . 5318 1 47 . 1 1 27 27 ARG H H 1 7.02 0.02 . 1 . . . . . . . . 5318 1 48 . 1 1 27 27 ARG N N 15 116.29 0.02 . 1 . . . . . . . . 5318 1 49 . 1 1 28 28 VAL H H 1 7.01 0.02 . 1 . . . . . . . . 5318 1 50 . 1 1 28 28 VAL N N 15 119.15 0.02 . 1 . . . . . . . . 5318 1 51 . 1 1 30 30 ARG H H 1 7.86 0.02 . 1 . . . . . . . . 5318 1 52 . 1 1 30 30 ARG N N 15 121.78 0.02 . 1 . . . . . . . . 5318 1 53 . 1 1 31 31 ASP H H 1 8.69 0.02 . 1 . . . . . . . . 5318 1 54 . 1 1 31 31 ASP N N 15 124.58 0.02 . 1 . . . . . . . . 5318 1 55 . 1 1 32 32 GLY H H 1 9.45 0.02 . 1 . . . . . . . . 5318 1 56 . 1 1 32 32 GLY N N 15 109.84 0.02 . 1 . . . . . . . . 5318 1 57 . 1 1 33 33 ALA H H 1 7.86 0.02 . 1 . . . . . . . . 5318 1 58 . 1 1 33 33 ALA N N 15 126.42 0.02 . 1 . . . . . . . . 5318 1 59 . 1 1 34 34 PHE H H 1 8.59 0.02 . 1 . . . . . . . . 5318 1 60 . 1 1 34 34 PHE N N 15 117.53 0.02 . 1 . . . . . . . . 5318 1 61 . 1 1 35 35 LEU H H 1 9.22 0.02 . 1 . . . . . . . . 5318 1 62 . 1 1 35 35 LEU N N 15 114.53 0.02 . 1 . . . . . . . . 5318 1 63 . 1 1 36 36 VAL H H 1 9.44 0.02 . 1 . . . . . . . . 5318 1 64 . 1 1 36 36 VAL N N 15 120.69 0.02 . 1 . . . . . . . . 5318 1 65 . 1 1 37 37 ARG H H 1 9.48 0.02 . 1 . . . . . . . . 5318 1 66 . 1 1 37 37 ARG N N 15 123.06 0.02 . 1 . . . . . . . . 5318 1 67 . 1 1 38 38 LYS H H 1 8.01 0.02 . 1 . . . . . . . . 5318 1 68 . 1 1 38 38 LYS N N 15 124.82 0.02 . 1 . . . . . . . . 5318 1 69 . 1 1 39 39 ARG H H 1 7.98 0.02 . 1 . . . . . . . . 5318 1 70 . 1 1 39 39 ARG N N 15 127.09 0.02 . 1 . . . . . . . . 5318 1 71 . 1 1 40 40 ASN H H 1 8.49 0.02 . 1 . . . . . . . . 5318 1 72 . 1 1 40 40 ASN N N 15 118.32 0.02 . 1 . . . . . . . . 5318 1 73 . 1 1 41 41 GLU H H 1 7.31 0.02 . 1 . . . . . . . . 5318 1 74 . 1 1 41 41 GLU N N 15 120.00 0.02 . 1 . . . . . . . . 5318 1 75 . 1 1 43 43 ASN H H 1 8.78 0.02 . 1 . . . . . . . . 5318 1 76 . 1 1 43 43 ASN N N 15 116.16 0.02 . 1 . . . . . . . . 5318 1 77 . 1 1 44 44 SER H H 1 7.61 0.02 . 1 . . . . . . . . 5318 1 78 . 1 1 44 44 SER N N 15 109.49 0.02 . 1 . . . . . . . . 5318 1 79 . 1 1 45 45 TYR H H 1 9.06 0.02 . 1 . . . . . . . . 5318 1 80 . 1 1 45 45 TYR N N 15 124.37 0.02 . 1 . . . . . . . . 5318 1 81 . 1 1 46 46 ALA H H 1 9.43 0.02 . 1 . . . . . . . . 5318 1 82 . 1 1 46 46 ALA N N 15 121.29 0.02 . 1 . . . . . . . . 5318 1 83 . 1 1 47 47 ILE H H 1 9.03 0.02 . 1 . . . . . . . . 5318 1 84 . 1 1 47 47 ILE N N 15 121.21 0.02 . 1 . . . . . . . . 5318 1 85 . 1 1 48 48 SER H H 1 9.06 0.02 . 1 . . . . . . . . 5318 1 86 . 1 1 48 48 SER N N 15 126.60 0.02 . 1 . . . . . . . . 5318 1 87 . 1 1 49 49 PHE H H 1 8.83 0.02 . 1 . . . . . . . . 5318 1 88 . 1 1 49 49 PHE N N 15 121.38 0.02 . 1 . . . . . . . . 5318 1 89 . 1 1 50 50 ARG H H 1 8.24 0.02 . 1 . . . . . . . . 5318 1 90 . 1 1 50 50 ARG N N 15 119.43 0.02 . 1 . . . . . . . . 5318 1 91 . 1 1 51 51 ALA H H 1 8.87 0.02 . 1 . . . . . . . . 5318 1 92 . 1 1 51 51 ALA N N 15 126.95 0.02 . 1 . . . . . . . . 5318 1 93 . 1 1 52 52 GLU H H 1 9.23 0.02 . 1 . . . . . . . . 5318 1 94 . 1 1 52 52 GLU N N 15 121.64 0.02 . 1 . . . . . . . . 5318 1 95 . 1 1 53 53 GLY H H 1 9.32 0.02 . 1 . . . . . . . . 5318 1 96 . 1 1 53 53 GLY N N 15 105.80 0.02 . 1 . . . . . . . . 5318 1 97 . 1 1 54 54 LYS H H 1 7.83 0.02 . 1 . . . . . . . . 5318 1 98 . 1 1 54 54 LYS N N 15 120.78 0.02 . 1 . . . . . . . . 5318 1 99 . 1 1 55 55 ILE H H 1 8.21 0.02 . 1 . . . . . . . . 5318 1 100 . 1 1 55 55 ILE N N 15 119.84 0.02 . 1 . . . . . . . . 5318 1 101 . 1 1 56 56 LYS H H 1 8.48 0.02 . 1 . . . . . . . . 5318 1 102 . 1 1 56 56 LYS N N 15 128.99 0.02 . 1 . . . . . . . . 5318 1 103 . 1 1 57 57 HIS H H 1 7.89 0.02 . 1 . . . . . . . . 5318 1 104 . 1 1 57 57 HIS N N 15 115.65 0.02 . 1 . . . . . . . . 5318 1 105 . 1 1 58 58 CYS H H 1 9.44 0.02 . 1 . . . . . . . . 5318 1 106 . 1 1 58 58 CYS N N 15 121.40 0.02 . 1 . . . . . . . . 5318 1 107 . 1 1 59 59 ARG H H 1 8.86 0.02 . 1 . . . . . . . . 5318 1 108 . 1 1 59 59 ARG N N 15 126.13 0.02 . 1 . . . . . . . . 5318 1 109 . 1 1 60 60 VAL H H 1 8.87 0.02 . 1 . . . . . . . . 5318 1 110 . 1 1 60 60 VAL N N 15 123.90 0.02 . 1 . . . . . . . . 5318 1 111 . 1 1 61 61 GLN H H 1 8.54 0.02 . 1 . . . . . . . . 5318 1 112 . 1 1 61 61 GLN N N 15 125.83 0.02 . 1 . . . . . . . . 5318 1 113 . 1 1 62 62 GLN H H 1 8.66 0.02 . 1 . . . . . . . . 5318 1 114 . 1 1 62 62 GLN N N 15 125.56 0.02 . 1 . . . . . . . . 5318 1 115 . 1 1 63 63 GLU H H 1 8.70 0.02 . 1 . . . . . . . . 5318 1 116 . 1 1 63 63 GLU N N 15 129.78 0.02 . 1 . . . . . . . . 5318 1 117 . 1 1 64 64 GLY H H 1 8.87 0.02 . 1 . . . . . . . . 5318 1 118 . 1 1 64 64 GLY N N 15 116.06 0.02 . 1 . . . . . . . . 5318 1 119 . 1 1 65 65 GLN H H 1 8.99 0.02 . 1 . . . . . . . . 5318 1 120 . 1 1 65 65 GLN N N 15 126.41 0.02 . 1 . . . . . . . . 5318 1 121 . 1 1 66 66 THR H H 1 7.69 0.02 . 1 . . . . . . . . 5318 1 122 . 1 1 66 66 THR N N 15 113.11 0.02 . 1 . . . . . . . . 5318 1 123 . 1 1 67 67 VAL H H 1 8.69 0.02 . 1 . . . . . . . . 5318 1 124 . 1 1 67 67 VAL N N 15 117.21 0.02 . 1 . . . . . . . . 5318 1 125 . 1 1 68 68 MET H H 1 8.98 0.02 . 1 . . . . . . . . 5318 1 126 . 1 1 68 68 MET N N 15 121.56 0.02 . 1 . . . . . . . . 5318 1 127 . 1 1 69 69 LEU H H 1 8.44 0.02 . 1 . . . . . . . . 5318 1 128 . 1 1 69 69 LEU N N 15 125.65 0.02 . 1 . . . . . . . . 5318 1 129 . 1 1 70 70 GLY H H 1 9.31 0.02 . 1 . . . . . . . . 5318 1 130 . 1 1 70 70 GLY N N 15 118.27 0.02 . 1 . . . . . . . . 5318 1 131 . 1 1 71 71 ASN H H 1 8.79 0.02 . 1 . . . . . . . . 5318 1 132 . 1 1 71 71 ASN N N 15 124.77 0.02 . 1 . . . . . . . . 5318 1 133 . 1 1 72 72 SER H H 1 8.20 0.02 . 1 . . . . . . . . 5318 1 134 . 1 1 72 72 SER N N 15 118.12 0.02 . 1 . . . . . . . . 5318 1 135 . 1 1 73 73 GLU H H 1 7.90 0.02 . 1 . . . . . . . . 5318 1 136 . 1 1 73 73 GLU N N 15 124.10 0.02 . 1 . . . . . . . . 5318 1 137 . 1 1 74 74 PHE H H 1 9.02 0.02 . 1 . . . . . . . . 5318 1 138 . 1 1 74 74 PHE N N 15 120.29 0.02 . 1 . . . . . . . . 5318 1 139 . 1 1 75 75 ASP H H 1 9.34 0.02 . 1 . . . . . . . . 5318 1 140 . 1 1 75 75 ASP N N 15 119.71 0.02 . 1 . . . . . . . . 5318 1 141 . 1 1 76 76 SER H H 1 7.32 0.02 . 1 . . . . . . . . 5318 1 142 . 1 1 76 76 SER N N 15 105.72 0.02 . 1 . . . . . . . . 5318 1 143 . 1 1 77 77 LEU H H 1 9.17 0.02 . 1 . . . . . . . . 5318 1 144 . 1 1 77 77 LEU N N 15 122.71 0.02 . 1 . . . . . . . . 5318 1 145 . 1 1 78 78 VAL H H 1 7.83 0.02 . 1 . . . . . . . . 5318 1 146 . 1 1 78 78 VAL N N 15 116.69 0.02 . 1 . . . . . . . . 5318 1 147 . 1 1 79 79 ASP H H 1 7.70 0.02 . 1 . . . . . . . . 5318 1 148 . 1 1 79 79 ASP N N 15 121.61 0.02 . 1 . . . . . . . . 5318 1 149 . 1 1 80 80 LEU H H 1 7.29 0.02 . 1 . . . . . . . . 5318 1 150 . 1 1 80 80 LEU N N 15 123.37 0.02 . 1 . . . . . . . . 5318 1 151 . 1 1 81 81 ILE H H 1 7.76 0.02 . 1 . . . . . . . . 5318 1 152 . 1 1 81 81 ILE N N 15 119.52 0.02 . 1 . . . . . . . . 5318 1 153 . 1 1 82 82 SER H H 1 7.98 0.02 . 1 . . . . . . . . 5318 1 154 . 1 1 82 82 SER N N 15 112.73 0.02 . 1 . . . . . . . . 5318 1 155 . 1 1 83 83 TYR H H 1 7.82 0.02 . 1 . . . . . . . . 5318 1 156 . 1 1 83 83 TYR N N 15 121.94 0.02 . 1 . . . . . . . . 5318 1 157 . 1 1 84 84 TYR H H 1 7.63 0.02 . 1 . . . . . . . . 5318 1 158 . 1 1 84 84 TYR N N 15 118.88 0.02 . 1 . . . . . . . . 5318 1 159 . 1 1 85 85 GLU H H 1 7.40 0.02 . 1 . . . . . . . . 5318 1 160 . 1 1 85 85 GLU N N 15 117.13 0.02 . 1 . . . . . . . . 5318 1 161 . 1 1 86 86 LYS H H 1 7.07 0.02 . 1 . . . . . . . . 5318 1 162 . 1 1 86 86 LYS N N 15 116.67 0.02 . 1 . . . . . . . . 5318 1 163 . 1 1 87 87 HIS H H 1 7.72 0.02 . 1 . . . . . . . . 5318 1 164 . 1 1 87 87 HIS N N 15 120.01 0.02 . 1 . . . . . . . . 5318 1 165 . 1 1 89 89 LEU H H 1 8.38 0.02 . 1 . . . . . . . . 5318 1 166 . 1 1 89 89 LEU N N 15 123.90 0.02 . 1 . . . . . . . . 5318 1 167 . 1 1 90 90 TYR H H 1 6.80 0.02 . 1 . . . . . . . . 5318 1 168 . 1 1 90 90 TYR N N 15 118.04 0.02 . 1 . . . . . . . . 5318 1 169 . 1 1 91 91 ARG H H 1 8.86 0.02 . 1 . . . . . . . . 5318 1 170 . 1 1 91 91 ARG N N 15 125.86 0.02 . 1 . . . . . . . . 5318 1 171 . 1 1 92 92 LYS H H 1 8.30 0.02 . 1 . . . . . . . . 5318 1 172 . 1 1 92 92 LYS N N 15 119.53 0.02 . 1 . . . . . . . . 5318 1 173 . 1 1 93 93 MET H H 1 8.76 0.02 . 1 . . . . . . . . 5318 1 174 . 1 1 93 93 MET N N 15 124.41 0.02 . 1 . . . . . . . . 5318 1 175 . 1 1 94 94 LYS H H 1 7.94 0.02 . 1 . . . . . . . . 5318 1 176 . 1 1 94 94 LYS N N 15 127.34 0.02 . 1 . . . . . . . . 5318 1 177 . 1 1 95 95 LEU H H 1 8.24 0.02 . 1 . . . . . . . . 5318 1 178 . 1 1 95 95 LEU N N 15 119.48 0.02 . 1 . . . . . . . . 5318 1 179 . 1 1 96 96 ARG H H 1 8.40 0.02 . 1 . . . . . . . . 5318 1 180 . 1 1 96 96 ARG N N 15 121.45 0.02 . 1 . . . . . . . . 5318 1 181 . 1 1 97 97 TYR H H 1 7.68 0.02 . 1 . . . . . . . . 5318 1 182 . 1 1 97 97 TYR N N 15 117.95 0.02 . 1 . . . . . . . . 5318 1 183 . 1 1 99 99 ILE H H 1 8.24 0.02 . 1 . . . . . . . . 5318 1 184 . 1 1 99 99 ILE N N 15 124.05 0.02 . 1 . . . . . . . . 5318 1 185 . 1 1 100 100 ASN H H 1 8.46 0.02 . 1 . . . . . . . . 5318 1 186 . 1 1 100 100 ASN N N 15 125.30 0.02 . 1 . . . . . . . . 5318 1 187 . 1 1 101 101 GLU H H 1 8.47 0.02 . 1 . . . . . . . . 5318 1 188 . 1 1 101 101 GLU N N 15 120.18 0.02 . 1 . . . . . . . . 5318 1 189 . 1 1 102 102 GLU H H 1 8.39 0.02 . 1 . . . . . . . . 5318 1 190 . 1 1 102 102 GLU N N 15 121.28 0.02 . 1 . . . . . . . . 5318 1 191 . 1 1 103 103 ASN H H 1 8.33 0.02 . 1 . . . . . . . . 5318 1 192 . 1 1 103 103 ASN N N 15 119.12 0.02 . 1 . . . . . . . . 5318 1 193 . 1 1 104 104 SER H H 1 8.06 0.02 . 1 . . . . . . . . 5318 1 194 . 1 1 104 104 SER N N 15 115.20 0.02 . 1 . . . . . . . . 5318 1 195 . 1 1 105 105 SER H H 1 7.82 0.02 . 1 . . . . . . . . 5318 1 196 . 1 1 105 105 SER N N 15 123.22 0.02 . 1 . . . . . . . . 5318 1 stop_ save_