data_4888 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4888 _Entry.Title ; Backbone 1H and 15N Chemical Shift Assignment of c-Src SH3 in high salt solution ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-10-30 _Entry.Accession_date 2000-10-30 _Entry.Last_release_date 2002-01-23 _Entry.Original_release_date 2002-01-23 _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 Chunyu Wang . . . 4888 2 Norma Pawley . H. . 4888 3 Linda Nicholson . K. . 4888 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4888 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 70 4888 '1H chemical shifts' 70 4888 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 . . 2002-01-23 2000-10-30 original author . 4888 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4889 'c-Src SH3 RLP2 peptide complex' 4888 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4888 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21555253 _Citation.DOI . _Citation.PubMed_ID 11697910 _Citation.Full_citation . _Citation.Title 'The Role of Backbone Motions in Ligand Binding to the c-Src SH3 Domain' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 313 _Citation.Journal_issue 4 _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 873 _Citation.Page_last 887 _Citation.Year 2001 _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 Chunyu Wang . . . 4888 1 2 Norma Pawley . H. . 4888 1 3 Linda Nicholson . K. . 4888 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_SH3 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_SH3 _Assembly.Entry_ID 4888 _Assembly.ID 1 _Assembly.Name 'c-Src SH3 monomer' _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 present' _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 4888 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 'c-Src SH3' 1 $SH3 . . . native . . . . . 4888 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'c-Src SH3 monomer' system 4888 1 SH3 abbreviation 4888 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'binds proline rich motifs' 4888 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_SH3 _Entity.Sf_category entity _Entity.Sf_framecode SH3 _Entity.Entry_ID 4888 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Src Homology 3 domain' _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 ; AGGVTTFVALYDYESRTETD LSFKKGERLQIVNNTEGDWW LAHSLTTGQTGYIPSNYVAP SDSIQAEGIHRD ; _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 72 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _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 2015-01-29 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 16750 . c-src_SH3 . . . . . 81.94 80 98.31 100.00 1.77e-34 . . . . 4888 1 2 no BMRB 3433 . "Src tyrosine kinase" . . . . . 83.33 64 100.00 100.00 1.52e-35 . . . . 4888 1 3 no PDB 1FMK . "Crystal Structure Of Human Tyrosine-Protein Kinase C-Src" . . . . . 88.89 452 98.44 100.00 5.53e-35 . . . . 4888 1 4 no PDB 1KSW . "Structure Of Human C-Src Tyrosine Kinase (Thr338gly Mutant) In Complex With N6-Benzyl Adp" . . . . . 88.89 452 98.44 100.00 5.87e-35 . . . . 4888 1 5 no PDB 1NLO . "Structure Of Signal Transduction Protein, Nmr, Minimized Average Structure" . . . . . 83.33 64 100.00 100.00 1.36e-35 . . . . 4888 1 6 no PDB 1NLP . "Structure Of Signal Transduction Protein, Nmr, Minimized Average Structure" . . . . . 83.33 64 100.00 100.00 1.36e-35 . . . . 4888 1 7 no PDB 1PRL . "Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions" . . . . . 84.72 64 100.00 100.00 3.28e-36 . . . . 4888 1 8 no PDB 1PRM . "Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions" . . . . . 84.72 64 100.00 100.00 3.28e-36 . . . . 4888 1 9 no PDB 1QWE . "C-Src Sh3 Domain Complexed With Ligand App12" . . . . . 83.33 64 100.00 100.00 1.36e-35 . . . . 4888 1 10 no PDB 1QWF . "C-Src Sh3 Domain Complexed With Ligand Vsl12" . . . . . 83.33 64 100.00 100.00 1.36e-35 . . . . 4888 1 11 no PDB 1RLP . "Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions" . . . . . 84.72 64 100.00 100.00 3.28e-36 . . . . 4888 1 12 no PDB 1RLQ . "Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions" . . . . . 84.72 64 100.00 100.00 3.28e-36 . . . . 4888 1 13 no PDB 1SRL . "1h And 15n Assignments And Secondary Structure Of The Src Sh3 Domain" . . . . . 84.72 64 100.00 100.00 3.28e-36 . . . . 4888 1 14 no PDB 1SRM . "1h And 15n Assignments And Secondary Structure Of The Src Sh3 Domain" . . . . . 84.72 64 100.00 100.00 3.28e-36 . . . . 4888 1 15 no PDB 1Y57 . "Structure Of Unphosphorylated C-Src In Complex With An Inhibitor" . . . . . 88.89 452 98.44 100.00 5.70e-35 . . . . 4888 1 16 no PDB 2H8H . "Src Kinase In Complex With A Quinazoline Inhibitor" . . . . . 93.06 535 98.51 100.00 4.22e-37 . . . . 4888 1 17 no PDB 2PTK . "Chicken Src Tyrosine Kinase" . . . . . 91.67 453 100.00 100.00 6.34e-37 . . . . 4888 1 18 no PDB 2SRC . "Crystal Structure Of Human Tyrosine-protein Kinase C-src, In Complex With Amp-pnp" . . . . . 88.89 452 98.44 100.00 5.53e-35 . . . . 4888 1 19 no PDB 3FJ5 . "Crystal Structure Of The C-Src-Sh3 Domain" . . . . . 77.78 57 98.21 100.00 4.12e-32 . . . . 4888 1 20 no PDB 4K11 . "The Structure Of 1na In Complex With Src T338g" . . . . . 87.50 448 98.41 100.00 2.34e-34 . . . . 4888 1 21 no DBJ BAE26865 . "unnamed protein product [Mus musculus]" . . . . . 93.06 535 98.51 100.00 4.26e-37 . . . . 4888 1 22 no DBJ BAI47379 . "v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [synthetic construct]" . . . . . 93.06 536 98.51 100.00 4.28e-37 . . . . 4888 1 23 no EMBL CAA23696 . "pp60-c-src protein [Gallus gallus]" . . . . . 93.06 533 100.00 100.00 1.81e-37 . . . . 4888 1 24 no EMBL CAA33404 . "unnamed protein product [Rous sarcoma virus]" . . . . . 93.06 526 98.51 98.51 4.53e-36 . . . . 4888 1 25 no EMBL CAA36154 . "scr [Rous sarcoma virus]" . . . . . 93.06 526 97.01 97.01 9.65e-35 . . . . 4888 1 26 no EMBL CAA36156 . "src protein [Avian sarcoma virus]" . . . . . 93.06 587 100.00 100.00 3.23e-37 . . . . 4888 1 27 no EMBL CAA37004 . "v-3src-1 [Rous sarcoma virus]" . . . . . 93.06 526 98.51 98.51 4.44e-36 . . . . 4888 1 28 no GB AAA42565 . "src-p60 phosphoprotein [Rous sarcoma virus]" . . . . . 93.06 526 100.00 100.00 1.63e-37 . . . . 4888 1 29 no GB AAA42571 . "src-p60 phoshoprotein [Rous sarcoma virus]" . . . . . 93.06 204 98.51 98.51 6.07e-38 . . . . 4888 1 30 no GB AAA42583 . "p66-src protein [Rous sarcoma virus]" . . . . . 93.06 587 100.00 100.00 3.23e-37 . . . . 4888 1 31 no GB AAA49078 . "pp60c-scr [Gallus gallus]" . . . . . 93.06 193 100.00 100.00 5.56e-40 . . . . 4888 1 32 no GB AAA60584 . "pp60 c-src-1 protein [Homo sapiens]" . . . . . 93.06 536 98.51 100.00 4.28e-37 . . . . 4888 1 33 no REF NP_001020566 . "neuronal proto-oncogene tyrosine-protein kinase Src isoform 2 [Mus musculus]" . . . . . 93.06 535 98.51 100.00 4.35e-37 . . . . 4888 1 34 no REF NP_001104274 . "proto-oncogene tyrosine-protein kinase Src [Bos taurus]" . . . . . 93.06 542 97.01 100.00 1.78e-36 . . . . 4888 1 35 no REF NP_001248263 . "v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [Macaca mulatta]" . . . . . 93.06 536 98.51 100.00 4.28e-37 . . . . 4888 1 36 no REF NP_005408 . "proto-oncogene tyrosine-protein kinase Src [Homo sapiens]" . . . . . 93.06 536 98.51 100.00 4.28e-37 . . . . 4888 1 37 no REF NP_056888 . "p60 src [Rous sarcoma virus]" . . . . . 93.06 526 98.51 98.51 5.20e-36 . . . . 4888 1 38 no SP P00523 . "RecName: Full=Proto-oncogene tyrosine-protein kinase Src; AltName: Full=Proto-oncogene c-Src; AltName: Full=pp60c-src; Short=p6" . . . . . 93.06 533 100.00 100.00 1.81e-37 . . . . 4888 1 39 no SP P00524 . "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src [Rous sarco" . . . . . 93.06 526 100.00 100.00 1.63e-37 . . . . 4888 1 40 no SP P00525 . "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src [Avian sarc" . . . . . 93.06 526 100.00 100.00 1.63e-37 . . . . 4888 1 41 no SP P00526 . "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src [Rous sarco" . . . . . 93.06 526 98.51 98.51 5.20e-36 . . . . 4888 1 42 no SP P12931 . "RecName: Full=Proto-oncogene tyrosine-protein kinase Src; AltName: Full=Proto-oncogene c-Src; AltName: Full=pp60c-src; Short=p6" . . . . . 93.06 536 98.51 100.00 4.28e-37 . . . . 4888 1 43 no TPG DAA23281 . "TPA: v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [Bos taurus]" . . . . . 93.06 542 97.01 100.00 1.78e-36 . . . . 4888 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID SH3 abbreviation 4888 1 'Src Homology 3 domain' common 4888 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 . ALA . 4888 1 2 . GLY . 4888 1 3 . GLY . 4888 1 4 . VAL . 4888 1 5 . THR . 4888 1 6 . THR . 4888 1 7 . PHE . 4888 1 8 . VAL . 4888 1 9 . ALA . 4888 1 10 . LEU . 4888 1 11 . TYR . 4888 1 12 . ASP . 4888 1 13 . TYR . 4888 1 14 . GLU . 4888 1 15 . SER . 4888 1 16 . ARG . 4888 1 17 . THR . 4888 1 18 . GLU . 4888 1 19 . THR . 4888 1 20 . ASP . 4888 1 21 . LEU . 4888 1 22 . SER . 4888 1 23 . PHE . 4888 1 24 . LYS . 4888 1 25 . LYS . 4888 1 26 . GLY . 4888 1 27 . GLU . 4888 1 28 . ARG . 4888 1 29 . LEU . 4888 1 30 . GLN . 4888 1 31 . ILE . 4888 1 32 . VAL . 4888 1 33 . ASN . 4888 1 34 . ASN . 4888 1 35 . THR . 4888 1 36 . GLU . 4888 1 37 . GLY . 4888 1 38 . ASP . 4888 1 39 . TRP . 4888 1 40 . TRP . 4888 1 41 . LEU . 4888 1 42 . ALA . 4888 1 43 . HIS . 4888 1 44 . SER . 4888 1 45 . LEU . 4888 1 46 . THR . 4888 1 47 . THR . 4888 1 48 . GLY . 4888 1 49 . GLN . 4888 1 50 . THR . 4888 1 51 . GLY . 4888 1 52 . TYR . 4888 1 53 . ILE . 4888 1 54 . PRO . 4888 1 55 . SER . 4888 1 56 . ASN . 4888 1 57 . TYR . 4888 1 58 . VAL . 4888 1 59 . ALA . 4888 1 60 . PRO . 4888 1 61 . SER . 4888 1 62 . ASP . 4888 1 63 . SER . 4888 1 64 . ILE . 4888 1 65 . GLN . 4888 1 66 . ALA . 4888 1 67 . GLU . 4888 1 68 . GLY . 4888 1 69 . ILE . 4888 1 70 . HIS . 4888 1 71 . ARG . 4888 1 72 . ASP . 4888 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 . ALA 1 1 4888 1 . GLY 2 2 4888 1 . GLY 3 3 4888 1 . VAL 4 4 4888 1 . THR 5 5 4888 1 . THR 6 6 4888 1 . PHE 7 7 4888 1 . VAL 8 8 4888 1 . ALA 9 9 4888 1 . LEU 10 10 4888 1 . TYR 11 11 4888 1 . ASP 12 12 4888 1 . TYR 13 13 4888 1 . GLU 14 14 4888 1 . SER 15 15 4888 1 . ARG 16 16 4888 1 . THR 17 17 4888 1 . GLU 18 18 4888 1 . THR 19 19 4888 1 . ASP 20 20 4888 1 . LEU 21 21 4888 1 . SER 22 22 4888 1 . PHE 23 23 4888 1 . LYS 24 24 4888 1 . LYS 25 25 4888 1 . GLY 26 26 4888 1 . GLU 27 27 4888 1 . ARG 28 28 4888 1 . LEU 29 29 4888 1 . GLN 30 30 4888 1 . ILE 31 31 4888 1 . VAL 32 32 4888 1 . ASN 33 33 4888 1 . ASN 34 34 4888 1 . THR 35 35 4888 1 . GLU 36 36 4888 1 . GLY 37 37 4888 1 . ASP 38 38 4888 1 . TRP 39 39 4888 1 . TRP 40 40 4888 1 . LEU 41 41 4888 1 . ALA 42 42 4888 1 . HIS 43 43 4888 1 . SER 44 44 4888 1 . LEU 45 45 4888 1 . THR 46 46 4888 1 . THR 47 47 4888 1 . GLY 48 48 4888 1 . GLN 49 49 4888 1 . THR 50 50 4888 1 . GLY 51 51 4888 1 . TYR 52 52 4888 1 . ILE 53 53 4888 1 . PRO 54 54 4888 1 . SER 55 55 4888 1 . ASN 56 56 4888 1 . TYR 57 57 4888 1 . VAL 58 58 4888 1 . ALA 59 59 4888 1 . PRO 60 60 4888 1 . SER 61 61 4888 1 . ASP 62 62 4888 1 . SER 63 63 4888 1 . ILE 64 64 4888 1 . GLN 65 65 4888 1 . ALA 66 66 4888 1 . GLU 67 67 4888 1 . GLY 68 68 4888 1 . ILE 69 69 4888 1 . HIS 70 70 4888 1 . ARG 71 71 4888 1 . ASP 72 72 4888 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 4888 _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 $SH3 . 9031 . . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 4888 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 4888 _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 $SH3 . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4888 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4888 _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 'Src Homology 3 domain' [U-N15] . . 1 $SH3 . . 1 . . mM . . . . 4888 1 2 'sodium phosphate' . . . . . . . 50 . . mM . . . . 4888 1 3 'sodium sulphate' . . . . . . . 200 . . mM . . . . 4888 1 4 DTT . . . . . . . 10 . . mM . . . . 4888 1 5 pepstatin . . . . . . . 5 . . mg/ml . . . . 4888 1 6 EDTA . . . . . . . 50 . . uM . . . . 4888 1 7 benzamidine . . . . . . . 10 . . ug/ml . . . . 4888 1 8 chloramphenicol . . . . . . . 50 . . uM . . . . 4888 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 4888 _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 6.5 0.2 n/a 4888 1 temperature 298 1 K 4888 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Software.Sf_category software _Software.Sf_framecode NMRpipe _Software.Entry_ID 4888 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . 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 4888 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4888 _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 NMR_spectrometer Varian INOVA . 600 . . . 4888 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 4888 _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 '1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4888 1 2 '1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4888 1 3 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4888 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 4888 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4888 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4888 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_sh3_unlig _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode sh3_unlig _Assigned_chem_shift_list.Entry_ID 4888 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4888 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 ALA H H 1 8.21 0.02 . 1 . . . . . . . . 4888 1 2 . 1 1 1 1 ALA N N 15 125.05 0.2 . 1 . . . . . . . . 4888 1 3 . 1 1 2 2 GLY H H 1 8.29 0.02 . 1 . . . . . . . . 4888 1 4 . 1 1 2 2 GLY N N 15 107.03 0.2 . 1 . . . . . . . . 4888 1 5 . 1 1 3 3 GLY H H 1 8.18 0.02 . 1 . . . . . . . . 4888 1 6 . 1 1 3 3 GLY N N 15 107.57 0.2 . 1 . . . . . . . . 4888 1 7 . 1 1 4 4 VAL H H 1 7.94 0.02 . 1 . . . . . . . . 4888 1 8 . 1 1 4 4 VAL N N 15 118.71 0.2 . 1 . . . . . . . . 4888 1 9 . 1 1 5 5 THR H H 1 8.39 0.02 . 1 . . . . . . . . 4888 1 10 . 1 1 5 5 THR N N 15 118.63 0.2 . 1 . . . . . . . . 4888 1 11 . 1 1 6 6 THR H H 1 8.3 0.02 . 1 . . . . . . . . 4888 1 12 . 1 1 6 6 THR N N 15 118.82 0.2 . 1 . . . . . . . . 4888 1 13 . 1 1 7 7 PHE H H 1 9.41 0.02 . 1 . . . . . . . . 4888 1 14 . 1 1 7 7 PHE N N 15 126.65 0.2 . 1 . . . . . . . . 4888 1 15 . 1 1 8 8 VAL H H 1 9.43 0.02 . 1 . . . . . . . . 4888 1 16 . 1 1 8 8 VAL N N 15 118.75 0.2 . 1 . . . . . . . . 4888 1 17 . 1 1 9 9 ALA H H 1 8.45 0.02 . 1 . . . . . . . . 4888 1 18 . 1 1 9 9 ALA N N 15 126.85 0.2 . 1 . . . . . . . . 4888 1 19 . 1 1 10 10 LEU H H 1 9.36 0.02 . 1 . . . . . . . . 4888 1 20 . 1 1 10 10 LEU N N 15 125.47 0.2 . 1 . . . . . . . . 4888 1 21 . 1 1 11 11 TYR H H 1 7.12 0.02 . 1 . . . . . . . . 4888 1 22 . 1 1 11 11 TYR N N 15 111.13 0.2 . 1 . . . . . . . . 4888 1 23 . 1 1 12 12 ASP H H 1 8.25 0.02 . 1 . . . . . . . . 4888 1 24 . 1 1 12 12 ASP N N 15 117 0.2 . 1 . . . . . . . . 4888 1 25 . 1 1 13 13 TYR H H 1 8.6 0.02 . 1 . . . . . . . . 4888 1 26 . 1 1 13 13 TYR N N 15 120.97 0.2 . 1 . . . . . . . . 4888 1 27 . 1 1 14 14 GLU H H 1 7.4 0.02 . 1 . . . . . . . . 4888 1 28 . 1 1 14 14 GLU N N 15 128.19 0.2 . 1 . . . . . . . . 4888 1 29 . 1 1 15 15 SER H H 1 8.11 0.02 . 1 . . . . . . . . 4888 1 30 . 1 1 15 15 SER N N 15 117.66 0.2 . 1 . . . . . . . . 4888 1 31 . 1 1 16 16 ARG H H 1 9.71 0.02 . 1 . . . . . . . . 4888 1 32 . 1 1 16 16 ARG N N 15 124.88 0.2 . 1 . . . . . . . . 4888 1 33 . 1 1 17 17 THR H H 1 8.38 0.02 . 1 . . . . . . . . 4888 1 34 . 1 1 17 17 THR N N 15 113.17 0.2 . 1 . . . . . . . . 4888 1 35 . 1 1 18 18 GLU H H 1 8.83 0.02 . 1 . . . . . . . . 4888 1 36 . 1 1 18 18 GLU N N 15 119.3 0.2 . 1 . . . . . . . . 4888 1 37 . 1 1 19 19 THR H H 1 7.73 0.02 . 1 . . . . . . . . 4888 1 38 . 1 1 19 19 THR N N 15 104.57 0.2 . 1 . . . . . . . . 4888 1 39 . 1 1 20 20 ASP H H 1 7.87 0.02 . 1 . . . . . . . . 4888 1 40 . 1 1 20 20 ASP N N 15 123.39 0.2 . 1 . . . . . . . . 4888 1 41 . 1 1 21 21 LEU H H 1 8.61 0.02 . 1 . . . . . . . . 4888 1 42 . 1 1 21 21 LEU N N 15 124.11 0.2 . 1 . . . . . . . . 4888 1 43 . 1 1 22 22 SER H H 1 7.96 0.02 . 1 . . . . . . . . 4888 1 44 . 1 1 22 22 SER N N 15 116.8 0.2 . 1 . . . . . . . . 4888 1 45 . 1 1 23 23 PHE H H 1 8.58 0.02 . 1 . . . . . . . . 4888 1 46 . 1 1 23 23 PHE N N 15 116.65 0.2 . 1 . . . . . . . . 4888 1 47 . 1 1 24 24 LYS H H 1 8.63 0.02 . 1 . . . . . . . . 4888 1 48 . 1 1 24 24 LYS N N 15 119.48 0.2 . 1 . . . . . . . . 4888 1 49 . 1 1 25 25 LYS H H 1 9.17 0.02 . 1 . . . . . . . . 4888 1 50 . 1 1 25 25 LYS N N 15 120.9 0.2 . 1 . . . . . . . . 4888 1 51 . 1 1 26 26 GLY H H 1 9.07 0.02 . 1 . . . . . . . . 4888 1 52 . 1 1 26 26 GLY N N 15 114.16 0.2 . 1 . . . . . . . . 4888 1 53 . 1 1 27 27 GLU H H 1 8.33 0.02 . 1 . . . . . . . . 4888 1 54 . 1 1 27 27 GLU N N 15 123.27 0.2 . 1 . . . . . . . . 4888 1 55 . 1 1 28 28 ARG H H 1 8.03 0.02 . 1 . . . . . . . . 4888 1 56 . 1 1 28 28 ARG N N 15 121.48 0.2 . 1 . . . . . . . . 4888 1 57 . 1 1 29 29 LEU H H 1 9.18 0.02 . 1 . . . . . . . . 4888 1 58 . 1 1 29 29 LEU N N 15 123.49 0.2 . 1 . . . . . . . . 4888 1 59 . 1 1 30 30 GLN H H 1 9.15 0.02 . 1 . . . . . . . . 4888 1 60 . 1 1 30 30 GLN N N 15 121.4 0.2 . 1 . . . . . . . . 4888 1 61 . 1 1 31 31 ILE H H 1 9.07 0.02 . 1 . . . . . . . . 4888 1 62 . 1 1 31 31 ILE N N 15 125.89 0.2 . 1 . . . . . . . . 4888 1 63 . 1 1 32 32 VAL H H 1 8.72 0.02 . 1 . . . . . . . . 4888 1 64 . 1 1 32 32 VAL N N 15 127.55 0.2 . 1 . . . . . . . . 4888 1 65 . 1 1 33 33 ASN H H 1 7.68 0.02 . 1 . . . . . . . . 4888 1 66 . 1 1 33 33 ASN N N 15 115.78 0.2 . 1 . . . . . . . . 4888 1 67 . 1 1 34 34 ASN H H 1 8.35 0.02 . 1 . . . . . . . . 4888 1 68 . 1 1 34 34 ASN N N 15 123.09 0.2 . 1 . . . . . . . . 4888 1 69 . 1 1 35 35 THR H H 1 7.89 0.02 . 1 . . . . . . . . 4888 1 70 . 1 1 35 35 THR N N 15 110.72 0.2 . 1 . . . . . . . . 4888 1 71 . 1 1 36 36 GLU H H 1 8.51 0.02 . 1 . . . . . . . . 4888 1 72 . 1 1 36 36 GLU N N 15 121.51 0.2 . 1 . . . . . . . . 4888 1 73 . 1 1 37 37 GLY H H 1 8.34 0.02 . 1 . . . . . . . . 4888 1 74 . 1 1 37 37 GLY N N 15 107.41 0.2 . 1 . . . . . . . . 4888 1 75 . 1 1 38 38 ASP H H 1 8.55 0.02 . 1 . . . . . . . . 4888 1 76 . 1 1 38 38 ASP N N 15 118.24 0.2 . 1 . . . . . . . . 4888 1 77 . 1 1 39 39 TRP H H 1 7.73 0.02 . 1 . . . . . . . . 4888 1 78 . 1 1 39 39 TRP N N 15 120.59 0.2 . 1 . . . . . . . . 4888 1 79 . 1 1 40 40 TRP H H 1 9.12 0.02 . 1 . . . . . . . . 4888 1 80 . 1 1 40 40 TRP N N 15 124.45 0.2 . 1 . . . . . . . . 4888 1 81 . 1 1 41 41 LEU H H 1 8.82 0.02 . 1 . . . . . . . . 4888 1 82 . 1 1 41 41 LEU N N 15 125.25 0.2 . 1 . . . . . . . . 4888 1 83 . 1 1 42 42 ALA H H 1 9.07 0.02 . 1 . . . . . . . . 4888 1 84 . 1 1 42 42 ALA N N 15 131.61 0.2 . 1 . . . . . . . . 4888 1 85 . 1 1 43 43 HIS H H 1 9.09 0.02 . 1 . . . . . . . . 4888 1 86 . 1 1 43 43 HIS N N 15 117.53 0.2 . 1 . . . . . . . . 4888 1 87 . 1 1 44 44 SER H H 1 8.84 0.02 . 1 . . . . . . . . 4888 1 88 . 1 1 44 44 SER N N 15 119.3 0.2 . 1 . . . . . . . . 4888 1 89 . 1 1 45 45 LEU H H 1 8.82 0.02 . 1 . . . . . . . . 4888 1 90 . 1 1 45 45 LEU N N 15 130.09 0.2 . 1 . . . . . . . . 4888 1 91 . 1 1 46 46 THR H H 1 8.33 0.02 . 1 . . . . . . . . 4888 1 92 . 1 1 46 46 THR N N 15 115.17 0.2 . 1 . . . . . . . . 4888 1 93 . 1 1 47 47 THR H H 1 8.26 0.02 . 1 . . . . . . . . 4888 1 94 . 1 1 47 47 THR N N 15 107.73 0.2 . 1 . . . . . . . . 4888 1 95 . 1 1 48 48 GLY H H 1 7.87 0.02 . 1 . . . . . . . . 4888 1 96 . 1 1 48 48 GLY N N 15 110.35 0.2 . 1 . . . . . . . . 4888 1 97 . 1 1 49 49 GLN H H 1 7.43 0.02 . 1 . . . . . . . . 4888 1 98 . 1 1 49 49 GLN N N 15 118.62 0.2 . 1 . . . . . . . . 4888 1 99 . 1 1 50 50 THR H H 1 8.54 0.02 . 1 . . . . . . . . 4888 1 100 . 1 1 50 50 THR N N 15 116.1 0.2 . 1 . . . . . . . . 4888 1 101 . 1 1 51 51 GLY H H 1 9.07 0.02 . 1 . . . . . . . . 4888 1 102 . 1 1 51 51 GLY N N 15 111.8 0.2 . 1 . . . . . . . . 4888 1 103 . 1 1 52 52 TYR H H 1 8.92 0.02 . 1 . . . . . . . . 4888 1 104 . 1 1 52 52 TYR N N 15 119.34 0.2 . 1 . . . . . . . . 4888 1 105 . 1 1 53 53 ILE H H 1 9.45 0.02 . 1 . . . . . . . . 4888 1 106 . 1 1 53 53 ILE N N 15 111.93 0.2 . 1 . . . . . . . . 4888 1 107 . 1 1 55 55 SER H H 1 7.63 0.02 . 1 . . . . . . . . 4888 1 108 . 1 1 55 55 SER N N 15 121.02 0.2 . 1 . . . . . . . . 4888 1 109 . 1 1 56 56 ASN H H 1 7.98 0.02 . 1 . . . . . . . . 4888 1 110 . 1 1 56 56 ASN N N 15 114.53 0.2 . 1 . . . . . . . . 4888 1 111 . 1 1 57 57 TYR H H 1 7.89 0.02 . 1 . . . . . . . . 4888 1 112 . 1 1 57 57 TYR N N 15 119.29 0.2 . 1 . . . . . . . . 4888 1 113 . 1 1 58 58 VAL H H 1 7.12 0.02 . 1 . . . . . . . . 4888 1 114 . 1 1 58 58 VAL N N 15 107.53 0.2 . 1 . . . . . . . . 4888 1 115 . 1 1 59 59 ALA H H 1 8.68 0.02 . 1 . . . . . . . . 4888 1 116 . 1 1 59 59 ALA N N 15 121.68 0.2 . 1 . . . . . . . . 4888 1 117 . 1 1 61 61 SER H H 1 8.38 0.02 . 1 . . . . . . . . 4888 1 118 . 1 1 61 61 SER N N 15 117.43 0.2 . 1 . . . . . . . . 4888 1 119 . 1 1 62 62 ASP H H 1 8.31 0.02 . 1 . . . . . . . . 4888 1 120 . 1 1 62 62 ASP N N 15 120.04 0.2 . 1 . . . . . . . . 4888 1 121 . 1 1 63 63 SER H H 1 7.91 0.02 . 1 . . . . . . . . 4888 1 122 . 1 1 63 63 SER N N 15 114.29 0.2 . 1 . . . . . . . . 4888 1 123 . 1 1 64 64 ILE H H 1 8.05 0.02 . 1 . . . . . . . . 4888 1 124 . 1 1 64 64 ILE N N 15 122.22 0.2 . 1 . . . . . . . . 4888 1 125 . 1 1 65 65 GLN H H 1 8.35 0.02 . 1 . . . . . . . . 4888 1 126 . 1 1 65 65 GLN N N 15 123.09 0.2 . 1 . . . . . . . . 4888 1 127 . 1 1 66 66 ALA H H 1 8.07 0.02 . 1 . . . . . . . . 4888 1 128 . 1 1 66 66 ALA N N 15 124.19 0.2 . 1 . . . . . . . . 4888 1 129 . 1 1 67 67 GLU H H 1 8.17 0.02 . 1 . . . . . . . . 4888 1 130 . 1 1 67 67 GLU N N 15 119.41 0.2 . 1 . . . . . . . . 4888 1 131 . 1 1 68 68 GLY H H 1 8.29 0.02 . 1 . . . . . . . . 4888 1 132 . 1 1 68 68 GLY N N 15 108.19 0.2 . 1 . . . . . . . . 4888 1 133 . 1 1 69 69 ILE H H 1 7.67 0.02 . 1 . . . . . . . . 4888 1 134 . 1 1 69 69 ILE N N 15 119.01 0.2 . 1 . . . . . . . . 4888 1 135 . 1 1 70 70 HIS H H 1 8.42 0.02 . 1 . . . . . . . . 4888 1 136 . 1 1 70 70 HIS N N 15 123.47 0.2 . 1 . . . . . . . . 4888 1 137 . 1 1 71 71 ARG H H 1 8.26 0.02 . 1 . . . . . . . . 4888 1 138 . 1 1 71 71 ARG N N 15 123.92 0.2 . 1 . . . . . . . . 4888 1 139 . 1 1 72 72 ASP H H 1 8.02 0.02 . 1 . . . . . . . . 4888 1 140 . 1 1 72 72 ASP N N 15 127.53 0.2 . 1 . . . . . . . . 4888 1 stop_ save_