data_2950 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 2950 _Entry.Title ; Assessment of cheY binding regions using 2D NMR and paramagnetic ligands ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _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 L. Kar . . . 2950 2 P. 'de Croos' . Z. . 2950 3 S. Roman . J. . 2950 4 P. Matsumura . . . 2950 5 M. Johnson . E. . 2950 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 2950 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 21 2950 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 4 . . 2010-06-17 . revision BMRB 'Complete natural source information' 2950 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 2950 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 2950 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 2950 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 2950 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kar, L., de Croos, P.Z., Roman, S.J., Matsumura, P., Johnson, M. E., "Assessment of cheY binding regions using 2D NMR and paramagnetic ligands," Proteins Struct. Dyn. Design, 68-73 (1991). ; _Citation.Title 'Assessment of cheY binding regions using 2D NMR and paramagnetic ligands' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proteins Struct. Dyn. Design' _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 68 _Citation.Page_last 73 _Citation.Year 1991 _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 L. Kar . . . 2950 1 2 P. 'de Croos' . Z. . 2950 1 3 S. Roman . J. . 2950 1 4 P. Matsumura . . . 2950 1 5 M. Johnson . E. . 2950 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_che_Y_protein _Assembly.Sf_category assembly _Assembly.Sf_framecode system_che_Y_protein _Assembly.Entry_ID 2950 _Assembly.ID 1 _Assembly.Name 'che Y protein' _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 . _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 'che Y protein' 1 $che_Y_protein . . . . . . . . . 2950 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'che Y protein' system 2950 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_che_Y_protein _Entity.Sf_category entity _Entity.Sf_framecode che_Y_protein _Entity.Entry_ID 2950 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'che Y protein' _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 ; MADKELKFLVVDDFSTMRRI VRNLLKELGFNNVEEAEDGV DALNKLQAGGYGFVISDWNM PNMDGLELLKTIRADGAMSA LPVLMVTAEAKKENIIAAAQ AGASGYVVKPFTAATLEEKL NKIFEKLGM ; _Entity.Polymer_seq_one_letter_code ; MADKELKFLVVDDFSTMRRI VRNLLKELGFNNVEEAEDGV DALNKLQAGGYGFVISDWNM PNMDGLELLKTIRADGAMSA LPVLMVTAEAKKENIIAAAQ AGASGYVVKPFTAATLEEKL NKIFEKLGM ; _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 129 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 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 2951 . "che Y protein" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 2 no BMRB 3440 . "che Y protein" . . . . . 99.22 129 99.22 100.00 1.78e-84 . . . . 2950 1 3 no BMRB 4083 . "E. coli CheY" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 4 no BMRB 4472 . "Chemotaxis protein Y" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 5 no PDB 1A0O . "Chey-Binding Domain Of Chea In Complex With Chey" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 6 no PDB 1AB5 . "Structure Of Chey Mutant F14n, V21t" . . . . . 96.90 125 98.40 98.40 1.65e-80 . . . . 2950 1 7 no PDB 1AB6 . "Structure Of Chey Mutant F14n, V86t" . . . . . 96.90 125 98.40 98.40 1.65e-80 . . . . 2950 1 8 no PDB 1BDJ . "Complex Structure Of Hpt Domain And Chey" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 9 no PDB 1C4W . "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" . . . . . 99.22 128 99.22 99.22 1.11e-83 . . . . 2950 1 10 no PDB 1CEY . "Assignments, Secondary Structure, Global Fold, And Dynamics Of Chemotaxis Y Protein Using Three-And Four-Dimensional Heteronucl" . . . . . 98.45 128 100.00 100.00 3.78e-84 . . . . 2950 1 11 no PDB 1CHN . "Magnesium Binding To The Bacterial Chemotaxis Protein Chey Results In Large Conformational Changes Involving Its Functional Sur" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 12 no PDB 1CYE . "Three Dimensional Structure Of Chemotactic Che Y Protein In Aqueous Solution By Nuclear Magnetic Resonance Methods" . . . . . 99.22 129 99.22 100.00 1.78e-84 . . . . 2950 1 13 no PDB 1D4Z . "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" . . . . . 99.22 128 99.22 100.00 1.53e-84 . . . . 2950 1 14 no PDB 1DJM . "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 15 no PDB 1E6K . "Two-Component Signal Transduction System D12a Mutant Of Chey" . . . . . 99.22 130 98.44 99.22 2.85e-83 . . . . 2950 1 16 no PDB 1E6L . "Two-Component Signal Transduction System D13a Mutant Of Chey" . . . . . 98.45 127 99.21 99.21 5.25e-83 . . . . 2950 1 17 no PDB 1E6M . "Two-Component Signal Transduction System D57a Mutant Of Chey" . . . . . 99.22 128 98.44 99.22 3.47e-83 . . . . 2950 1 18 no PDB 1EAY . "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 19 no PDB 1EHC . "Structure Of Signal Transduction Protein Chey" . . . . . 99.22 128 99.22 99.22 8.29e-84 . . . . 2950 1 20 no PDB 1F4V . "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 21 no PDB 1FFG . "Chey-binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 22 no PDB 1FFS . "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 23 no PDB 1FFW . "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 24 no PDB 1FQW . "Crystal Structure Of Activated Chey" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 25 no PDB 1JBE . "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" . . . . . 99.22 128 98.44 98.44 1.26e-82 . . . . 2950 1 26 no PDB 1KMI . "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 27 no PDB 1MIH . "A Role For Chey Glu 89 In Chez-Mediated Dephosphorylation Of The E. Coli Chemotaxis Response Regulator Chey" . . . . . 100.00 129 99.22 99.22 1.12e-84 . . . . 2950 1 28 no PDB 1VLZ . "Uncoupled Phosphorylation And Activation In Bacterial Chemotaxis: The 2.1 Angstrom Structure Of A Threonine To Isoleucine Mutan" . . . . . 99.22 128 99.22 99.22 6.59e-84 . . . . 2950 1 29 no PDB 1YMU . "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" . . . . . 99.22 130 98.44 99.22 3.82e-83 . . . . 2950 1 30 no PDB 1ZDM . "Crystal Structure Of Activated Chey Bound To Xe" . . . . . 100.00 129 99.22 99.22 1.54e-84 . . . . 2950 1 31 no PDB 2B1J . "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 32 no PDB 2CHE . "Structure Of The Mg2+-Bound Form Of Chey And Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 2950 1 33 no PDB 2CHF . "Structure Of The Mg2+-Bound Form Of Chey And The Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 2950 1 34 no PDB 2FKA . "Crystal Structure Of Mg(2+) And Bef(3)(-)-Bound Chey In Complex With Chez(200-214) Solved From A F432 Crystal Grown In Caps (Ph" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 35 no PDB 2FLK . "Crystal Structure Of Chey In Complex With Chez(200-214) Solved From A F432 Crystal Grown In Caps (Ph 10.5)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 36 no PDB 2FLW . "Crystal Structure Of Mg2+ And Bef3- Ound Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Hepes (ph 7.5)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 37 no PDB 2FMF . "Crystal Structure Of Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Hepes (ph 7.5)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 38 no PDB 2FMH . "Crystal Structure Of Mg2+ And Bef3- Bound Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Tris (Ph 8.4)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 39 no PDB 2FMI . "Crystal Structure Of Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Tris (Ph 8.4)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 40 no PDB 2FMK . "Crystal Structure Of Mg2+ And Bef3- Bound Chey In Complex With Chez 200-214 Solved From A P2(1)2(1)2 Crystal Grown In Mes (Ph 6" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 41 no PDB 2ID7 . "1.75 A Structure Of T87i Phosphono-Chey" . . . . . 99.22 128 98.44 98.44 1.06e-82 . . . . 2950 1 42 no PDB 2ID9 . "1.85 A Structure Of T87i/y106w Phosphono-chey" . . . . . 99.22 128 97.66 98.44 6.53e-82 . . . . 2950 1 43 no PDB 2IDM . "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" . . . . . 99.22 128 97.66 98.44 6.53e-82 . . . . 2950 1 44 no PDB 2LP4 . "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 45 no PDB 2PL9 . "Crystal Structure Of Chey-mg(2+)-bef(3)(-) In Complex With Chez(c19) Peptide Solved From A P2(1)2(1)2 Crystal" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 2950 1 46 no PDB 2PMC . "Crystal Structure Of Chey-mg(2+) In Complex With Chez(c15) Peptide Solved From A P1 Crystal" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 2950 1 47 no PDB 3CHY . "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 2950 1 48 no PDB 3F7N . "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 8.22e-81 . . . . 2950 1 49 no PDB 3FFT . "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" . . . . . 99.22 128 98.44 98.44 1.30e-82 . . . . 2950 1 50 no PDB 3FFW . "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 1.97e-81 . . . . 2950 1 51 no PDB 3FFX . "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 7.13e-82 . . . . 2950 1 52 no PDB 3FGZ . "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 2.53e-81 . . . . 2950 1 53 no PDB 3MYY . "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" . . . . . 99.22 128 99.22 99.22 5.72e-84 . . . . 2950 1 54 no PDB 3OLV . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88v-Bef3-Mg Complex" . . . . . 100.00 129 99.22 99.22 6.30e-85 . . . . 2950 1 55 no PDB 3OLW . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88t-Bef3-Mn Complex" . . . . . 100.00 129 99.22 99.22 5.65e-85 . . . . 2950 1 56 no PDB 3OLX . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88s-Bef3-Mn Complex" . . . . . 100.00 129 99.22 100.00 3.57e-85 . . . . 2950 1 57 no PDB 3OLY . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88m-Bef3-Mn Complex" . . . . . 100.00 129 99.22 99.22 1.11e-84 . . . . 2950 1 58 no PDB 3OO0 . "Structure Of Apo Chey A113p" . . . . . 100.00 129 99.22 99.22 7.93e-85 . . . . 2950 1 59 no PDB 3OO1 . "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" . . . . . 100.00 129 99.22 99.22 7.93e-85 . . . . 2950 1 60 no PDB 3RVJ . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" . . . . . 100.00 132 98.45 100.00 1.25e-84 . . . . 2950 1 61 no PDB 3RVK . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" . . . . . 100.00 132 98.45 100.00 1.25e-84 . . . . 2950 1 62 no PDB 3RVL . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 2950 1 63 no PDB 3RVM . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 2950 1 64 no PDB 3RVN . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" . . . . . 100.00 132 98.45 99.22 5.91e-84 . . . . 2950 1 65 no PDB 3RVO . "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" . . . . . 100.00 132 98.45 99.22 5.91e-84 . . . . 2950 1 66 no PDB 3RVP . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" . . . . . 100.00 132 98.45 100.00 2.78e-84 . . . . 2950 1 67 no PDB 3RVQ . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" . . . . . 100.00 132 98.45 100.00 2.78e-84 . . . . 2950 1 68 no PDB 3RVR . "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 2950 1 69 no PDB 3RVS . "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 2950 1 70 no PDB 5CHY . "Structure Of Chemotaxis Protein Chey" . . . . . 99.22 128 99.22 100.00 8.48e-84 . . . . 2950 1 71 no PDB 6CHY . "Structure Of Chemotaxis Protein Chey" . . . . . 99.22 128 98.44 99.22 7.05e-83 . . . . 2950 1 72 no DBJ BAA15698 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 73 no DBJ BAB36015 . "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 74 no DBJ BAG77641 . "chemotactic response regulator CheY [Escherichia coli SE11]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 75 no DBJ BAI25973 . "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 76 no DBJ BAI30936 . "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 77 no EMBL CAD05667 . "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 78 no EMBL CAP76371 . "chemotaxis protein cheY [Escherichia coli LF82]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 79 no EMBL CAQ32359 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 80 no EMBL CAQ98822 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 81 no EMBL CAR03242 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" . . . . . 100.00 129 99.22 100.00 4.49e-85 . . . . 2950 1 82 no GB AAA23570 . "cheY protein [Escherichia coli]" . . . . . 100.00 129 99.22 99.22 7.93e-85 . . . . 2950 1 83 no GB AAA23577 . "CheY [Escherichia coli]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 84 no GB AAA27037 . "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 85 no GB AAC74952 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 86 no GB AAG56872 . "chemotaxis regulator transmits chemoreceptor signals to flagelllar motor components [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 87 no PIR AH0745 . "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 88 no REF NP_310619 . "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 89 no REF NP_416396 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 90 no REF NP_456482 . "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 91 no REF NP_460873 . "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 92 no REF NP_707777 . "chemotaxis regulatory protein CheY [Shigella flexneri 2a str. 301]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 93 no SP P0A2D5 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 94 no SP P0A2D6 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 2950 1 95 no SP P0AE67 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 96 no SP P0AE68 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 97 no SP P0AE69 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 2950 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'che Y protein' common 2950 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 2950 1 2 . ALA . 2950 1 3 . ASP . 2950 1 4 . LYS . 2950 1 5 . GLU . 2950 1 6 . LEU . 2950 1 7 . LYS . 2950 1 8 . PHE . 2950 1 9 . LEU . 2950 1 10 . VAL . 2950 1 11 . VAL . 2950 1 12 . ASP . 2950 1 13 . ASP . 2950 1 14 . PHE . 2950 1 15 . SER . 2950 1 16 . THR . 2950 1 17 . MET . 2950 1 18 . ARG . 2950 1 19 . ARG . 2950 1 20 . ILE . 2950 1 21 . VAL . 2950 1 22 . ARG . 2950 1 23 . ASN . 2950 1 24 . LEU . 2950 1 25 . LEU . 2950 1 26 . LYS . 2950 1 27 . GLU . 2950 1 28 . LEU . 2950 1 29 . GLY . 2950 1 30 . PHE . 2950 1 31 . ASN . 2950 1 32 . ASN . 2950 1 33 . VAL . 2950 1 34 . GLU . 2950 1 35 . GLU . 2950 1 36 . ALA . 2950 1 37 . GLU . 2950 1 38 . ASP . 2950 1 39 . GLY . 2950 1 40 . VAL . 2950 1 41 . ASP . 2950 1 42 . ALA . 2950 1 43 . LEU . 2950 1 44 . ASN . 2950 1 45 . LYS . 2950 1 46 . LEU . 2950 1 47 . GLN . 2950 1 48 . ALA . 2950 1 49 . GLY . 2950 1 50 . GLY . 2950 1 51 . TYR . 2950 1 52 . GLY . 2950 1 53 . PHE . 2950 1 54 . VAL . 2950 1 55 . ILE . 2950 1 56 . SER . 2950 1 57 . ASP . 2950 1 58 . TRP . 2950 1 59 . ASN . 2950 1 60 . MET . 2950 1 61 . PRO . 2950 1 62 . ASN . 2950 1 63 . MET . 2950 1 64 . ASP . 2950 1 65 . GLY . 2950 1 66 . LEU . 2950 1 67 . GLU . 2950 1 68 . LEU . 2950 1 69 . LEU . 2950 1 70 . LYS . 2950 1 71 . THR . 2950 1 72 . ILE . 2950 1 73 . ARG . 2950 1 74 . ALA . 2950 1 75 . ASP . 2950 1 76 . GLY . 2950 1 77 . ALA . 2950 1 78 . MET . 2950 1 79 . SER . 2950 1 80 . ALA . 2950 1 81 . LEU . 2950 1 82 . PRO . 2950 1 83 . VAL . 2950 1 84 . LEU . 2950 1 85 . MET . 2950 1 86 . VAL . 2950 1 87 . THR . 2950 1 88 . ALA . 2950 1 89 . GLU . 2950 1 90 . ALA . 2950 1 91 . LYS . 2950 1 92 . LYS . 2950 1 93 . GLU . 2950 1 94 . ASN . 2950 1 95 . ILE . 2950 1 96 . ILE . 2950 1 97 . ALA . 2950 1 98 . ALA . 2950 1 99 . ALA . 2950 1 100 . GLN . 2950 1 101 . ALA . 2950 1 102 . GLY . 2950 1 103 . ALA . 2950 1 104 . SER . 2950 1 105 . GLY . 2950 1 106 . TYR . 2950 1 107 . VAL . 2950 1 108 . VAL . 2950 1 109 . LYS . 2950 1 110 . PRO . 2950 1 111 . PHE . 2950 1 112 . THR . 2950 1 113 . ALA . 2950 1 114 . ALA . 2950 1 115 . THR . 2950 1 116 . LEU . 2950 1 117 . GLU . 2950 1 118 . GLU . 2950 1 119 . LYS . 2950 1 120 . LEU . 2950 1 121 . ASN . 2950 1 122 . LYS . 2950 1 123 . ILE . 2950 1 124 . PHE . 2950 1 125 . GLU . 2950 1 126 . LYS . 2950 1 127 . LEU . 2950 1 128 . GLY . 2950 1 129 . MET . 2950 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 2950 1 . ALA 2 2 2950 1 . ASP 3 3 2950 1 . LYS 4 4 2950 1 . GLU 5 5 2950 1 . LEU 6 6 2950 1 . LYS 7 7 2950 1 . PHE 8 8 2950 1 . LEU 9 9 2950 1 . VAL 10 10 2950 1 . VAL 11 11 2950 1 . ASP 12 12 2950 1 . ASP 13 13 2950 1 . PHE 14 14 2950 1 . SER 15 15 2950 1 . THR 16 16 2950 1 . MET 17 17 2950 1 . ARG 18 18 2950 1 . ARG 19 19 2950 1 . ILE 20 20 2950 1 . VAL 21 21 2950 1 . ARG 22 22 2950 1 . ASN 23 23 2950 1 . LEU 24 24 2950 1 . LEU 25 25 2950 1 . LYS 26 26 2950 1 . GLU 27 27 2950 1 . LEU 28 28 2950 1 . GLY 29 29 2950 1 . PHE 30 30 2950 1 . ASN 31 31 2950 1 . ASN 32 32 2950 1 . VAL 33 33 2950 1 . GLU 34 34 2950 1 . GLU 35 35 2950 1 . ALA 36 36 2950 1 . GLU 37 37 2950 1 . ASP 38 38 2950 1 . GLY 39 39 2950 1 . VAL 40 40 2950 1 . ASP 41 41 2950 1 . ALA 42 42 2950 1 . LEU 43 43 2950 1 . ASN 44 44 2950 1 . LYS 45 45 2950 1 . LEU 46 46 2950 1 . GLN 47 47 2950 1 . ALA 48 48 2950 1 . GLY 49 49 2950 1 . GLY 50 50 2950 1 . TYR 51 51 2950 1 . GLY 52 52 2950 1 . PHE 53 53 2950 1 . VAL 54 54 2950 1 . ILE 55 55 2950 1 . SER 56 56 2950 1 . ASP 57 57 2950 1 . TRP 58 58 2950 1 . ASN 59 59 2950 1 . MET 60 60 2950 1 . PRO 61 61 2950 1 . ASN 62 62 2950 1 . MET 63 63 2950 1 . ASP 64 64 2950 1 . GLY 65 65 2950 1 . LEU 66 66 2950 1 . GLU 67 67 2950 1 . LEU 68 68 2950 1 . LEU 69 69 2950 1 . LYS 70 70 2950 1 . THR 71 71 2950 1 . ILE 72 72 2950 1 . ARG 73 73 2950 1 . ALA 74 74 2950 1 . ASP 75 75 2950 1 . GLY 76 76 2950 1 . ALA 77 77 2950 1 . MET 78 78 2950 1 . SER 79 79 2950 1 . ALA 80 80 2950 1 . LEU 81 81 2950 1 . PRO 82 82 2950 1 . VAL 83 83 2950 1 . LEU 84 84 2950 1 . MET 85 85 2950 1 . VAL 86 86 2950 1 . THR 87 87 2950 1 . ALA 88 88 2950 1 . GLU 89 89 2950 1 . ALA 90 90 2950 1 . LYS 91 91 2950 1 . LYS 92 92 2950 1 . GLU 93 93 2950 1 . ASN 94 94 2950 1 . ILE 95 95 2950 1 . ILE 96 96 2950 1 . ALA 97 97 2950 1 . ALA 98 98 2950 1 . ALA 99 99 2950 1 . GLN 100 100 2950 1 . ALA 101 101 2950 1 . GLY 102 102 2950 1 . ALA 103 103 2950 1 . SER 104 104 2950 1 . GLY 105 105 2950 1 . TYR 106 106 2950 1 . VAL 107 107 2950 1 . VAL 108 108 2950 1 . LYS 109 109 2950 1 . PRO 110 110 2950 1 . PHE 111 111 2950 1 . THR 112 112 2950 1 . ALA 113 113 2950 1 . ALA 114 114 2950 1 . THR 115 115 2950 1 . LEU 116 116 2950 1 . GLU 117 117 2950 1 . GLU 118 118 2950 1 . LYS 119 119 2950 1 . LEU 120 120 2950 1 . ASN 121 121 2950 1 . LYS 122 122 2950 1 . ILE 123 123 2950 1 . PHE 124 124 2950 1 . GLU 125 125 2950 1 . LYS 126 126 2950 1 . LEU 127 127 2950 1 . GLY 128 128 2950 1 . MET 129 129 2950 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 2950 _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 $che_Y_protein . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 2950 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 2950 _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 $che_Y_protein . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2950 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 2950 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 2950 _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 . na 2950 1 temperature 303 . K 2950 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 2950 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 2950 _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 unknown unknown . 0 'spectrometer information not available' . . 2950 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 2950 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 2950 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 2950 _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 . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 2950 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_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 2950 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _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_one . 2950 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 58 58 TRP HA H 1 5.46 . . 1 . . . . . . . . 2950 1 2 . 1 1 58 58 TRP HB2 H 1 4.54 . . 1 . . . . . . . . 2950 1 3 . 1 1 58 58 TRP HB3 H 1 4.27 . . 1 . . . . . . . . 2950 1 4 . 1 1 58 58 TRP HD1 H 1 7.28 . . 1 . . . . . . . . 2950 1 5 . 1 1 58 58 TRP HE1 H 1 10.32 . . 1 . . . . . . . . 2950 1 6 . 1 1 58 58 TRP HE3 H 1 7.37 . . 1 . . . . . . . . 2950 1 7 . 1 1 58 58 TRP HZ2 H 1 7.49 . . 1 . . . . . . . . 2950 1 8 . 1 1 58 58 TRP HZ3 H 1 6.75 . . 1 . . . . . . . . 2950 1 9 . 1 1 58 58 TRP HH2 H 1 7.27 . . 1 . . . . . . . . 2950 1 10 . 1 1 87 87 THR HA H 1 5.1 . . 1 . . . . . . . . 2950 1 11 . 1 1 87 87 THR HB H 1 4.1 . . 1 . . . . . . . . 2950 1 12 . 1 1 87 87 THR HG21 H 1 .94 . . 1 . . . . . . . . 2950 1 13 . 1 1 87 87 THR HG22 H 1 .94 . . 1 . . . . . . . . 2950 1 14 . 1 1 87 87 THR HG23 H 1 .94 . . 1 . . . . . . . . 2950 1 15 . 1 1 106 106 TYR HA H 1 5.87 . . 1 . . . . . . . . 2950 1 16 . 1 1 106 106 TYR HB2 H 1 2.37 . . 1 . . . . . . . . 2950 1 17 . 1 1 106 106 TYR HB3 H 1 2.73 . . 1 . . . . . . . . 2950 1 18 . 1 1 106 106 TYR HD1 H 1 6.75 . . 1 . . . . . . . . 2950 1 19 . 1 1 106 106 TYR HD2 H 1 6.75 . . 1 . . . . . . . . 2950 1 20 . 1 1 106 106 TYR HE1 H 1 6.58 . . 1 . . . . . . . . 2950 1 21 . 1 1 106 106 TYR HE2 H 1 6.58 . . 1 . . . . . . . . 2950 1 stop_ save_