data_2950 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assessment of cheY binding regions using 2D NMR and paramagnetic ligands ; _BMRB_accession_number 2950 _BMRB_flat_file_name bmr2950.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kar L. . . 2 'de Croos' P. Z. . 3 Roman S. J. . 4 Matsumura P. . . 5 Johnson M. E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 19 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-17 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kar L. . . 2 'de Croos' P. Z. . 3 Roman S. J. . 4 Matsumura P. . . 5 Johnson M. E. . stop_ _Journal_abbreviation 'Proteins Struct. Dyn. Design' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 68 _Page_last 73 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_che_Y_protein _Saveframe_category molecular_system _Mol_system_name 'che Y protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'che Y protein' $che_Y_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_che_Y_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'che Y protein' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; MADKELKFLVVDDFSTMRRI VRNLLKELGFNNVEEAEDGV DALNKLQAGGYGFVISDWNM PNMDGLELLKTIRADGAMSA LPVLMVTAEAKKENIIAAAQ AGASGYVVKPFTAATLEEKL NKIFEKLGM ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 LYS 5 GLU 6 LEU 7 LYS 8 PHE 9 LEU 10 VAL 11 VAL 12 ASP 13 ASP 14 PHE 15 SER 16 THR 17 MET 18 ARG 19 ARG 20 ILE 21 VAL 22 ARG 23 ASN 24 LEU 25 LEU 26 LYS 27 GLU 28 LEU 29 GLY 30 PHE 31 ASN 32 ASN 33 VAL 34 GLU 35 GLU 36 ALA 37 GLU 38 ASP 39 GLY 40 VAL 41 ASP 42 ALA 43 LEU 44 ASN 45 LYS 46 LEU 47 GLN 48 ALA 49 GLY 50 GLY 51 TYR 52 GLY 53 PHE 54 VAL 55 ILE 56 SER 57 ASP 58 TRP 59 ASN 60 MET 61 PRO 62 ASN 63 MET 64 ASP 65 GLY 66 LEU 67 GLU 68 LEU 69 LEU 70 LYS 71 THR 72 ILE 73 ARG 74 ALA 75 ASP 76 GLY 77 ALA 78 MET 79 SER 80 ALA 81 LEU 82 PRO 83 VAL 84 LEU 85 MET 86 VAL 87 THR 88 ALA 89 GLU 90 ALA 91 LYS 92 LYS 93 GLU 94 ASN 95 ILE 96 ILE 97 ALA 98 ALA 99 ALA 100 GLN 101 ALA 102 GLY 103 ALA 104 SER 105 GLY 106 TYR 107 VAL 108 VAL 109 LYS 110 PRO 111 PHE 112 THR 113 ALA 114 ALA 115 THR 116 LEU 117 GLU 118 GLU 119 LYS 120 LEU 121 ASN 122 LYS 123 ILE 124 PHE 125 GLU 126 LYS 127 LEU 128 GLY 129 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 2951 "che Y protein" 100.00 129 100.00 100.00 1.38e-85 BMRB 3440 "che Y protein" 99.22 129 99.22 100.00 1.68e-84 BMRB 4083 "E. coli CheY" 99.22 128 100.00 100.00 7.24e-85 BMRB 4472 "Chemotaxis protein Y" 100.00 129 100.00 100.00 1.38e-85 PDB 1A0O "Chey-Binding Domain Of Chea In Complex With Chey" 99.22 128 100.00 100.00 7.24e-85 PDB 1AB5 "Structure Of Chey Mutant F14n, V21t" 96.90 125 98.40 98.40 1.56e-80 PDB 1AB6 "Structure Of Chey Mutant F14n, V86t" 96.90 125 98.40 98.40 1.56e-80 PDB 1BDJ "Complex Structure Of Hpt Domain And Chey" 99.22 128 100.00 100.00 7.24e-85 PDB 1C4W "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" 99.22 128 99.22 99.22 1.05e-83 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 3.57e-84 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 7.24e-85 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 1.68e-84 PDB 1D4Z "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" 99.22 128 99.22 100.00 1.44e-84 PDB 1DJM "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" 100.00 129 100.00 100.00 1.38e-85 PDB 1E6K "Two-Component Signal Transduction System D12a Mutant Of Chey" 99.22 130 98.44 99.22 2.69e-83 PDB 1E6L "Two-Component Signal Transduction System D13a Mutant Of Chey" 98.45 127 99.21 99.21 4.95e-83 PDB 1E6M "Two-Component Signal Transduction System D57a Mutant Of Chey" 99.22 128 98.44 99.22 3.27e-83 PDB 1EAY "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" 99.22 128 100.00 100.00 7.24e-85 PDB 1EHC "Structure Of Signal Transduction Protein Chey" 99.22 128 99.22 99.22 7.83e-84 PDB 1F4V "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" 99.22 128 100.00 100.00 7.24e-85 PDB 1FFG "Chey-binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" 99.22 128 100.00 100.00 7.24e-85 PDB 1FFS "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" 99.22 128 100.00 100.00 7.24e-85 PDB 1FFW "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" 99.22 128 100.00 100.00 7.24e-85 PDB 1FQW "Crystal Structure Of Activated Chey" 99.22 128 100.00 100.00 7.24e-85 PDB 1JBE "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" 99.22 128 98.44 98.44 1.19e-82 PDB 1KMI "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" 100.00 129 100.00 100.00 1.38e-85 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 1.06e-84 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 6.22e-84 PDB 1YMU "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" 99.22 130 98.44 99.22 3.61e-83 PDB 1ZDM "Crystal Structure Of Activated Chey Bound To Xe" 100.00 129 99.22 99.22 1.46e-84 PDB 2B1J "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" 99.22 128 100.00 100.00 7.24e-85 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 3.17e-83 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 3.17e-83 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 5.06e-84 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 5.06e-84 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 5.06e-84 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 5.06e-84 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 5.06e-84 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 5.06e-84 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 5.06e-84 PDB 2ID7 "1.75 A Structure Of T87i Phosphono-Chey" 99.22 128 98.44 98.44 9.96e-83 PDB 2ID9 "1.85 A Structure Of T87i/y106w Phosphono-chey" 99.22 128 97.66 98.44 6.17e-82 PDB 2IDM "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" 99.22 128 97.66 98.44 6.17e-82 PDB 2LP4 "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" 99.22 128 100.00 100.00 7.24e-85 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 3.17e-83 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 3.17e-83 PDB 3CHY "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" 99.22 128 100.00 100.00 7.24e-85 PDB 3F7N "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 7.76e-81 PDB 3FFT "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" 99.22 128 98.44 98.44 1.23e-82 PDB 3FFW "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 1.86e-81 PDB 3FFX "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 6.73e-82 PDB 3FGZ "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 2.39e-81 PDB 3MYY "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" 99.22 128 99.22 99.22 5.40e-84 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 5.95e-85 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 5.33e-85 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 3.37e-85 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 1.05e-84 PDB 3OO0 "Structure Of Apo Chey A113p" 100.00 129 99.22 99.22 7.48e-85 PDB 3OO1 "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" 100.00 129 99.22 99.22 7.48e-85 PDB 3RVJ "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" 100.00 132 98.45 100.00 1.18e-84 PDB 3RVK "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" 100.00 132 98.45 100.00 1.18e-84 PDB 3RVL "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.45 99.22 3.23e-84 PDB 3RVM "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.45 99.22 3.23e-84 PDB 3RVN "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" 100.00 132 98.45 99.22 5.58e-84 PDB 3RVO "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" 100.00 132 98.45 99.22 5.58e-84 PDB 3RVP "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" 100.00 132 98.45 100.00 2.63e-84 PDB 3RVQ "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" 100.00 132 98.45 100.00 2.63e-84 PDB 3RVR "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" 100.00 132 98.45 99.22 3.23e-84 PDB 3RVS "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" 100.00 132 98.45 99.22 3.23e-84 PDB 5CHY "Structure Of Chemotaxis Protein Chey" 99.22 128 99.22 100.00 8.00e-84 PDB 6CHY "Structure Of Chemotaxis Protein Chey" 99.22 128 98.44 99.22 6.65e-83 DBJ BAA15698 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K12 substr. W3110]" 100.00 129 100.00 100.00 1.38e-85 DBJ BAB36015 "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 1.38e-85 DBJ BAG77641 "chemotactic response regulator CheY [Escherichia coli SE11]" 100.00 129 100.00 100.00 1.38e-85 DBJ BAI25973 "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O26:H11 str. 11368]" 100.00 129 100.00 100.00 1.38e-85 DBJ BAI30936 "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O103:H2 str. 12009]" 100.00 129 100.00 100.00 1.38e-85 EMBL CAD05667 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.67 99.22 5.06e-84 EMBL CAP76371 "chemotaxis protein cheY [Escherichia coli LF82]" 100.00 129 100.00 100.00 1.38e-85 EMBL CAQ32359 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" 100.00 129 100.00 100.00 1.38e-85 EMBL CAQ98822 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" 100.00 129 100.00 100.00 1.38e-85 EMBL CAR03242 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" 100.00 129 99.22 100.00 4.24e-85 GB AAA23570 "cheY protein [Escherichia coli]" 100.00 129 99.22 99.22 7.48e-85 GB AAA23577 "CheY [Escherichia coli]" 100.00 129 100.00 100.00 1.38e-85 GB AAA27037 "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 129 97.67 99.22 5.06e-84 GB AAC74952 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" 100.00 129 100.00 100.00 1.38e-85 GB AAG56872 "chemotaxis regulator transmits chemoreceptor signals to flagelllar motor components [Escherichia coli O157:H7 str. EDL933]" 100.00 129 100.00 100.00 1.38e-85 PIR AH0745 "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 129 97.67 99.22 5.06e-84 REF NP_310619 "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 1.38e-85 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 1.38e-85 REF NP_456482 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.67 99.22 5.06e-84 REF NP_460873 "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 129 97.67 99.22 5.06e-84 REF NP_707777 "chemotaxis regulatory protein CheY [Shigella flexneri 2a str. 301]" 100.00 129 100.00 100.00 1.38e-85 SP P0A2D5 "RecName: Full=Chemotaxis protein CheY" 100.00 129 97.67 99.22 5.06e-84 SP P0A2D6 "RecName: Full=Chemotaxis protein CheY" 100.00 129 97.67 99.22 5.06e-84 SP P0AE67 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 1.38e-85 SP P0AE68 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 1.38e-85 SP P0AE69 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 1.38e-85 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $che_Y_protein 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $che_Y_protein 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 . na temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'che Y protein' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 58 TRP HA H 5.46 . 1 2 . 58 TRP HB2 H 4.54 . 1 3 . 58 TRP HB3 H 4.27 . 1 4 . 58 TRP HD1 H 7.28 . 1 5 . 58 TRP HE1 H 10.32 . 1 6 . 58 TRP HE3 H 7.37 . 1 7 . 58 TRP HZ2 H 7.49 . 1 8 . 58 TRP HZ3 H 6.75 . 1 9 . 58 TRP HH2 H 7.27 . 1 10 . 87 THR HA H 5.1 . 1 11 . 87 THR HB H 4.1 . 1 12 . 87 THR HG2 H .94 . 1 13 . 106 TYR HA H 5.87 . 1 14 . 106 TYR HB2 H 2.37 . 1 15 . 106 TYR HB3 H 2.73 . 1 16 . 106 TYR HD1 H 6.75 . 1 17 . 106 TYR HD2 H 6.75 . 1 18 . 106 TYR HE1 H 6.58 . 1 19 . 106 TYR HE2 H 6.58 . 1 stop_ save_