data_18234 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of P1-CheY/P2 complex in bacterial chemotaxis ; _BMRB_accession_number 18234 _BMRB_flat_file_name bmr18234.str _Entry_type original _Submission_date 2012-02-01 _Accession_date 2012-02-01 _Entry_origination author _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 dahlquist Frederick . . 2 Mo Guoya . . 3 Zhou Hongjun . . 4 Kamamura Tetsuya . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 108 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-10-22 original author . stop_ _Original_release_date 2012-10-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of P1-CheY/P2 complex in bacterial chemotaxis' _Citation_status 'in preparation' _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 Mo Guoya . . 2 Zhou Hongjun . . 3 Kamamura Tetsuya . . 4 dahlquist Frederick . . stop_ _Journal_abbreviation Biochemistry _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'P1-CheY/P2 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CheA_P1P2 $CheA_P1P2 CheY $CheY stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CheA_P1P2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CheA_P1P2 _Molecular_mass 24991.010 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 225 _Mol_residue_sequence ; MSMDISDFYQTFFDEADELL ADMEQHLLDLVPESPDAEQL NAIFRAAHSIKGGAGTFGFT ILQETTHLMENLLDEARRGE MQLNTDIINLFLETKDIMQE QLDAYKNSEEPDAASFEYIC NALRQLALEAKGETPSAVTR LSVVAKSEPQDEQSRSQSPR RIILSRLKAGEVDLLEEELG HLTTLTDVVKGADSLSAILP GDIAEDDITAVLCFVIEADQ ITFET ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 MET 4 ASP 5 ILE 6 SER 7 ASP 8 PHE 9 TYR 10 GLN 11 THR 12 PHE 13 PHE 14 ASP 15 GLU 16 ALA 17 ASP 18 GLU 19 LEU 20 LEU 21 ALA 22 ASP 23 MET 24 GLU 25 GLN 26 HIS 27 LEU 28 LEU 29 ASP 30 LEU 31 VAL 32 PRO 33 GLU 34 SER 35 PRO 36 ASP 37 ALA 38 GLU 39 GLN 40 LEU 41 ASN 42 ALA 43 ILE 44 PHE 45 ARG 46 ALA 47 ALA 48 HIS 49 SER 50 ILE 51 LYS 52 GLY 53 GLY 54 ALA 55 GLY 56 THR 57 PHE 58 GLY 59 PHE 60 THR 61 ILE 62 LEU 63 GLN 64 GLU 65 THR 66 THR 67 HIS 68 LEU 69 MET 70 GLU 71 ASN 72 LEU 73 LEU 74 ASP 75 GLU 76 ALA 77 ARG 78 ARG 79 GLY 80 GLU 81 MET 82 GLN 83 LEU 84 ASN 85 THR 86 ASP 87 ILE 88 ILE 89 ASN 90 LEU 91 PHE 92 LEU 93 GLU 94 THR 95 LYS 96 ASP 97 ILE 98 MET 99 GLN 100 GLU 101 GLN 102 LEU 103 ASP 104 ALA 105 TYR 106 LYS 107 ASN 108 SER 109 GLU 110 GLU 111 PRO 112 ASP 113 ALA 114 ALA 115 SER 116 PHE 117 GLU 118 TYR 119 ILE 120 CYS 121 ASN 122 ALA 123 LEU 124 ARG 125 GLN 126 LEU 127 ALA 128 LEU 129 GLU 130 ALA 131 LYS 132 GLY 133 GLU 134 THR 135 PRO 136 SER 137 ALA 138 VAL 139 THR 140 ARG 141 LEU 142 SER 143 VAL 144 VAL 145 ALA 146 LYS 147 SER 148 GLU 149 PRO 150 GLN 151 ASP 152 GLU 153 GLN 154 SER 155 ARG 156 SER 157 GLN 158 SER 159 PRO 160 ARG 161 ARG 162 ILE 163 ILE 164 LEU 165 SER 166 ARG 167 LEU 168 LYS 169 ALA 170 GLY 171 GLU 172 VAL 173 ASP 174 LEU 175 LEU 176 GLU 177 GLU 178 GLU 179 LEU 180 GLY 181 HIS 182 LEU 183 THR 184 THR 185 LEU 186 THR 187 ASP 188 VAL 189 VAL 190 LYS 191 GLY 192 ALA 193 ASP 194 SER 195 LEU 196 SER 197 ALA 198 ILE 199 LEU 200 PRO 201 GLY 202 ASP 203 ILE 204 ALA 205 GLU 206 ASP 207 ASP 208 ILE 209 THR 210 ALA 211 VAL 212 LEU 213 CYS 214 PHE 215 VAL 216 ILE 217 GLU 218 ALA 219 ASP 220 GLN 221 ILE 222 THR 223 PHE 224 GLU 225 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 PDB 2LP4 "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" 100.00 225 100.00 100.00 3.75e-160 EMBL CQF39165 "chemotaxis protein CheA [Salmonella enterica subsp. enterica serovar Typhimurium str. DT104]" 58.67 147 100.00 100.00 6.79e-89 GB EIQ53621 "fused chemotactic sensory histidine kinase in two-component regulatory system with CheB and CheY [Shigella sonnei 4822-66]" 69.78 586 97.45 98.73 3.49e-98 REF WP_042351715 "chemotaxis protein CheA, partial [Escherichia coli]" 60.89 566 97.08 98.54 6.22e-83 stop_ save_ save_CheY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CheY _Molecular_mass 13981.248 _Mol_thiol_state 'not reported' _Details . _Residue_count 128 _Mol_residue_sequence ; ADKELKFLVVDDFSTMRRIV RNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMP NMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQA GASGYVVKPFTAATLEEKLN KIFEKLGM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 ASP 3 4 LYS 4 5 GLU 5 6 LEU 6 7 LYS 7 8 PHE 8 9 LEU 9 10 VAL 10 11 VAL 11 12 ASP 12 13 ASP 13 14 PHE 14 15 SER 15 16 THR 16 17 MET 17 18 ARG 18 19 ARG 19 20 ILE 20 21 VAL 21 22 ARG 22 23 ASN 23 24 LEU 24 25 LEU 25 26 LYS 26 27 GLU 27 28 LEU 28 29 GLY 29 30 PHE 30 31 ASN 31 32 ASN 32 33 VAL 33 34 GLU 34 35 GLU 35 36 ALA 36 37 GLU 37 38 ASP 38 39 GLY 39 40 VAL 40 41 ASP 41 42 ALA 42 43 LEU 43 44 ASN 44 45 LYS 45 46 LEU 46 47 GLN 47 48 ALA 48 49 GLY 49 50 GLY 50 51 TYR 51 52 GLY 52 53 PHE 53 54 VAL 54 55 ILE 55 56 SER 56 57 ASP 57 58 TRP 58 59 ASN 59 60 MET 60 61 PRO 61 62 ASN 62 63 MET 63 64 ASP 64 65 GLY 65 66 LEU 66 67 GLU 67 68 LEU 68 69 LEU 69 70 LYS 70 71 THR 71 72 ILE 72 73 ARG 73 74 ALA 74 75 ASP 75 76 GLY 76 77 ALA 77 78 MET 78 79 SER 79 80 ALA 80 81 LEU 81 82 PRO 82 83 VAL 83 84 LEU 84 85 MET 85 86 VAL 86 87 THR 87 88 ALA 88 89 GLU 89 90 ALA 90 91 LYS 91 92 LYS 92 93 GLU 93 94 ASN 94 95 ILE 95 96 ILE 96 97 ALA 97 98 ALA 98 99 ALA 99 100 GLN 100 101 ALA 101 102 GLY 102 103 ALA 103 104 SER 104 105 GLY 105 106 TYR 106 107 VAL 107 108 VAL 108 109 LYS 109 110 PRO 110 111 PHE 111 112 THR 112 113 ALA 113 114 ALA 114 115 THR 115 116 LEU 116 117 GLU 117 118 GLU 118 119 LYS 119 120 LEU 120 121 ASN 121 122 LYS 122 123 ILE 123 124 PHE 124 125 GLU 125 126 LYS 126 127 LEU 127 128 GLY 128 129 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 2950 "che Y protein" 100.00 129 100.00 100.00 5.18e-85 BMRB 2951 "che Y protein" 100.00 129 100.00 100.00 5.18e-85 BMRB 3440 "che Y protein" 100.00 129 99.22 100.00 1.38e-84 BMRB 4083 CheY 100.00 128 100.00 100.00 8.66e-85 BMRB 4472 CheY 100.00 129 100.00 100.00 5.18e-85 PDB 1A0O "Chey-Binding Domain Of Chea In Complex With Chey" 100.00 128 100.00 100.00 8.66e-85 PDB 1AB5 "Structure Of Chey Mutant F14n, V21t" 97.66 125 98.40 98.40 9.29e-81 PDB 1AB6 "Structure Of Chey Mutant F14n, V86t" 97.66 125 98.40 98.40 9.29e-81 PDB 1BDJ "Complex Structure Of Hpt Domain And Chey" 100.00 128 100.00 100.00 8.66e-85 PDB 1C4W "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" 100.00 128 99.22 99.22 7.20e-84 PDB 1CEY "Assignments, Secondary Structure, Global Fold, And Dynamics Of Chemotaxis Y Protein Using Three-And Four-Dimensional Heteronucl" 99.22 128 100.00 100.00 2.67e-84 PDB 1CHN "Magnesium Binding To The Bacterial Chemotaxis Protein Chey Results In Large Conformational Changes Involving Its Functional Sur" 100.00 128 100.00 100.00 8.66e-85 PDB 1CYE "Three Dimensional Structure Of Chemotactic Che Y Protein In Aqueous Solution By Nuclear Magnetic Resonance Methods" 100.00 129 99.22 100.00 1.38e-84 PDB 1D4Z "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" 100.00 128 99.22 100.00 1.37e-84 PDB 1DJM "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" 100.00 129 100.00 100.00 5.18e-85 PDB 1E6K "Two-Component Signal Transduction System D12a Mutant Of Chey" 100.00 130 98.44 99.22 1.82e-83 PDB 1E6L "Two-Component Signal Transduction System D13a Mutant Of Chey" 99.22 127 99.21 99.21 3.36e-83 PDB 1E6M "Two-Component Signal Transduction System D57a Mutant Of Chey" 100.00 128 98.44 99.22 2.15e-83 PDB 1EAY "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" 100.00 128 100.00 100.00 8.66e-85 PDB 1EHC "Structure Of Signal Transduction Protein Chey" 100.00 128 99.22 99.22 6.82e-84 PDB 1F4V "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" 100.00 128 100.00 100.00 8.66e-85 PDB 1FFG "Chey-Binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" 100.00 128 100.00 100.00 8.66e-85 PDB 1FFS "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" 100.00 128 100.00 100.00 8.66e-85 PDB 1FFW "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" 100.00 128 100.00 100.00 8.66e-85 PDB 1FQW "Crystal Structure Of Activated Chey" 100.00 128 100.00 100.00 8.66e-85 PDB 1JBE "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" 100.00 128 98.44 98.44 8.13e-83 PDB 1KMI "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" 100.00 129 100.00 100.00 5.18e-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 4.08e-84 PDB 1VLZ "Uncoupled Phosphorylation And Activation In Bacterial Chemotaxis: The 2.1 Angstrom Structure Of A Threonine To Isoleucine Mutan" 100.00 128 99.22 99.22 6.82e-84 PDB 1YMU "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" 100.00 130 98.44 99.22 4.04e-83 PDB 1ZDM "Crystal Structure Of Activated Chey Bound To Xe" 100.00 129 99.22 99.22 7.44e-84 PDB 2B1J "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" 100.00 128 100.00 100.00 8.66e-85 PDB 2CHE "Structure Of The Mg2+-Bound Form Of Chey And Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" 100.00 128 97.66 99.22 3.62e-83 PDB 2CHF "Structure Of The Mg2+-Bound Form Of Chey And The Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" 100.00 128 97.66 99.22 3.62e-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 97.66 99.22 2.24e-83 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 97.66 99.22 2.24e-83 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 97.66 99.22 2.24e-83 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 97.66 99.22 2.24e-83 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 97.66 99.22 2.24e-83 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 97.66 99.22 2.24e-83 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 97.66 99.22 2.24e-83 PDB 2ID7 "1.75 A Structure Of T87i Phosphono-Chey" 100.00 128 98.44 98.44 6.05e-83 PDB 2ID9 "1.85 A Structure Of T87i/y106w Phosphono-chey" 100.00 128 97.66 98.44 4.76e-82 PDB 2IDM "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" 100.00 128 97.66 98.44 4.76e-82 PDB 2LP4 "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" 100.00 128 100.00 100.00 8.66e-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" 100.00 128 97.66 99.22 3.62e-83 PDB 2PMC "Crystal Structure Of Chey-mg(2+) In Complex With Chez(c15) Peptide Solved From A P1 Crystal" 100.00 128 97.66 99.22 3.62e-83 PDB 3CHY "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" 100.00 128 100.00 100.00 8.66e-85 PDB 3F7N "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 5.37e-81 PDB 3FFT "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" 100.00 128 98.44 98.44 1.24e-82 PDB 3FFW "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 1.29e-81 PDB 3FFX "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 4.66e-82 PDB 3FGZ "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 1.88e-81 PDB 3MYY "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" 100.00 128 99.22 99.22 4.36e-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 2.39e-84 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 2.07e-84 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 1.45e-84 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 3.18e-84 PDB 3OO0 "Structure Of Apo Chey A113p" 100.00 129 99.22 99.22 3.86e-84 PDB 3OO1 "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" 100.00 129 99.22 99.22 3.86e-84 PDB 3RVJ "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" 100.00 132 98.44 100.00 5.72e-84 PDB 3RVK "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" 100.00 132 98.44 100.00 5.72e-84 PDB 3RVL "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.44 99.22 1.30e-83 PDB 3RVM "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.44 99.22 1.30e-83 PDB 3RVN "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" 100.00 132 98.44 99.22 2.22e-83 PDB 3RVO "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" 100.00 132 98.44 99.22 2.22e-83 PDB 3RVP "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" 100.00 132 98.44 100.00 1.04e-83 PDB 3RVQ "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" 100.00 132 98.44 100.00 1.04e-83 PDB 3RVR "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" 100.00 132 98.44 99.22 1.30e-83 PDB 3RVS "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" 100.00 132 98.44 99.22 1.30e-83 PDB 5CHY "Structure Of Chemotaxis Protein Chey" 100.00 128 99.22 100.00 4.55e-84 PDB 6CHY "Structure Of Chemotaxis Protein Chey" 100.00 128 98.44 99.22 3.87e-83 DBJ BAA15698 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. W3110]" 100.00 129 100.00 100.00 5.18e-85 DBJ BAB36015 "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 5.18e-85 DBJ BAG77641 "chemotactic response regulator CheY [Escherichia coli SE11]" 100.00 129 100.00 100.00 5.18e-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 5.18e-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 5.18e-85 EMBL CAD05667 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.66 99.22 2.24e-83 EMBL CAP76371 "chemotaxis protein cheY [Escherichia coli LF82]" 100.00 129 100.00 100.00 5.18e-85 EMBL CAQ32359 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" 100.00 129 100.00 100.00 5.18e-85 EMBL CAQ98822 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" 100.00 129 100.00 100.00 5.18e-85 EMBL CAR03242 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" 100.00 129 99.22 100.00 1.63e-84 GB AAA23570 "cheY protein [Escherichia coli]" 100.00 129 99.22 99.22 3.86e-84 GB AAA23577 "CheY [Escherichia coli]" 100.00 129 100.00 100.00 5.18e-85 GB AAA27037 "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 129 97.66 99.22 2.24e-83 GB AAC74952 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" 100.00 129 100.00 100.00 5.18e-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 5.18e-85 PIR AH0745 "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 129 97.66 99.22 2.24e-83 REF NP_288319 "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. EDL933]" 100.00 129 100.00 100.00 5.18e-85 REF NP_310619 "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 5.18e-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 5.18e-85 REF NP_456482 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.66 99.22 2.24e-83 REF NP_460873 "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 129 97.66 99.22 2.24e-83 SP P0A2D5 "RecName: Full=Chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 129 97.66 99.22 2.24e-83 SP P0A2D6 "RecName: Full=Chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi]" 100.00 129 97.66 99.22 2.24e-83 SP P0AE67 "RecName: Full=Chemotaxis protein CheY [Escherichia coli K-12]" 100.00 129 100.00 100.00 5.18e-85 SP P0AE68 "RecName: Full=Chemotaxis protein CheY [Escherichia coli O157:H7]" 100.00 129 100.00 100.00 5.18e-85 SP P0AE69 "RecName: Full=Chemotaxis protein CheY [Shigella flexneri]" 100.00 129 100.00 100.00 5.18e-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 $CheA_P1P2 'Escherichia coli' 562 Bacteria . Escherichia coli $CheY 'Escherichia coli' 562 Bacteria . 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 $CheA_P1P2 'recombinant technology' . Escherichia coli . pQE12 $CheY 'recombinant technology' . Escherichia coli . pCW stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '50 mM sodium phosphate, pH 6.5. 5 mM DTT, 0.2% sodium azide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CheY 200 mM '[U-15N; U-2H]' $CheA_P1P2 3000 mM [U-2H] $CheA_P1P2 250 mM [U-2H] 'sodium phosphate' 50 mM 'natural abundance' DTT 5 mM 'natural abundance' 'sodium azide' 0.2 % 'natural abundance' H2O 92 % 'natural abundance' D2O 8 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG3.3 _Saveframe_category software _Name ANSIG3.3 _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.5 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name CheY _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 3 2 ASP H H 8.589 0.02 1 2 3 2 ASP N N 121.39 0.2 1 3 4 3 LYS H H 8.529 0.02 1 4 4 3 LYS N N 122.47 0.2 1 5 5 4 GLU H H 8.702 0.02 1 6 5 4 GLU N N 119.02 0.2 1 7 6 5 LEU H H 7.530 0.02 1 8 6 5 LEU N N 124.23 0.2 1 9 7 6 LYS H H 8.486 0.02 1 10 7 6 LYS N N 126.09 0.2 1 11 8 7 PHE H H 9.206 0.02 1 12 8 7 PHE N N 128.54 0.2 1 13 9 8 LEU H H 8.827 0.02 1 14 9 8 LEU N N 121.92 0.2 1 15 10 9 VAL H H 8.983 0.02 1 16 10 9 VAL N N 127.28 0.2 1 17 11 10 VAL H H 9.251 0.02 1 18 11 10 VAL N N 127.25 0.2 1 19 12 11 ASP H H 8.144 0.02 1 20 12 11 ASP N N 123.77 0.2 1 21 13 12 ASP H H 9.709 0.02 1 22 13 12 ASP N N 124.94 0.2 1 23 15 14 SER H H 9.493 0.02 1 24 15 14 SER N N 126.80 0.2 1 25 16 15 THR H H 7.372 0.02 1 26 16 15 THR N N 116.70 0.2 1 27 17 16 MET H H 6.326 0.02 1 28 17 16 MET N N 119.00 0.2 1 29 18 17 ARG H H 7.515 0.02 1 30 18 17 ARG N N 116.67 0.2 1 31 19 18 ARG H H 7.638 0.02 1 32 19 18 ARG N N 116.98 0.2 1 33 20 19 ILE H H 7.789 0.02 1 34 20 19 ILE N N 120.79 0.2 1 35 21 20 VAL H H 8.389 0.02 1 36 21 20 VAL N N 119.34 0.2 1 37 22 21 ARG H H 8.622 0.02 1 38 22 21 ARG N N 119.43 0.2 1 39 24 23 LEU H H 8.490 0.02 1 40 24 23 LEU N N 123.39 0.2 1 41 26 25 LYS H H 7.932 0.02 1 42 26 25 LYS N N 120.62 0.2 1 43 27 26 GLU H H 7.985 0.02 1 44 27 26 GLU N N 122.29 0.2 1 45 28 27 LEU H H 7.431 0.02 1 46 28 27 LEU N N 117.21 0.2 1 47 29 28 GLY H H 7.735 0.02 1 48 29 28 GLY N N 106.17 0.2 1 49 30 29 PHE H H 8.188 0.02 1 50 30 29 PHE N N 121.14 0.2 1 51 31 30 ASN H H 8.305 0.02 1 52 31 30 ASN N N 118.22 0.2 1 53 32 31 ASN H H 9.874 0.02 1 54 32 31 ASN N N 124.51 0.2 1 55 33 32 VAL H H 7.522 0.02 1 56 33 32 VAL N N 122.03 0.2 1 57 34 33 GLU H H 9.124 0.02 1 58 34 33 GLU N N 126.88 0.2 1 59 35 34 GLU H H 8.933 0.02 1 60 35 34 GLU N N 120.80 0.2 1 61 36 35 ALA H H 8.878 0.02 1 62 36 35 ALA N N 120.50 0.2 1 63 37 36 GLU H H 9.476 0.02 1 64 37 36 GLU N N 117.42 0.2 1 65 38 37 ASP H H 7.450 0.02 1 66 38 37 ASP N N 131.50 0.2 1 67 39 38 GLY H H 8.148 0.02 1 68 39 38 GLY N N 102.39 0.2 1 69 40 39 VAL H H 7.962 0.02 1 70 40 39 VAL N N 122.62 0.2 1 71 41 40 ASP H H 8.518 0.02 1 72 41 40 ASP N N 121.11 0.2 1 73 42 41 ALA H H 8.337 0.02 1 74 42 41 ALA N N 116.97 0.2 1 75 43 42 LEU H H 8.121 0.02 1 76 43 42 LEU N N 118.28 0.2 1 77 46 45 LEU H H 8.748 0.02 1 78 46 45 LEU N N 118.53 0.2 1 79 47 46 GLN H H 7.865 0.02 1 80 47 46 GLN N N 116.82 0.2 1 81 48 47 ALA H H 7.611 0.02 1 82 48 47 ALA N N 120.46 0.2 1 83 49 48 GLY H H 7.574 0.02 1 84 49 48 GLY N N 104.28 0.2 1 85 50 49 GLY H H 8.367 0.02 1 86 50 49 GLY N N 103.81 0.2 1 87 51 50 TYR H H 8.126 0.02 1 88 51 50 TYR N N 118.74 0.2 1 89 52 51 GLY H H 9.556 0.02 1 90 52 51 GLY N N 106.90 0.2 1 91 53 52 PHE H H 7.527 0.02 1 92 53 52 PHE N N 121.38 0.2 1 93 54 53 VAL H H 8.246 0.02 1 94 54 53 VAL N N 127.15 0.2 1 95 55 54 ILE H H 9.235 0.02 1 96 55 54 ILE N N 128.13 0.2 1 97 56 55 SER H H 8.678 0.02 1 98 56 55 SER N N 118.20 0.2 1 99 57 56 ASP H H 8.412 0.02 1 100 57 56 ASP N N 127.29 0.2 1 101 59 58 ASN H H 8.716 0.02 1 102 59 58 ASN N N 116.98 0.2 1 103 62 61 ASN H H 8.598 0.02 1 104 62 61 ASN N N 112.14 0.2 1 105 63 62 MET H H 9.192 0.02 1 106 63 62 MET N N 122.95 0.2 1 107 64 63 ASP H H 8.518 0.02 1 108 64 63 ASP N N 126.54 0.2 1 109 66 65 LEU H H 7.733 0.02 1 110 66 65 LEU N N 121.87 0.2 1 111 67 66 GLU H H 8.085 0.02 1 112 67 66 GLU N N 119.47 0.2 1 113 68 67 LEU H H 8.299 0.02 1 114 68 67 LEU N N 123.91 0.2 1 115 69 68 LEU H H 8.249 0.02 1 116 69 68 LEU N N 120.64 0.2 1 117 70 69 LYS H H 8.400 0.02 1 118 70 69 LYS N N 116.08 0.2 1 119 71 70 THR H H 8.028 0.02 1 120 71 70 THR N N 117.49 0.2 1 121 72 71 ILE H H 8.459 0.02 1 122 72 71 ILE N N 123.64 0.2 1 123 73 72 ARG H H 8.112 0.02 1 124 73 72 ARG N N 113.35 0.2 1 125 74 73 ALA H H 7.286 0.02 1 126 74 73 ALA N N 118.90 0.2 1 127 75 74 ASP H H 7.399 0.02 1 128 75 74 ASP N N 121.87 0.2 1 129 76 75 GLY H H 8.728 0.02 1 130 76 75 GLY N N 112.23 0.2 1 131 77 76 ALA H H 8.558 0.02 1 132 77 76 ALA N N 121.97 0.2 1 133 78 77 MET H H 8.477 0.02 1 134 78 77 MET N N 116.18 0.2 1 135 79 78 SER H H 7.436 0.02 1 136 79 78 SER N N 112.91 0.2 1 137 80 79 ALA H H 8.246 0.02 1 138 80 79 ALA N N 123.08 0.2 1 139 81 80 LEU H H 7.816 0.02 1 140 81 80 LEU N N 124.13 0.2 1 141 83 82 VAL H H 7.731 0.02 1 142 83 82 VAL N N 118.86 0.2 1 143 84 83 LEU H H 9.135 0.02 1 144 84 83 LEU N N 130.45 0.2 1 145 85 84 MET H H 7.855 0.02 1 146 85 84 MET N N 124.08 0.2 1 147 86 85 VAL H H 9.198 0.02 1 148 86 85 VAL N N 124.81 0.2 1 149 87 86 THR H H 8.715 0.02 1 150 87 86 THR N N 116.56 0.2 1 151 88 87 ALA H H 8.807 0.02 1 152 88 87 ALA N N 125.46 0.2 1 153 90 89 ALA H H 9.090 0.02 1 154 90 89 ALA N N 129.99 0.2 1 155 91 90 LYS H H 7.197 0.02 1 156 91 90 LYS N N 121.03 0.2 1 157 93 92 GLU H H 9.648 0.02 1 158 93 92 GLU N N 116.28 0.2 1 159 94 93 ASN H H 7.116 0.02 1 160 94 93 ASN N N 117.03 0.2 1 161 95 94 ILE H H 7.546 0.02 1 162 95 94 ILE N N 121.11 0.2 1 163 96 95 ILE H H 8.172 0.02 1 164 96 95 ILE N N 117.16 0.2 1 165 97 96 ALA H H 7.541 0.02 1 166 97 96 ALA N N 120.06 0.2 1 167 98 97 ALA H H 8.524 0.02 1 168 98 97 ALA N N 119.15 0.2 1 169 100 99 GLN H H 8.974 0.02 1 170 100 99 GLN N N 118.21 0.2 1 171 101 100 ALA H H 7.624 0.02 1 172 101 100 ALA N N 117.99 0.2 1 173 103 102 ALA H H 8.726 0.02 1 174 103 102 ALA N N 123.64 0.2 1 175 104 103 SER H H 9.114 0.02 1 176 104 103 SER N N 115.00 0.2 1 177 105 104 GLY H H 7.442 0.02 1 178 105 104 GLY N N 103.25 0.2 1 179 106 105 TYR H H 8.524 0.02 1 180 106 105 TYR N N 118.86 0.2 1 181 108 107 VAL H H 8.089 0.02 1 182 108 107 VAL N N 127.36 0.2 1 183 109 108 LYS H H 8.376 0.02 1 184 109 108 LYS N N 123.48 0.2 1 185 111 110 PHE H H 7.583 0.02 1 186 111 110 PHE N N 115.95 0.2 1 187 112 111 THR H H 7.916 0.02 1 188 112 111 THR N N 130.47 0.2 1 189 113 112 ALA H H 9.188 0.02 1 190 113 112 ALA N N 122.65 0.2 1 191 114 113 ALA H H 8.212 0.02 1 192 114 113 ALA N N 118.69 0.2 1 193 116 115 LEU H H 8.235 0.02 1 194 116 115 LEU N N 121.77 0.2 1 195 117 116 GLU H H 8.857 0.02 1 196 117 116 GLU N N 119.06 0.2 1 197 118 117 GLU H H 7.670 0.02 1 198 118 117 GLU N N 117.75 0.2 1 199 120 119 LEU H H 8.543 0.02 1 200 120 119 LEU N N 118.40 0.2 1 201 121 120 ASN H H 8.605 0.02 1 202 121 120 ASN N N 115.13 0.2 1 203 122 121 LYS H H 7.585 0.02 1 204 122 121 LYS N N 119.73 0.2 1 205 123 122 ILE H H 7.385 0.02 1 206 123 122 ILE N N 120.98 0.2 1 207 124 123 PHE H H 9.111 0.02 1 208 124 123 PHE N N 117.66 0.2 1 209 125 124 GLU H H 8.330 0.02 1 210 125 124 GLU N N 119.19 0.2 1 211 126 125 LYS H H 8.317 0.02 1 212 126 125 LYS N N 121.31 0.2 1 213 128 127 GLY H H 7.966 0.02 1 214 128 127 GLY N N 110.53 0.2 1 215 129 128 MET H H 8.432 0.02 1 216 129 128 MET N N 124.43 0.2 1 stop_ save_