data_4784 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N chemical shift assignments and interproton 3JHNHA coupling constants of the DNA-binding domain of the tyrosine repressor from Haemophilus influenzae, a transcription factor that belongs to the prokaryotic NtrC superfamily ; _BMRB_accession_number 4784 _BMRB_flat_file_name bmr4784.str _Entry_type original _Submission_date 2000-07-13 _Accession_date 2000-07-13 _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 Wang Yunjun Y. . 2 Zhao Shimin S. . 3 Somerville Ronald L. . 4 Jardetzky Oleg O. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 329 "15N chemical shifts" 63 "coupling constants" 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-17 original author . stop_ _Original_release_date 2001-07-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the DNA-binding Domain of the TyrR Protein of Haemophilus influenzae ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21243163 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Yunjun Y. . 2 Zhao Shimin S. . 3 Somerville Ronald L. . 4 Jardetzky Oleg O. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 10 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 592 _Page_last 598 _Year 2001 _Details . loop_ _Keyword 'Tyr repressor' NMR 'DNA-binding domain' 'Haemophilus influenzae' Helix-turn-helix stop_ save_ ################################## # Molecular system description # ################################## save_system_TyrR _Saveframe_category molecular_system _Mol_system_name 'Tyrosine repressor' _Abbreviation_common TyrR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Tyr repressor DNA binding domain' $TyrR(258-318) stop_ _System_molecular_weight 6878 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TyrR(258-318) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common repressor _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; SAVISLDEFENKTLDEIIGF YEAQVLKLFYAEYPSTRKLA QRLGVSHTAIANKLKQYGIG K ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ALA 3 VAL 4 ILE 5 SER 6 LEU 7 ASP 8 GLU 9 PHE 10 GLU 11 ASN 12 LYS 13 THR 14 LEU 15 ASP 16 GLU 17 ILE 18 ILE 19 GLY 20 PHE 21 TYR 22 GLU 23 ALA 24 GLN 25 VAL 26 LEU 27 LYS 28 LEU 29 PHE 30 TYR 31 ALA 32 GLU 33 TYR 34 PRO 35 SER 36 THR 37 ARG 38 LYS 39 LEU 40 ALA 41 GLN 42 ARG 43 LEU 44 GLY 45 VAL 46 SER 47 HIS 48 THR 49 ALA 50 ILE 51 ALA 52 ASN 53 LYS 54 LEU 55 LYS 56 GLN 57 TYR 58 GLY 59 ILE 60 GLY 61 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1G2H "Solution Structure Of The Dna-Binding Domain Of The Tyrr Protein Of Haemophilus Influenzae" 100.00 61 100.00 100.00 3.55e-35 EMBL CBW28709 "transcriptional regulatory protein TyrR [Haemophilus influenzae 10810]" 100.00 318 100.00 100.00 9.91e-33 EMBL CBY81959 "Transcriptional regulatory protein TyrR [Haemophilus influenzae F3031]" 100.00 318 100.00 100.00 1.07e-32 EMBL CBY86469 "Transcriptional regulatory protein TyrR [Haemophilus influenzae F3047]" 100.00 318 98.36 98.36 4.05e-32 GB AAC22069 "transcriptional regulatory protein (tyrR) [Haemophilus influenzae Rd KW20]" 100.00 318 100.00 100.00 9.91e-33 GB ADO80156 "Tyrosine repressor protein TyrR [Haemophilus influenzae R2866]" 100.00 318 100.00 100.00 1.11e-32 GB ADO95632 "Tyrosine repressor protein TyrR [Haemophilus influenzae R2846]" 100.00 318 100.00 100.00 1.06e-32 GB AIB45125 "Transcriptional repressor protein TyrR [Haemophilus influenzae CGSHiCZ412602]" 100.00 318 100.00 100.00 1.17e-32 GB EDJ91589 "transcriptional regulatory protein [Haemophilus influenzae R3021]" 100.00 318 100.00 100.00 1.08e-32 REF NP_438572 "transcriptional regulatory protein [Haemophilus influenzae Rd KW20]" 100.00 318 100.00 100.00 9.91e-33 REF WP_005630049 "transcriptional regulator [Haemophilus haemolyticus]" 100.00 318 98.36 98.36 2.12e-31 REF WP_005634169 "transcriptional regulator [Haemophilus haemolyticus]" 100.00 318 98.36 98.36 1.83e-31 REF WP_005652170 "transcriptional regulator [Haemophilus influenzae]" 100.00 318 100.00 100.00 1.08e-32 REF WP_005656417 "transcriptional regulator [Haemophilus influenzae]" 100.00 318 100.00 100.00 1.02e-32 SP P44694 "RecName: Full=Transcriptional regulatory protein TyrR [Haemophilus influenzae Rd KW20]" 100.00 318 100.00 100.00 9.91e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TyrR(258-318) 'Haemophilus influenzae' 727 Eubacteria . Haemophilus influenzae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Cell_line _Vector_type _Vector_name $TyrR(258-318) 'recombinant technology' 'E. Coli' Escherichia coli . BL21 plasmid pZZ257 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TyrR(258-318) 2.0 mM [U-15N] stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_1 loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $TyrR(258-318) 95 % 'SDS gel and mass spectrometry' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 800 _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 DSS H 1 'methyl protons' ppm 0 internal direct . . . . N 15 . ppm . . . . . . 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Tyr repressor DNA binding domain' _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 . 2 ALA H H 8.77 0.02 1 2 . 2 ALA HA H 4.49 0.02 1 3 . 2 ALA HB H 1.47 0.02 1 4 . 2 ALA N N 124.75 0.02 1 5 . 3 VAL H H 8.32 0.02 1 6 . 3 VAL HA H 4.12 0.02 1 7 . 3 VAL HB H 2.01 0.02 1 8 . 3 VAL HG1 H 0.90 0.02 2 9 . 3 VAL HG2 H 0.95 0.02 2 10 . 3 VAL N N 121.44 0.02 1 11 . 4 ILE H H 8.19 0.02 1 12 . 4 ILE HA H 4.38 0.02 1 13 . 4 ILE HB H 1.80 0.02 1 14 . 4 ILE HG12 H 1.48 0.02 2 15 . 4 ILE HG13 H 1.14 0.02 2 16 . 4 ILE HG2 H 0.75 0.02 1 17 . 4 ILE HD1 H 0.89 0.02 1 18 . 4 ILE N N 120.51 0.02 1 19 . 5 SER H H 7.91 0.02 1 20 . 5 SER HA H 4.60 0.02 1 21 . 5 SER HB2 H 3.66 0.02 2 22 . 5 SER HB3 H 3.82 0.02 2 23 . 5 SER N N 113.81 0.02 1 24 . 6 LEU H H 8.80 0.02 1 25 . 6 LEU HA H 3.93 0.02 1 26 . 6 LEU HB2 H 1.61 0.02 2 27 . 6 LEU HG H 1.44 0.02 1 28 . 6 LEU HD1 H 0.55 0.02 2 29 . 6 LEU HD2 H 0.22 0.02 2 30 . 6 LEU N N 122.82 0.02 1 31 . 7 ASP H H 8.26 0.02 1 32 . 7 ASP HA H 4.27 0.02 1 33 . 7 ASP HB2 H 2.62 0.02 1 34 . 7 ASP HB3 H 2.53 0.02 1 35 . 7 ASP N N 119.35 0.02 1 36 . 8 GLU H H 7.42 0.02 1 37 . 8 GLU HA H 4.02 0.02 1 38 . 8 GLU HB2 H 1.81 0.02 2 39 . 8 GLU HB3 H 1.72 0.02 2 40 . 8 GLU HG2 H 1.94 0.02 2 41 . 8 GLU HG3 H 2.20 0.02 2 42 . 8 GLU N N 117.81 0.02 1 43 . 9 PHE H H 7.40 0.02 1 44 . 9 PHE HA H 4.90 0.02 1 45 . 9 PHE HB2 H 3.81 0.02 1 46 . 9 PHE HB3 H 3.00 0.02 1 47 . 9 PHE HD1 H 7.17 0.02 1 48 . 9 PHE HD2 H 7.17 0.02 1 49 . 9 PHE HE1 H 7.27 0.02 1 50 . 9 PHE HE2 H 7.27 0.02 1 51 . 9 PHE HZ H 7.25 0.02 1 52 . 9 PHE N N 116.27 0.02 1 53 . 10 GLU H H 7.34 0.02 1 54 . 10 GLU HA H 4.08 0.02 1 55 . 10 GLU HB2 H 1.99 0.02 2 56 . 10 GLU HG2 H 2.10 0.02 2 57 . 10 GLU HG3 H 2.34 0.02 2 58 . 10 GLU N N 122.82 0.02 1 59 . 11 ASN H H 9.14 0.02 1 60 . 11 ASN HA H 4.44 0.02 1 61 . 11 ASN HB2 H 3.05 0.02 1 62 . 11 ASN HB3 H 3.14 0.02 1 63 . 11 ASN HD21 H 7.69 0.02 2 64 . 11 ASN HD22 H 7.02 0.02 2 65 . 11 ASN N N 117.81 0.02 1 66 . 11 ASN ND2 N 114.73 0.02 1 67 . 12 LYS H H 7.87 0.02 1 68 . 12 LYS HA H 4.97 0.02 1 69 . 12 LYS HB2 H 1.94 0.02 1 70 . 12 LYS HB3 H 1.88 0.02 1 71 . 12 LYS HG2 H 1.65 0.02 2 72 . 12 LYS HG3 H 1.53 0.02 2 73 . 12 LYS HD2 H 1.40 0.02 2 74 . 12 LYS HD3 H 1.31 0.02 2 75 . 12 LYS N N 117.42 0.02 1 76 . 13 THR H H 8.64 0.02 1 77 . 13 THR HA H 4.80 0.02 1 78 . 13 THR HB H 4.21 0.02 1 79 . 13 THR HG2 H 1.30 0.02 1 80 . 13 THR N N 111.64 0.02 1 81 . 14 LEU H H 8.87 0.02 1 82 . 14 LEU HA H 3.98 0.02 1 83 . 14 LEU HB2 H 1.88 0.02 2 84 . 14 LEU HD1 H 0.90 0.02 2 85 . 14 LEU HD2 H 0.97 0.02 2 86 . 14 LEU N N 120.12 0.02 1 87 . 15 ASP H H 8.53 0.02 1 88 . 15 ASP HA H 4.38 0.02 1 89 . 15 ASP HB2 H 2.55 0.02 1 90 . 15 ASP HB3 H 2.64 0.02 1 91 . 15 ASP N N 115.88 0.02 1 92 . 16 GLU H H 7.58 0.02 1 93 . 16 GLU HA H 4.13 0.02 1 94 . 16 GLU HB2 H 2.43 0.02 1 95 . 16 GLU HB3 H 2.29 0.02 1 96 . 16 GLU HG2 H 2.03 0.02 2 97 . 16 GLU HG3 H 2.18 0.02 2 98 . 16 GLU N N 120.51 0.02 1 99 . 17 ILE H H 8.44 0.02 1 100 . 17 ILE HA H 3.73 0.02 1 101 . 17 ILE HB H 1.96 0.02 1 102 . 17 ILE HG2 H 0.74 0.02 1 103 . 17 ILE HD1 H 0.46 0.02 1 104 . 17 ILE N N 122.44 0.02 1 105 . 18 ILE H H 8.85 0.02 1 106 . 18 ILE HA H 4.02 0.02 1 107 . 18 ILE HB H 2.22 0.02 1 108 . 18 ILE HG12 H 1.55 0.02 2 109 . 18 ILE HG13 H 1.77 0.02 2 110 . 18 ILE HG2 H 1.04 0.02 1 111 . 18 ILE HD1 H 0.82 0.02 1 112 . 18 ILE N N 119.74 0.02 1 113 . 19 GLY H H 8.36 0.02 1 114 . 19 GLY HA2 H 4.03 0.02 2 115 . 19 GLY HA3 H 4.20 0.02 2 116 . 19 GLY N N 108.91 0.02 1 117 . 20 PHE H H 8.16 0.02 1 118 . 20 PHE HA H 4.33 0.02 1 119 . 20 PHE HB2 H 3.42 0.02 1 120 . 20 PHE HB3 H 3.29 0.02 1 121 . 20 PHE HD1 H 7.45 0.02 1 122 . 20 PHE HD2 H 7.45 0.02 1 123 . 20 PHE HE1 H 7.42 0.02 1 124 . 20 PHE HE2 H 7.42 0.02 1 125 . 20 PHE N N 120.89 0.02 1 126 . 21 TYR H H 7.51 0.02 1 127 . 21 TYR HA H 4.05 0.02 1 128 . 21 TYR HB2 H 2.72 0.02 1 129 . 21 TYR HB3 H 2.90 0.02 1 130 . 21 TYR HD1 H 6.50 0.02 1 131 . 21 TYR HD2 H 6.50 0.02 1 132 . 21 TYR HE1 H 6.42 0.02 1 133 . 21 TYR HE2 H 6.42 0.02 1 134 . 21 TYR N N 120.12 0.02 1 135 . 22 GLU H H 9.26 0.02 1 136 . 22 GLU HA H 3.38 0.02 1 137 . 22 GLU HB2 H 2.22 0.02 1 138 . 22 GLU HB3 H 2.29 0.02 1 139 . 22 GLU HG2 H 1.99 0.02 2 140 . 22 GLU HG3 H 2.06 0.02 2 141 . 22 GLU N N 119.74 0.02 1 142 . 23 ALA H H 7.84 0.02 1 143 . 23 ALA HA H 3.18 0.02 1 144 . 23 ALA HB H 0.85 0.02 1 145 . 23 ALA N N 118.96 0.02 1 146 . 24 GLN H H 7.19 0.02 1 147 . 24 GLN HA H 3.77 0.02 1 148 . 24 GLN HB2 H 1.89 0.02 2 149 . 24 GLN HB3 H 2.00 0.02 2 150 . 24 GLN HG2 H 2.06 0.02 2 151 . 24 GLN HG3 H 2.18 0.02 2 152 . 24 GLN HE21 H 6.64 0.02 2 153 . 24 GLN HE22 H 6.91 0.02 2 154 . 24 GLN N N 116.27 0.02 1 155 . 24 GLN NE2 N 112.09 0.02 1 156 . 25 VAL H H 8.16 0.02 1 157 . 25 VAL HA H 3.30 0.02 1 158 . 25 VAL HB H 1.82 0.02 1 159 . 25 VAL HG1 H 0.62 0.02 1 160 . 25 VAL HG2 H 0.25 0.02 1 161 . 25 VAL N N 120.51 0.02 1 162 . 26 LEU H H 8.72 0.02 1 163 . 26 LEU HA H 4.08 0.02 1 164 . 26 LEU HB2 H 1.15 0.02 2 165 . 26 LEU HG H 1.83 0.02 1 166 . 26 LEU HD1 H 0.84 0.02 2 167 . 26 LEU HD2 H 0.72 0.02 2 168 . 26 LEU N N 118.22 0.02 1 169 . 27 LYS H H 8.17 0.02 1 170 . 27 LYS HA H 3.89 0.02 1 171 . 27 LYS HB2 H 1.88 0.02 2 172 . 27 LYS N N 120.12 0.02 1 173 . 28 LEU H H 7.51 0.02 1 174 . 28 LEU HA H 4.13 0.02 1 175 . 28 LEU HB2 H 1.70 0.02 2 176 . 28 LEU HB3 H 1.75 0.02 2 177 . 28 LEU HG H 1.50 0.02 1 178 . 28 LEU HD1 H 0.74 0.02 2 179 . 28 LEU HD2 H 0.82 0.02 2 180 . 28 LEU N N 120.12 0.02 1 181 . 29 PHE H H 8.50 0.02 1 182 . 29 PHE HA H 4.22 0.02 1 183 . 29 PHE HB2 H 2.96 0.02 1 184 . 29 PHE HB3 H 3.14 0.02 1 185 . 29 PHE HD1 H 7.35 0.02 1 186 . 29 PHE HD2 H 7.35 0.02 1 187 . 29 PHE HE1 H 7.08 0.02 1 188 . 29 PHE HE2 H 7.08 0.02 1 189 . 29 PHE N N 116.65 0.02 1 190 . 30 TYR H H 9.23 0.02 1 191 . 30 TYR HA H 4.31 0.02 1 192 . 30 TYR HB2 H 3.08 0.02 1 193 . 30 TYR HB3 H 2.93 0.02 1 194 . 30 TYR HD1 H 7.02 0.02 1 195 . 30 TYR HD2 H 7.02 0.02 1 196 . 30 TYR HE1 H 6.69 0.02 1 197 . 30 TYR HE2 H 6.69 0.02 1 198 . 30 TYR N N 121.28 0.02 1 199 . 31 ALA H H 7.12 0.02 1 200 . 31 ALA HA H 3.99 0.02 1 201 . 31 ALA HB H 1.52 0.02 1 202 . 31 ALA N N 116.27 0.02 1 203 . 32 GLU H H 6.99 0.02 1 204 . 32 GLU HA H 4.13 0.02 1 205 . 32 GLU HB2 H 1.78 0.02 2 206 . 32 GLU HG2 H 2.00 0.02 2 207 . 32 GLU N N 115.48 0.02 1 208 . 33 TYR H H 8.19 0.02 1 209 . 33 TYR HA H 4.80 0.02 1 210 . 33 TYR HB2 H 3.15 0.02 1 211 . 33 TYR HB3 H 2.62 0.02 1 212 . 33 TYR HD1 H 7.35 0.02 1 213 . 33 TYR HD2 H 7.35 0.02 1 214 . 33 TYR HE1 H 6.93 0.02 1 215 . 33 TYR HE2 H 6.93 0.02 1 216 . 33 TYR N N 118.19 0.02 1 217 . 34 PRO HA H 4.02 0.02 1 218 . 34 PRO HB2 H 1.98 0.02 2 219 . 34 PRO HB3 H 1.94 0.02 2 220 . 34 PRO HG2 H 1.73 0.02 2 221 . 34 PRO HG3 H 1.81 0.02 2 222 . 34 PRO HD2 H 3.12 0.02 2 223 . 34 PRO HD3 H 3.45 0.02 2 224 . 35 SER H H 8.20 0.02 1 225 . 35 SER HA H 4.92 0.02 1 226 . 35 SER HB2 H 3.80 0.02 2 227 . 35 SER HB3 H 4.17 0.02 2 228 . 35 SER N N 115.49 0.02 1 229 . 36 THR HA H 3.95 0.02 1 230 . 36 THR HB H 4.24 0.02 1 231 . 36 THR HG2 H 1.30 0.02 1 232 . 36 THR N N 125.13 0.02 1 233 . 37 ARG H H 8.41 0.02 1 234 . 37 ARG HA H 3.92 0.02 1 235 . 37 ARG HB2 H 1.72 0.02 2 236 . 37 ARG HB3 H 1.56 0.02 2 237 . 37 ARG HG2 H 1.33 0.02 2 238 . 37 ARG HD2 H 3.07 0.02 1 239 . 37 ARG HD3 H 3.07 0.02 1 240 . 37 ARG N N 123.59 0.02 1 241 . 38 LYS H H 7.69 0.02 1 242 . 38 LYS HA H 4.14 0.02 1 243 . 38 LYS HB2 H 1.97 0.02 2 244 . 38 LYS HB3 H 1.73 0.02 2 245 . 38 LYS HG2 H 1.55 0.02 2 246 . 38 LYS N N 119.74 0.02 1 247 . 39 LEU H H 8.60 0.02 1 248 . 39 LEU HA H 3.75 0.02 1 249 . 39 LEU HB2 H 2.24 0.02 2 250 . 39 LEU HG H 1.76 0.02 1 251 . 39 LEU HD1 H 1.01 0.02 2 252 . 39 LEU HD2 H 1.05 0.02 2 253 . 39 LEU N N 121.66 0.02 1 254 . 40 ALA H H 8.32 0.02 1 255 . 40 ALA HA H 3.76 0.02 1 256 . 40 ALA HB H 1.58 0.02 1 257 . 40 ALA N N 120.89 0.02 1 258 . 41 GLN H H 7.39 0.02 1 259 . 41 GLN HA H 4.06 0.02 1 260 . 41 GLN HB2 H 2.13 0.02 1 261 . 41 GLN HB3 H 2.19 0.02 1 262 . 41 GLN HG2 H 2.38 0.02 2 263 . 41 GLN HG3 H 2.54 0.02 2 264 . 41 GLN HE21 H 7.53 0.02 1 265 . 41 GLN HE22 H 6.89 0.02 1 266 . 41 GLN N N 115.49 0.02 1 267 . 41 GLN NE2 N 111.87 0.02 1 268 . 42 ARG H H 7.89 0.02 1 269 . 42 ARG HA H 4.20 0.02 1 270 . 42 ARG HB2 H 1.58 0.02 2 271 . 42 ARG N N 119.35 0.02 1 272 . 43 LEU H H 8.10 0.02 1 273 . 43 LEU HA H 4.26 0.02 1 274 . 43 LEU HB2 H 1.49 0.02 2 275 . 43 LEU HB3 H 1.64 0.02 2 276 . 43 LEU HG H 1.07 0.02 1 277 . 43 LEU HD1 H -0.20 0.02 2 278 . 43 LEU HD2 H 0.38 0.02 2 279 . 43 LEU N N 113.27 0.02 1 280 . 44 GLY H H 7.87 0.02 1 281 . 44 GLY HA2 H 3.87 0.02 2 282 . 44 GLY HA3 H 4.06 0.02 2 283 . 44 GLY N N 110.48 0.02 1 284 . 45 VAL H H 7.73 0.02 1 285 . 45 VAL HA H 4.68 0.02 1 286 . 45 VAL HB H 2.05 0.02 1 287 . 45 VAL HG1 H 0.78 0.02 1 288 . 45 VAL HG2 H 0.97 0.02 1 289 . 45 VAL N N 113.59 0.02 1 290 . 46 SER H H 8.48 0.02 1 291 . 46 SER HA H 4.46 0.02 1 292 . 46 SER HB2 H 4.00 0.02 2 293 . 46 SER HB3 H 4.32 0.02 2 294 . 46 SER N N 116.65 0.02 1 295 . 47 HIS H H 9.10 0.02 1 296 . 47 HIS HA H 4.09 0.02 1 297 . 47 HIS HB2 H 3.17 0.02 1 298 . 47 HIS HB3 H 3.19 0.02 1 299 . 47 HIS HD2 H 6.81 0.02 1 300 . 47 HIS HE1 H 7.73 0.02 1 301 . 47 HIS N N 121.78 0.02 1 302 . 48 THR H H 7.98 0.02 1 303 . 48 THR HA H 3.98 0.02 1 304 . 48 THR HB H 3.79 0.02 1 305 . 48 THR HG2 H 1.14 0.02 1 306 . 48 THR N N 130.24 0.02 1 307 . 49 ALA H H 7.71 0.02 1 308 . 49 ALA HA H 4.15 0.02 1 309 . 49 ALA HB H 1.44 0.02 1 310 . 49 ALA N N 124.75 0.02 1 311 . 50 ILE H H 8.02 0.02 1 312 . 50 ILE HA H 3.95 0.02 1 313 . 50 ILE HB H 1.96 0.02 1 314 . 50 ILE HG12 H 1.58 0.02 2 315 . 50 ILE HG2 H 1.08 0.02 1 316 . 50 ILE HD1 H 0.78 0.02 1 317 . 50 ILE N N 117.04 0.02 1 318 . 51 ALA H H 8.31 0.02 1 319 . 51 ALA HA H 3.96 0.02 1 320 . 51 ALA HB H 1.41 0.02 1 321 . 51 ALA N N 124.36 0.02 1 322 . 52 ASN H H 8.04 0.02 1 323 . 52 ASN HA H 4.42 0.02 1 324 . 52 ASN HB2 H 2.78 0.02 1 325 . 52 ASN HB3 H 2.89 0.02 1 326 . 52 ASN HD21 H 7.55 0.02 2 327 . 52 ASN HD22 H 6.90 0.02 2 328 . 52 ASN N N 116.65 0.02 1 329 . 53 LYS H H 7.94 0.02 1 330 . 53 LYS HA H 3.89 0.02 1 331 . 53 LYS HB2 H 1.91 0.02 2 332 . 53 LYS HB3 H 1.62 0.02 2 333 . 53 LYS HG2 H 1.52 0.02 2 334 . 53 LYS HG3 H 1.42 0.02 2 335 . 53 LYS N N 122.05 0.02 1 336 . 54 LEU H H 8.55 0.02 1 337 . 54 LEU HA H 3.86 0.02 1 338 . 54 LEU HG H 1.94 0.02 1 339 . 54 LEU HD1 H 0.70 0.02 2 340 . 54 LEU HD2 H 0.54 0.02 2 341 . 54 LEU N N 117.42 0.02 1 342 . 55 LYS H H 7.44 0.02 1 343 . 55 LYS HA H 4.10 0.02 1 344 . 55 LYS HB2 H 1.89 0.02 2 345 . 55 LYS HB3 H 1.68 0.02 2 346 . 55 LYS HG2 H 1.52 0.02 2 347 . 55 LYS HG3 H 1.41 0.02 2 348 . 55 LYS N N 117.42 0.02 1 349 . 56 GLN H H 8.12 0.02 1 350 . 56 GLN HA H 3.86 0.02 1 351 . 56 GLN HB2 H 1.89 0.02 2 352 . 56 GLN HB3 H 1.68 0.02 2 353 . 56 GLN HG2 H 1.93 0.02 1 354 . 56 GLN HG3 H 1.76 0.02 1 355 . 56 GLN HE21 H 6.95 0.02 2 356 . 56 GLN HE22 H 6.70 0.02 2 357 . 56 GLN NE2 N 110.40 0.02 1 358 . 56 GLN N N 121.28 0.02 1 359 . 57 TYR H H 7.56 0.02 1 360 . 57 TYR HA H 4.89 0.02 1 361 . 57 TYR HB2 H 2.57 0.02 1 362 . 57 TYR HB3 H 3.38 0.02 1 363 . 57 TYR HD1 H 7.00 0.02 1 364 . 57 TYR HD2 H 7.00 0.02 1 365 . 57 TYR HE1 H 6.59 0.02 1 366 . 57 TYR HE2 H 6.59 0.02 1 367 . 57 TYR N N 114.34 0.02 1 368 . 58 GLY H H 7.84 0.02 1 369 . 58 GLY HA2 H 3.90 0.02 2 370 . 58 GLY HA3 H 3.95 0.02 2 371 . 58 GLY N N 111.25 0.02 1 372 . 59 ILE H H 8.28 0.02 1 373 . 59 ILE HA H 3.88 0.02 1 374 . 59 ILE HB H 1.48 0.02 1 375 . 59 ILE HG12 H 1.52 0.02 2 376 . 59 ILE HG13 H 1.44 0.02 2 377 . 59 ILE HG2 H 0.42 0.02 1 378 . 59 ILE HD1 H 0.84 0.02 1 379 . 59 ILE N N 120.89 0.02 1 380 . 60 GLY H H 8.22 0.02 1 381 . 60 GLY HA2 H 3.68 0.02 2 382 . 60 GLY HA3 H 3.79 0.02 2 383 . 60 GLY N N 113.57 0.02 1 384 . 61 LYS H H 7.65 0.02 1 385 . 61 LYS HA H 4.18 0.02 1 386 . 61 LYS HB2 H 1.83 0.02 2 387 . 61 LYS HB3 H 1.73 0.02 2 388 . 61 LYS HG2 H 1.70 0.02 2 389 . 61 LYS HG3 H 1.40 0.02 2 390 . 61 LYS HD2 H 1.48 0.02 2 391 . 61 LYS HE2 H 3.00 0.02 2 392 . 61 LYS N N 124.75 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 800 _Mol_system_component_name 'Tyr repressor DNA binding domain' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 5 SER H 5 SER HA 4.4 . . 0.5 2 3JHNHA 6 LEU H 6 LEU HA 7.5 . . 0.5 3 3JHNHA 10 GLU H 10 GLU HA 10.0 . . 0.5 4 3JHNHA 11 ASN H 11 ASN HA 7.8 . . 0.5 5 3JHNHA 13 THR H 13 THR HA 5.8 . . 0.5 6 3JHNHA 14 LEU H 14 LEU HA 5.0 . . 0.5 7 3JHNHA 15 ASP H 15 ASP HA 4.4 . . 0.5 8 3JHNHA 16 GLU H 16 GLU HA 5.4 . . 0.5 9 3JHNHA 17 ILE H 17 ILE HA 4.6 . . 0.5 10 3JHNHA 18 ILE H 18 ILE HA 8.0 . . 0.5 11 3JHNHA 22 GLU H 22 GLU HA 5.4 . . 0.5 12 3JHNHA 23 ALA H 23 ALA HA 4.6 . . 0.5 13 3JHNHA 25 VAL H 25 VAL HA 4.3 . . 0.5 14 3JHNHA 26 LEU H 26 LEU HA 5.5 . . 0.5 15 3JHNHA 27 LYS H 27 LYS HA 4.6 . . 0.5 16 3JHNHA 30 TYR H 30 TYR HA 5.4 . . 0.5 17 3JHNHA 32 GLU H 32 GLU HA 9.7 . . 0.5 18 3JHNHA 33 TYR H 33 TYR HA 7.7 . . 0.5 19 3JHNHA 35 SER H 35 SER HA 5.0 . . 0.5 20 3JHNHA 36 THR H 36 THR HA 4.2 . . 0.5 21 3JHNHA 37 ARG H 37 ARG HA 5.3 . . 0.5 22 3JHNHA 38 LYS H 38 LYS HA 6.2 . . 0.5 23 3JHNHA 39 LEU H 39 LEU HA 5.9 . . 0.5 24 3JHNHA 41 GLN H 41 GLN HA 4.5 . . 0.5 25 3JHNHA 43 LEU H 43 LEU HA 6.9 . . 0.5 26 3JHNHA 45 VAL H 45 VAL HA 7.2 . . 0.5 27 3JHNHA 48 THR H 48 THR HA 5.1 . . 0.5 28 3JHNHA 49 ALA H 49 ALA HA 4.5 . . 0.5 29 3JHNHA 50 ILE H 50 ILE HA 5.0 . . 0.5 30 3JHNHA 52 ASN H 52 ASN HA 4.1 . . 0.5 31 3JHNHA 53 LYS H 53 LYS HA 4.6 . . 0.5 32 3JHNHA 54 LEU H 54 LEU HA 4.7 . . 0.5 33 3JHNHA 57 TYR H 57 TYR HA 5.8 . . 0.5 34 3JHNHA 61 LYS H 61 LYS HA 5.5 . . 0.5 stop_ save_