data_4864 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aa ; _BMRB_accession_number 4864 _BMRB_flat_file_name bmr4864.str _Entry_type original _Submission_date 2000-10-17 _Accession_date 2000-10-17 _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 Song Jikui . . 2 Markley John L . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 46 "13C chemical shifts" 96 "15N chemical shifts" 46 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-01 original author 'original release' 2001-06-01 update author 'update of publication' stop_ loop_ _Related_BMRB_accession_number _Relationship 4865 'complex form' stop_ _Original_release_date 2000-10-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aa ; _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 Song Jikui . . 2 Markley John L . stop_ _Journal_abbreviation 'J. Mol. Recognit.' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 166 _Page_last 171 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_OMTKY3 _Saveframe_category molecular_system _Mol_system_name 'Turkey Ovomucoid Third Domain' _Abbreviation_common OMTKY3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OMTKY3 $OMTKY3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OMTKY3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ovomucoid Third Domain from Turkey' _Abbreviation_common OMTKY3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; LAAVSVDCSEYPKPACTLEY RPLCGSDNKTYGNKCNFCNA VVESNGTLTLSHFGKC ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 ALA 3 ALA 4 VAL 5 SER 6 VAL 7 ASP 8 CYS 9 SER 10 GLU 11 TYR 12 PRO 13 LYS 14 PRO 15 ALA 16 CYS 17 THR 18 LEU 19 GLU 20 TYR 21 ARG 22 PRO 23 LEU 24 CYS 25 GLY 26 SER 27 ASP 28 ASN 29 LYS 30 THR 31 TYR 32 GLY 33 ASN 34 LYS 35 CYS 36 ASN 37 PHE 38 CYS 39 ASN 40 ALA 41 VAL 42 VAL 43 GLU 44 SER 45 ASN 46 GLY 47 THR 48 LEU 49 THR 50 LEU 51 SER 52 HIS 53 PHE 54 GLY 55 LYS 56 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $OMTKY3 Turkey 9103 Eukaryota Metazoa Meleagris Gallopavo 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 $OMTKY3 'recombinant technology' . . . . . 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 $OMTKY3 2 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.3 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shifts_OMTKY3_pH7.3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCO stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name OMTKY3 _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 . 7 ASP C C 177.03 . 1 2 . 8 CYS C C 176.91 . 1 3 . 8 CYS CA C 51.72 . 1 4 . 8 CYS H H 8.94 . 1 5 . 8 CYS N N 126.83 . 1 6 . 9 SER C C 175.74 . 1 7 . 9 SER CA C 62.44 . 1 8 . 9 SER H H 8.80 . 1 9 . 9 SER N N 120.46 . 1 10 . 10 GLU C C 174.17 . 1 11 . 10 GLU CA C 56.73 . 1 12 . 10 GLU H H 8.85 . 1 13 . 10 GLU N N 120.55 . 1 14 . 11 TYR C C 173.32 . 1 15 . 11 TYR CA C 58.05 . 1 16 . 11 TYR H H 7.55 . 1 17 . 11 TYR N N 119.90 . 1 18 . 12 PRO C C 175.91 . 1 19 . 12 PRO CA C 62.16 . 1 20 . 13 LYS CA C 53.56 . 1 21 . 13 LYS H H 9.35 . 1 22 . 13 LYS N N 121.94 . 1 23 . 14 PRO C C 175.73 . 1 24 . 14 PRO CA C 64.07 . 1 25 . 15 ALA C C 175.99 . 1 26 . 15 ALA CA C 51.24 . 1 27 . 15 ALA H H 7.49 . 1 28 . 15 ALA N N 119.52 . 1 29 . 16 CYS C C 175.75 . 1 30 . 16 CYS H H 8.61 . 1 31 . 16 CYS N N 119.22 . 1 32 . 17 THR C C 174.79 . 1 33 . 17 THR CA C 61.52 . 1 34 . 17 THR H H 8.19 . 1 35 . 17 THR N N 113.89 . 1 36 . 18 LEU C C 177.32 . 1 37 . 18 LEU CA C 54.97 . 1 38 . 18 LEU H H 8.43 . 1 39 . 18 LEU N N 120.45 . 1 40 . 19 GLU C C 175.47 . 1 41 . 19 GLU CA C 57.42 . 1 42 . 19 GLU H H 8.30 . 1 43 . 19 GLU N N 123.31 . 1 44 . 20 TYR C C 174.94 . 1 45 . 20 TYR CA C 57.31 . 1 46 . 20 TYR H H 8.94 . 1 47 . 20 TYR N N 128.28 . 1 48 . 21 ARG C C 172.03 . 1 49 . 21 ARG CA C 53.59 . 1 50 . 21 ARG H H 8.91 . 1 51 . 21 ARG N N 130.89 . 1 52 . 22 PRO C C 176.64 . 1 53 . 22 PRO CA C 63.09 . 1 54 . 23 LEU C C 173.91 . 1 55 . 23 LEU CA C 55.12 . 1 56 . 23 LEU H H 8.50 . 1 57 . 23 LEU N N 120.59 . 1 58 . 24 CYS C C 175.70 . 1 59 . 24 CYS CA C 54.55 . 1 60 . 24 CYS H H 8.30 . 1 61 . 24 CYS N N 121.68 . 1 62 . 25 GLY C C 174.97 . 1 63 . 25 GLY CA C 45.43 . 1 64 . 25 GLY H H 9.40 . 1 65 . 25 GLY N N 116.66 . 1 66 . 26 SER C C 173.92 . 1 67 . 26 SER CA C 60.93 . 1 68 . 26 SER H H 9.39 . 1 69 . 26 SER N N 119.02 . 1 70 . 27 ASP C C 176.31 . 1 71 . 27 ASP CA C 53.22 . 1 72 . 27 ASP H H 8.49 . 1 73 . 27 ASP N N 122.43 . 1 74 . 28 ASN C C 173.98 . 1 75 . 28 ASN CA C 55.07 . 1 76 . 28 ASN H H 8.68 . 1 77 . 28 ASN N N 116.83 . 1 78 . 29 LYS C C 174.78 . 1 79 . 29 LYS CA C 55.07 . 1 80 . 29 LYS H H 7.89 . 1 81 . 29 LYS N N 120.17 . 1 82 . 30 THR C C 174.91 . 1 83 . 30 THR CA C 62.73 . 1 84 . 30 THR H H 8.24 . 1 85 . 30 THR N N 121.73 . 1 86 . 31 TYR C C 177.05 . 1 87 . 31 TYR CA C 58.13 . 1 88 . 31 TYR H H 9.79 . 1 89 . 31 TYR N N 131.00 . 1 90 . 32 GLY C C 172.00 . 1 91 . 32 GLY CA C 48.07 . 1 92 . 32 GLY H H 9.18 . 1 93 . 32 GLY N N 110.59 . 1 94 . 33 ASN C C 176.08 . 1 95 . 33 ASN CA C 52.03 . 1 96 . 33 ASN H H 7.48 . 1 97 . 33 ASN N N 107.87 . 1 98 . 34 LYS C C 175.99 . 1 99 . 34 LYS CA C 60.08 . 1 100 . 34 LYS H H 8.94 . 1 101 . 34 LYS N N 120.46 . 1 102 . 35 CYS C C 175.78 . 1 103 . 35 CYS CA C 58.68 . 1 104 . 35 CYS H H 8.30 . 1 105 . 35 CYS N N 122.35 . 1 106 . 36 ASN C C 178.51 . 1 107 . 36 ASN CA C 56.80 . 1 108 . 36 ASN H H 8.36 . 1 109 . 36 ASN N N 119.49 . 1 110 . 37 PHE C C 175.71 . 1 111 . 37 PHE CA C 61.25 . 1 112 . 37 PHE H H 8.39 . 1 113 . 37 PHE N N 120.59 . 1 114 . 38 CYS C C 177.66 . 1 115 . 38 CYS CA C 55.64 . 1 116 . 38 CYS H H 9.21 . 1 117 . 38 CYS N N 118.20 . 1 118 . 39 ASN C C 177.91 . 1 119 . 39 ASN CA C 55.86 . 1 120 . 39 ASN H H 8.20 . 1 121 . 39 ASN N N 120.62 . 1 122 . 40 ALA C C 181.06 . 1 123 . 40 ALA CA C 54.86 . 1 124 . 40 ALA H H 7.31 . 1 125 . 40 ALA N N 124.96 . 1 126 . 41 VAL C C 181.32 . 1 127 . 41 VAL CA C 66.79 . 1 128 . 41 VAL H H 8.58 . 1 129 . 41 VAL N N 124.76 . 1 130 . 42 VAL C C 179.44 . 1 131 . 42 VAL CA C 66.21 . 1 132 . 42 VAL H H 8.05 . 1 133 . 42 VAL N N 121.12 . 1 134 . 43 GLU C C 177.12 . 1 135 . 43 GLU CA C 58.49 . 1 136 . 43 GLU H H 7.77 . 1 137 . 43 GLU N N 122.11 . 1 138 . 44 SER C C 175.62 . 1 139 . 44 SER CA C 59.14 . 1 140 . 44 SER H H 7.88 . 1 141 . 44 SER N N 114.34 . 1 142 . 45 ASN C C 175.61 . 1 143 . 45 ASN CA C 54.39 . 1 144 . 45 ASN H H 8.49 . 1 145 . 45 ASN N N 121.74 . 1 146 . 46 GLY C C 175.04 . 1 147 . 46 GLY CA C 45.84 . 1 148 . 46 GLY H H 8.12 . 1 149 . 46 GLY N N 104.39 . 1 150 . 47 THR C C 174.71 . 1 151 . 47 THR CA C 63.25 . 1 152 . 47 THR H H 7.64 . 1 153 . 47 THR N N 111.99 . 1 154 . 48 LEU C C 174.61 . 1 155 . 48 LEU CA C 55.48 . 1 156 . 48 LEU H H 7.69 . 1 157 . 48 LEU N N 126.00 . 1 158 . 49 THR C C 173.29 . 1 159 . 49 THR CA C 59.40 . 1 160 . 49 THR H H 8.54 . 1 161 . 49 THR N N 117.04 . 1 162 . 50 LEU C C 176.63 . 1 163 . 50 LEU CA C 54.78 . 1 164 . 50 LEU H H 8.78 . 1 165 . 50 LEU N N 123.32 . 1 166 . 51 SER C C 174.96 . 1 167 . 51 SER CA C 60.44 . 1 168 . 51 SER H H 8.94 . 1 169 . 51 SER N N 123.63 . 1 170 . 52 HIS C C 173.21 . 1 171 . 52 HIS CA C 55.26 . 1 172 . 52 HIS H H 7.27 . 1 173 . 52 HIS N N 110.12 . 1 174 . 53 PHE C C 177.09 . 1 175 . 53 PHE CA C 59.99 . 1 176 . 53 PHE H H 8.92 . 1 177 . 53 PHE N N 120.44 . 1 178 . 54 GLY C C 170.71 . 1 179 . 54 GLY CA C 43.99 . 1 180 . 54 GLY H H 8.22 . 1 181 . 54 GLY N N 114.50 . 1 182 . 55 LYS C C 177.99 . 1 183 . 55 LYS CA C 56.03 . 1 184 . 55 LYS H H 7.92 . 1 185 . 55 LYS N N 114.36 . 1 186 . 56 CYS C C 180.71 . 1 187 . 56 CYS H H 8.27 . 1 188 . 56 CYS N N 126.074 . 1 stop_ save_