data_6387 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural and Functional Study of Anemonia Elastase Inhibitor, a "Non-classical" Kazal-type Inhibitor from Anemonia sulcata ; _BMRB_accession_number 6387 _BMRB_flat_file_name bmr6387.str _Entry_type original _Submission_date 2004-11-15 _Accession_date 2004-11-15 _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 Hemmi Hikaru . . 2 Kumazaki Takashi . . 3 Yoshizawa-Kumagaye Kumiko . . 4 Nishiuchi Yuji . . 5 Yoshida Takuya . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 263 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-09-08 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 6386 'aei monomer' stop_ _Original_release_date 2004-11-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and Functional Study of an Anemonia Elastase Inhibitor, a "Nonclassical" Kazal-Type Inhibitor from Anemonia sulcata. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16008348 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Kumazaki Takashi . . 3 Yoshizawa-Kumagaye Kumiko . . 4 Nishiuchi Yuji . . 5 Yoshida Takuya . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 44 _Journal_issue 28 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9626 _Page_last 9636 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_system_aei-analogue _Saveframe_category molecular_system _Mol_system_name 'aei-analogue monomer' _Abbreviation_common aei-analogue _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'aei-analogue monomer' $aei-analogue 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_aei-analogue _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'anemonia elastase inhibitor analogue' _Abbreviation_common aei-analogue _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 48 _Mol_residue_sequence ; KPDAPCICTMQYDPVCGSDG ITYGNACMLLCASARSDTPI ELVHKGRC ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 PRO 3 ASP 4 ALA 5 PRO 6 CYS 7 ILE 8 CYS 9 THR 10 MET 11 GLN 12 TYR 13 ASP 14 PRO 15 VAL 16 CYS 17 GLY 18 SER 19 ASP 20 GLY 21 ILE 22 THR 23 TYR 24 GLY 25 ASN 26 ALA 27 CYS 28 MET 29 LEU 30 LEU 31 CYS 32 ALA 33 SER 34 ALA 35 ARG 36 SER 37 ASP 38 THR 39 PRO 40 ILE 41 GLU 42 LEU 43 VAL 44 HIS 45 LYS 46 GLY 47 ARG 48 CYS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1Y1C 'Solution Structure Of Anemonia Elastase Inhibitor Analogue' 100.00 48 100.00 100.00 3.55e-20 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $aei-analogue 'Anemonia sulcata' 6108 Eukaryota Fungi Anemonia sulcata 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 $aei-analogue 'chemical synthesis' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $aei-analogue . mM 3.0 3.5 . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Task processing stop_ _Details . save_ save_Sparky _Saveframe_category software _Name SPARKY _Version . loop_ _Task assignment 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_DQFCOSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQFCOSY' _Sample_label . save_ save_1H-1H_ECOSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H ECOSY' _Sample_label . save_ save_1H-1H_ROESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H ROESY' _Sample_label . save_ save_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.4 0.1 pH 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-1H NOESY' '1H-1H TOCSY' '1H-1H DQFCOSY' '1H-1H ECOSY' '1H-1H ROESY' '1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'aei-analogue monomer' _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 . 1 LYS HA H 4.37 . 1 2 . 1 LYS HB2 H 1.95 . 2 3 . 1 LYS HB3 H 2.03 . 2 4 . 1 LYS HG2 H 1.51 . 2 5 . 1 LYS HG3 H 1.60 . 2 6 . 1 LYS HD2 H 1.73 . 1 7 . 1 LYS HD3 H 1.73 . 1 8 . 1 LYS HE2 H 3.03 . 1 9 . 1 LYS HE3 H 3.03 . 1 10 . 1 LYS HZ H 7.55 . 1 11 . 2 PRO HA H 4.49 . 1 12 . 2 PRO HB2 H 1.91 . 2 13 . 2 PRO HB3 H 2.34 . 2 14 . 2 PRO HG2 H 2.01 . 1 15 . 2 PRO HG3 H 2.01 . 1 16 . 2 PRO HD2 H 3.62 . 2 17 . 2 PRO HD3 H 3.75 . 2 18 . 3 ASP H H 8.66 . 1 19 . 3 ASP HA H 4.66 . 1 20 . 3 ASP HB2 H 2.81 . 2 21 . 3 ASP HB3 H 2.87 . 2 22 . 4 ALA H H 8.20 . 1 23 . 4 ALA HA H 4.59 . 1 24 . 4 ALA HB H 1.35 . 1 25 . 5 PRO HA H 4.36 . 1 26 . 5 PRO HB2 H 1.82 . 2 27 . 5 PRO HB3 H 2.26 . 2 28 . 5 PRO HG2 H 1.92 . 2 29 . 5 PRO HG3 H 2.00 . 2 30 . 5 PRO HD2 H 3.63 . 2 31 . 5 PRO HD3 H 3.78 . 2 32 . 6 CYS H H 8.66 . 1 33 . 6 CYS HA H 4.60 . 1 34 . 6 CYS HB2 H 2.92 . 2 35 . 6 CYS HB3 H 3.20 . 2 36 . 7 ILE H H 8.54 . 1 37 . 7 ILE HA H 4.30 . 1 38 . 7 ILE HB H 1.87 . 1 39 . 7 ILE HG12 H 1.12 . 2 40 . 7 ILE HG13 H 1.40 . 2 41 . 7 ILE HG2 H 0.85 . 1 42 . 7 ILE HD1 H 0.81 . 1 43 . 8 CYS H H 8.21 . 1 44 . 8 CYS HA H 5.24 . 1 45 . 8 CYS HB2 H 2.64 . 1 46 . 8 CYS HB3 H 3.32 . 1 47 . 9 THR H H 8.39 . 1 48 . 9 THR HA H 4.48 . 1 49 . 9 THR HB H 4.48 . 1 50 . 9 THR HG2 H 1.28 . 1 51 . 10 MET H H 8.37 . 1 52 . 10 MET HA H 4.55 . 1 53 . 10 MET HB2 H 1.95 . 1 54 . 10 MET HB3 H 2.29 . 1 55 . 10 MET HG2 H 2.56 . 2 56 . 10 MET HG3 H 2.73 . 2 57 . 10 MET HE H 2.12 . 1 58 . 11 GLN H H 7.79 . 1 59 . 11 GLN HA H 4.12 . 1 60 . 11 GLN HB2 H 2.01 . 1 61 . 11 GLN HB3 H 2.01 . 1 62 . 11 GLN HG2 H 2.32 . 2 63 . 11 GLN HG3 H 2.42 . 2 64 . 11 GLN HE21 H 6.94 . 2 65 . 11 GLN HE22 H 7.58 . 2 66 . 12 TYR H H 8.82 . 1 67 . 12 TYR HA H 4.69 . 1 68 . 12 TYR HB2 H 3.02 . 2 69 . 12 TYR HB3 H 3.06 . 2 70 . 12 TYR HD1 H 7.25 . 1 71 . 12 TYR HD2 H 7.25 . 1 72 . 12 TYR HE1 H 6.82 . 1 73 . 12 TYR HE2 H 6.82 . 1 74 . 13 ASP H H 8.78 . 1 75 . 13 ASP HA H 4.79 . 1 76 . 13 ASP HB2 H 2.67 . 1 77 . 13 ASP HB3 H 2.79 . 1 78 . 14 PRO HA H 4.51 . 1 79 . 14 PRO HB2 H 1.35 . 2 80 . 14 PRO HB3 H 1.79 . 2 81 . 14 PRO HG2 H 1.68 . 2 82 . 14 PRO HG3 H 1.85 . 2 83 . 14 PRO HD2 H 3.39 . 1 84 . 14 PRO HD3 H 3.39 . 1 85 . 15 VAL H H 8.33 . 1 86 . 15 VAL HA H 4.67 . 1 87 . 15 VAL HB H 1.92 . 1 88 . 15 VAL HG1 H 0.64 . 2 89 . 15 VAL HG2 H 0.95 . 2 90 . 16 CYS H H 8.37 . 1 91 . 16 CYS HA H 5.14 . 1 92 . 16 CYS HB2 H 1.35 . 1 93 . 16 CYS HB3 H 2.40 . 1 94 . 17 GLY H H 9.14 . 1 95 . 17 GLY HA2 H 4.00 . 2 96 . 17 GLY HA3 H 5.22 . 2 97 . 18 SER H H 9.25 . 1 98 . 18 SER HA H 4.08 . 1 99 . 18 SER HB2 H 3.78 . 2 100 . 18 SER HB3 H 4.24 . 2 101 . 19 ASP H H 8.33 . 1 102 . 19 ASP HA H 4.66 . 1 103 . 19 ASP HB2 H 2.88 . 2 104 . 19 ASP HB3 H 3.22 . 2 105 . 20 GLY H H 8.39 . 1 106 . 20 GLY HA2 H 3.79 . 2 107 . 20 GLY HA3 H 4.10 . 2 108 . 21 ILE H H 7.30 . 1 109 . 21 ILE HA H 3.96 . 1 110 . 21 ILE HB H 1.85 . 1 111 . 21 ILE HG12 H 0.91 . 2 112 . 21 ILE HG13 H 1.21 . 2 113 . 21 ILE HG2 H 0.07 . 1 114 . 21 ILE HD1 H 0.71 . 1 115 . 22 THR H H 8.06 . 1 116 . 22 THR HA H 4.85 . 1 117 . 22 THR HB H 4.00 . 1 118 . 22 THR HG2 H 1.14 . 1 119 . 23 TYR H H 9.22 . 1 120 . 23 TYR HA H 4.52 . 1 121 . 23 TYR HB2 H 2.49 . 1 122 . 23 TYR HB3 H 2.91 . 1 123 . 23 TYR HD1 H 7.25 . 1 124 . 23 TYR HD2 H 7.25 . 1 125 . 23 TYR HE1 H 6.89 . 1 126 . 23 TYR HE2 H 6.89 . 1 127 . 24 GLY H H 9.03 . 1 128 . 24 GLY HA2 H 3.67 . 2 129 . 24 GLY HA3 H 4.04 . 2 130 . 25 ASN H H 7.26 . 1 131 . 25 ASN HA H 4.84 . 1 132 . 25 ASN HB2 H 3.10 . 2 133 . 25 ASN HB3 H 3.54 . 2 134 . 25 ASN HD21 H 6.54 . 2 135 . 25 ASN HD22 H 7.75 . 2 136 . 26 ALA H H 9.10 . 1 137 . 26 ALA HA H 3.90 . 1 138 . 26 ALA HB H 1.43 . 1 139 . 27 CYS H H 8.10 . 1 140 . 27 CYS HA H 4.16 . 1 141 . 27 CYS HB2 H 3.48 . 1 142 . 27 CYS HB3 H 3.02 . 1 143 . 28 MET H H 8.36 . 1 144 . 28 MET HA H 4.06 . 1 145 . 28 MET HB2 H 2.23 . 1 146 . 28 MET HB3 H 2.32 . 1 147 . 28 MET HG2 H 2.67 . 2 148 . 28 MET HG3 H 2.88 . 2 149 . 28 MET HE H 2.24 . 1 150 . 29 LEU H H 7.31 . 1 151 . 29 LEU HA H 2.75 . 1 152 . 29 LEU HB2 H 1.65 . 1 153 . 29 LEU HB3 H 1.03 . 1 154 . 29 LEU HG H 1.06 . 1 155 . 29 LEU HD1 H 0.59 . 2 156 . 29 LEU HD2 H 0.63 . 2 157 . 30 LEU H H 8.03 . 1 158 . 30 LEU HA H 3.91 . 1 159 . 30 LEU HB2 H 1.94 . 1 160 . 30 LEU HB3 H 1.59 . 1 161 . 30 LEU HG H 1.74 . 1 162 . 30 LEU HD1 H 0.89 . 1 163 . 30 LEU HD2 H 0.89 . 1 164 . 31 CYS H H 8.48 . 1 165 . 31 CYS HA H 4.32 . 1 166 . 31 CYS HB2 H 3.18 . 2 167 . 31 CYS HB3 H 3.21 . 2 168 . 32 ALA H H 7.73 . 1 169 . 32 ALA HA H 4.08 . 1 170 . 32 ALA HB H 1.49 . 1 171 . 33 SER H H 8.63 . 1 172 . 33 SER HA H 3.97 . 1 173 . 33 SER HB2 H 4.01 . 2 174 . 33 SER HB3 H 4.11 . 2 175 . 34 ALA H H 7.78 . 1 176 . 34 ALA HA H 4.21 . 1 177 . 34 ALA HB H 1.54 . 1 178 . 35 ARG H H 7.35 . 1 179 . 35 ARG HA H 4.41 . 1 180 . 35 ARG HB2 H 1.80 . 2 181 . 35 ARG HB3 H 2.05 . 2 182 . 35 ARG HG2 H 1.73 . 1 183 . 35 ARG HG3 H 1.73 . 1 184 . 35 ARG HD2 H 3.21 . 1 185 . 35 ARG HD3 H 3.21 . 1 186 . 35 ARG HE H 7.24 . 1 187 . 36 SER H H 7.46 . 1 188 . 36 SER HA H 4.61 . 1 189 . 36 SER HB2 H 3.95 . 1 190 . 36 SER HB3 H 4.03 . 1 191 . 37 ASP H H 8.82 . 1 192 . 37 ASP HA H 4.59 . 1 193 . 37 ASP HB2 H 2.97 . 2 194 . 37 ASP HB3 H 3.01 . 2 195 . 38 THR H H 7.80 . 1 196 . 38 THR HA H 4.76 . 1 197 . 38 THR HB H 4.04 . 1 198 . 38 THR HG2 H 1.20 . 1 199 . 39 PRO HA H 4.32 . 1 200 . 39 PRO HB2 H 1.76 . 2 201 . 39 PRO HB3 H 2.15 . 2 202 . 39 PRO HG2 H 1.92 . 2 203 . 39 PRO HG3 H 2.02 . 2 204 . 39 PRO HD2 H 3.65 . 2 205 . 39 PRO HD3 H 3.82 . 2 206 . 40 ILE H H 8.21 . 1 207 . 40 ILE HA H 3.89 . 1 208 . 40 ILE HB H 1.34 . 1 209 . 40 ILE HG12 H 1.68 . 1 210 . 40 ILE HG13 H 1.68 . 1 211 . 40 ILE HG2 H 0.87 . 1 212 . 40 ILE HD1 H 0.81 . 1 213 . 41 GLU H H 8.52 . 1 214 . 41 GLU HA H 4.55 . 1 215 . 41 GLU HB2 H 1.76 . 1 216 . 41 GLU HB3 H 1.76 . 1 217 . 41 GLU HG2 H 2.03 . 2 218 . 41 GLU HG3 H 2.36 . 2 219 . 42 LEU H H 8.79 . 1 220 . 42 LEU HA H 4.09 . 1 221 . 42 LEU HB2 H 1.84 . 1 222 . 42 LEU HB3 H 1.48 . 1 223 . 42 LEU HG H 1.31 . 1 224 . 42 LEU HD1 H 0.64 . 2 225 . 42 LEU HD2 H 0.87 . 2 226 . 43 VAL H H 8.86 . 1 227 . 43 VAL HA H 4.06 . 1 228 . 43 VAL HB H 1.74 . 1 229 . 43 VAL HG1 H 0.85 . 2 230 . 43 VAL HG2 H 1.00 . 2 231 . 44 HIS H H 7.01 . 1 232 . 44 HIS HA H 4.80 . 1 233 . 44 HIS HB2 H 3.30 . 2 234 . 44 HIS HB3 H 3.72 . 2 235 . 44 HIS HD2 H 8.73 . 1 236 . 44 HIS HE1 H 7.26 . 1 237 . 45 LYS H H 9.27 . 1 238 . 45 LYS HA H 4.34 . 1 239 . 45 LYS HB2 H 1.91 . 2 240 . 45 LYS HB3 H 2.02 . 2 241 . 45 LYS HG2 H 1.48 . 2 242 . 45 LYS HG3 H 1.60 . 2 243 . 45 LYS HD2 H 1.72 . 1 244 . 45 LYS HD3 H 1.72 . 1 245 . 45 LYS HE2 H 2.99 . 1 246 . 45 LYS HE3 H 2.99 . 1 247 . 45 LYS HZ H 7.55 . 1 248 . 46 GLY H H 8.63 . 1 249 . 46 GLY HA2 H 3.52 . 2 250 . 46 GLY HA3 H 4.53 . 2 251 . 47 ARG H H 7.95 . 1 252 . 47 ARG HA H 4.12 . 1 253 . 47 ARG HB2 H 1.78 . 2 254 . 47 ARG HB3 H 1.85 . 2 255 . 47 ARG HG2 H 1.69 . 1 256 . 47 ARG HG3 H 1.69 . 1 257 . 47 ARG HD2 H 3.25 . 1 258 . 47 ARG HD3 H 3.25 . 1 259 . 47 ARG HE H 7.24 . 1 260 . 48 CYS H H 8.37 . 1 261 . 48 CYS HA H 4.46 . 1 262 . 48 CYS HB2 H 2.62 . 1 263 . 48 CYS HB3 H 3.24 . 1 stop_ save_