data_30562 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of SFTI-KLK5 inhibitor ; _BMRB_accession_number 30562 _BMRB_flat_file_name bmr30562.str _Entry_type original _Submission_date 2019-01-16 _Accession_date 2019-01-16 _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 White A. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 88 "13C chemical shifts" 36 "15N chemical shifts" 14 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-08 update BMRB 'update entry citation' 2019-03-28 original author 'original release' stop_ _Original_release_date 2019-02-27 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Amino Acid Scanning at P5' within the Bowman-Birk Inhibitory Loop Reveals Specificity Trends for Diverse Serine Proteases. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30888159 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li C. Y. . 2 'de Veer' S. J. . 3 White A. M. . 4 Chen X. . . 5 Harris J. M. . 6 Swedberg J. E. . 7 Craik D. J. . stop_ _Journal_abbreviation 'J. Med. Chem.' _Journal_name_full 'Journal of medicinal chemistry' _Journal_volume 62 _Journal_issue 7 _Journal_ISSN 1520-4804 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3696 _Page_last 3706 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'SFTI-KLK5 Peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 1694.889 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 14 _Mol_residue_sequence ; GFCHRSYPPECWPN ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PHE 3 CYS 4 HIS 5 ARG 6 SER 7 TYR 8 PRO 9 PRO 10 GLU 11 CYS 12 TRP 13 PRO 14 ASN 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 $entity_1 'common sunflower' 4232 Eukaryota Viridiplantae Helianthus annuus 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 $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1.5 mM SFTI-KLK5, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement 'structure calculation' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_software_5 _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C 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 pH 3.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 water H 1 protons ppm 4.76 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_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' '2D 1H-15N HSQC' '2D 1H-13C HSQC' '2D 1H-1H COSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_1 _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 1 GLY H H 8.378 0.003 . 2 1 1 GLY HA2 H 4.212 0.008 . 3 1 1 GLY HA3 H 3.833 0.011 . 4 1 1 GLY CA C 42.343 0.015 . 5 1 1 GLY N N 108.126 0.000 . 6 2 2 PHE H H 7.979 0.003 . 7 2 2 PHE HA H 4.642 0.003 . 8 2 2 PHE HB2 H 3.145 0.012 . 9 2 2 PHE HB3 H 3.145 0.012 . 10 2 2 PHE HD1 H 7.100 0.004 . 11 2 2 PHE HD2 H 7.100 0.004 . 12 2 2 PHE HE1 H 6.959 0.003 . 13 2 2 PHE HE2 H 6.959 0.003 . 14 2 2 PHE HZ H 7.208 0.000 . 15 2 2 PHE CA C 55.386 0.000 . 16 2 2 PHE CB C 36.986 0.000 . 17 2 2 PHE N N 121.450 0.000 . 18 3 3 CYS H H 8.143 0.003 . 19 3 3 CYS HA H 5.226 0.019 . 20 3 3 CYS HB2 H 2.820 0.004 . 21 3 3 CYS HB3 H 2.897 0.003 . 22 3 3 CYS CA C 53.226 0.000 . 23 3 3 CYS CB C 44.043 0.000 . 24 3 3 CYS N N 122.328 0.000 . 25 4 4 HIS H H 8.840 0.001 . 26 4 4 HIS HA H 4.685 0.005 . 27 4 4 HIS HB2 H 3.337 0.005 . 28 4 4 HIS HB3 H 3.337 0.005 . 29 4 4 HIS CA C 52.118 0.000 . 30 4 4 HIS CB C 27.118 0.000 . 31 4 4 HIS N N 120.664 0.000 . 32 5 5 ARG H H 8.574 0.001 . 33 5 5 ARG HA H 4.301 0.011 . 34 5 5 ARG HB2 H 1.711 0.006 . 35 5 5 ARG HB3 H 1.897 0.003 . 36 5 5 ARG HG2 H 1.544 0.005 . 37 5 5 ARG HG3 H 1.647 0.006 . 38 5 5 ARG HD2 H 3.172 0.003 . 39 5 5 ARG HD3 H 3.172 0.003 . 40 5 5 ARG HE H 7.175 0.003 . 41 5 5 ARG CA C 54.050 0.000 . 42 5 5 ARG CB C 27.417 0.021 . 43 5 5 ARG CG C 24.730 0.010 . 44 5 5 ARG CD C 40.636 0.000 . 45 5 5 ARG N N 123.683 0.000 . 46 5 5 ARG NE N 124.717 0.000 . 47 6 6 SER H H 7.565 0.003 . 48 6 6 SER HA H 4.362 0.006 . 49 6 6 SER HB2 H 3.756 0.002 . 50 6 6 SER HB3 H 3.875 0.003 . 51 6 6 SER CA C 55.265 0.000 . 52 6 6 SER CB C 61.514 0.024 . 53 6 6 SER N N 115.194 0.000 . 54 7 7 TYR H H 8.277 0.002 . 55 7 7 TYR HA H 4.448 0.014 . 56 7 7 TYR HB2 H 2.940 0.002 . 57 7 7 TYR HB3 H 2.995 0.003 . 58 7 7 TYR HD1 H 7.178 0.001 . 59 7 7 TYR HD2 H 7.178 0.001 . 60 7 7 TYR HE1 H 6.904 0.002 . 61 7 7 TYR HE2 H 6.904 0.002 . 62 7 7 TYR CA C 53.776 0.000 . 63 7 7 TYR CB C 37.289 0.054 . 64 7 7 TYR N N 119.853 0.000 . 65 8 8 PRO HA H 4.108 0.001 . 66 8 8 PRO HB2 H 1.874 0.006 . 67 8 8 PRO HB3 H 1.921 0.002 . 68 8 8 PRO HG2 H 1.717 0.004 . 69 8 8 PRO HG3 H 1.868 0.006 . 70 8 8 PRO HD2 H 3.428 0.013 . 71 8 8 PRO HD3 H 3.461 0.009 . 72 8 8 PRO CA C 58.606 0.000 . 73 8 8 PRO CB C 29.894 0.000 . 74 8 8 PRO CG C 22.139 0.015 . 75 8 8 PRO CD C 47.483 0.005 . 76 9 9 PRO HA H 4.525 0.003 . 77 9 9 PRO HB2 H 1.937 0.005 . 78 9 9 PRO HB3 H 2.177 0.005 . 79 9 9 PRO HG2 H 2.076 0.011 . 80 9 9 PRO HG3 H 2.186 0.016 . 81 9 9 PRO HD2 H 3.600 0.010 . 82 9 9 PRO HD3 H 3.630 0.004 . 83 9 9 PRO CA C 60.953 0.000 . 84 9 9 PRO CB C 29.257 0.071 . 85 9 9 PRO CG C 25.005 0.007 . 86 9 9 PRO CD C 47.888 0.006 . 87 10 10 GLU H H 8.026 0.002 . 88 10 10 GLU HA H 4.346 0.004 . 89 10 10 GLU HB2 H 1.789 0.004 . 90 10 10 GLU HB3 H 1.789 0.003 . 91 10 10 GLU HG2 H 1.903 0.009 . 92 10 10 GLU HG3 H 2.123 0.006 . 93 10 10 GLU CA C 52.754 0.000 . 94 10 10 GLU CB C 28.105 0.000 . 95 10 10 GLU CG C 31.459 0.030 . 96 10 10 GLU N N 121.665 0.000 . 97 11 11 CYS H H 8.510 0.002 . 98 11 11 CYS HA H 5.262 0.008 . 99 11 11 CYS HB2 H 2.950 0.009 . 100 11 11 CYS HB3 H 2.950 0.009 . 101 11 11 CYS CA C 53.334 0.000 . 102 11 11 CYS CB C 44.185 0.000 . 103 11 11 CYS N N 121.596 0.000 . 104 12 12 TRP H H 8.937 0.004 . 105 12 12 TRP HA H 5.034 0.003 . 106 12 12 TRP HB2 H 3.499 0.002 . 107 12 12 TRP HB3 H 3.499 0.002 . 108 12 12 TRP HD1 H 7.343 0.001 . 109 12 12 TRP HE1 H 10.183 0.004 . 110 12 12 TRP HE3 H 7.841 0.005 . 111 12 12 TRP HZ2 H 7.433 0.000 . 112 12 12 TRP HZ3 H 6.957 0.001 . 113 12 12 TRP HH2 H 7.107 0.002 . 114 12 12 TRP CA C 53.648 0.000 . 115 12 12 TRP CB C 27.407 0.000 . 116 12 12 TRP N N 124.764 0.000 . 117 12 12 TRP NE1 N 129.139 0.000 . 118 13 13 PRO HA H 4.444 0.003 . 119 13 13 PRO HB2 H 2.038 0.008 . 120 13 13 PRO HB3 H 2.459 0.006 . 121 13 13 PRO HG2 H 2.096 0.007 . 122 13 13 PRO HG3 H 2.199 0.005 . 123 13 13 PRO HD2 H 4.021 0.008 . 124 13 13 PRO HD3 H 4.023 0.008 . 125 13 13 PRO CA C 62.532 0.000 . 126 13 13 PRO CB C 29.111 0.064 . 127 13 13 PRO CG C 25.005 0.007 . 128 13 13 PRO CD C 48.729 0.000 . 129 14 14 ASN H H 7.995 0.003 . 130 14 14 ASN HA H 4.607 0.005 . 131 14 14 ASN HB2 H 2.946 0.012 . 132 14 14 ASN HB3 H 3.200 0.018 . 133 14 14 ASN HD21 H 7.475 0.005 . 134 14 14 ASN HD22 H 6.662 0.006 . 135 14 14 ASN CA C 50.470 0.000 . 136 14 14 ASN CB C 34.701 0.012 . 137 14 14 ASN N N 114.090 0.000 . 138 14 14 ASN ND2 N 109.715 0.022 . stop_ save_