data_5274 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical shift assignments of Schistocerca gregaria trypsin inhibitor ; _BMRB_accession_number 5274 _BMRB_flat_file_name bmr5274.str _Entry_type original _Submission_date 2002-02-06 _Accession_date 2002-02-06 _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 Gaspari Zoltan . . 2 Patthy Andras . . 3 Graf Laszlo . . 4 Perczel Andras . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-03-29 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5272 '1H Chemical shift assignments of Schistocerca gregaria chymotrypsin inhibitor' 5273 '1H chemical shift assignments for SGCI[L30R, K31M]' stop_ _Original_release_date 2002-02-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria ; _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 Gaspari Zoltan . . 2 Patthy Andras . . 3 Graf Laszlo . . 4 Patthy Andras . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 269 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 527 _Page_last 537 _Year 2002 _Details . loop_ _Keyword SGTI 'inhibitor specificity' 'serine protease inhibition' stop_ save_ ################################## # Molecular system description # ################################## save_system_SGTI _Saveframe_category molecular_system _Mol_system_name 'Schistocerca gregaria trypsin inhibitor' _Abbreviation_common SGTI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SGTI $SGTI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'protease inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SGTI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Schistocerca gregaria trypsin inhibitor' _Abbreviation_common SGTI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; EQECTPGQTKKQDCNTCNCT PTGVWACTRKGCPPH ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLN 3 GLU 4 CYS 5 THR 6 PRO 7 GLY 8 GLN 9 THR 10 LYS 11 LYS 12 GLN 13 ASP 14 CYS 15 ASN 16 THR 17 CYS 18 ASN 19 CYS 20 THR 21 PRO 22 THR 23 GLY 24 VAL 25 TRP 26 ALA 27 CYS 28 THR 29 ARG 30 LYS 31 GLY 32 CYS 33 PRO 34 PRO 35 HIS 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 1KJ0 'Solution Structure Of The Small Serine Protease Inhibitor Sgti' 100.00 35 100.00 100.00 1.53e-11 PDB 2F91 '1.2a Resolution Structure Of A Crayfish Trypsin Complexed With A Peptide Inhibitor, Sgti' 100.00 35 100.00 100.00 1.53e-11 EMBL CAA70818 'serine protease inhibitor I [Schistocerca gregaria]' 100.00 92 100.00 100.00 5.01e-12 SWISS-PROT O46162 ; Serine protease inhibitor I/II precursor [Contains: Protease inhibitor SGPI-1 (Schistocerca gregaria trypsin inhibitor) (SGTI); Protease inhibitor SGPI-2 (Schistocerca gregaria chymotrypsin inhibitor) (SGCI)] ; 100.00 92 100.00 100.00 5.01e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SGTI 'desert locust' 7010 Eukaryota Metazoa Schistocerca gregaria 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 _Details $SGTI 'chemical synthesis' . . . . . 'Solid phase peptide synthesis, Fmoc strategy.' 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 $SGTI 2.4 mM . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement 'structure solution' stop_ _Details Brunger save_ save_TRIAD_(SYBYL) _Saveframe_category software _Name 'TRIAD (SYBYL)' _Version 6.6 loop_ _Vendor _Address _Electronic_address 'Tripos, Inc.' . . stop_ loop_ _Task 'peak assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _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 3.0 0.2 n/a pressure 1 . atm temperature 300 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D TOCSY' '2D NOESY' 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 SGTI _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 GLN H H 8.80 0.01 1 2 . 2 GLN HA H 4.40 0.01 1 3 . 2 GLN HB2 H 2.00 0.01 2 4 . 2 GLN HB3 H 2.15 0.01 2 5 . 2 GLN HG2 H 2.30 0.01 1 6 . 2 GLN HG3 H 2.30 0.01 1 7 . 3 GLU H H 8.68 0.01 1 8 . 3 GLU HA H 4.27 0.01 1 9 . 3 GLU HB2 H 1.97 0.01 2 10 . 3 GLU HB3 H 2.09 0.01 2 11 . 3 GLU HG2 H 2.43 0.01 1 12 . 3 GLU HG3 H 2.43 0.01 1 13 . 4 CYS H H 7.52 0.01 1 14 . 4 CYS HA H 4.47 0.01 1 15 . 4 CYS HB2 H 1.65 0.01 2 16 . 4 CYS HB3 H 2.12 0.01 2 17 . 5 THR H H 8.04 0.01 1 18 . 5 THR HA H 4.29 0.01 1 19 . 5 THR HB H 3.74 0.01 1 20 . 5 THR HG2 H 1.08 0.01 1 21 . 6 PRO HA H 3.84 0.01 1 22 . 6 PRO HB2 H 1.79 0.01 1 23 . 6 PRO HB3 H 1.79 0.01 1 24 . 6 PRO HG2 H 1.72 0.01 2 25 . 6 PRO HG3 H 1.94 0.01 2 26 . 6 PRO HD2 H 3.38 0.01 1 27 . 6 PRO HD3 H 3.38 0.01 1 28 . 7 GLY H H 8.28 0.01 1 29 . 7 GLY HA2 H 4.36 0.01 1 30 . 7 GLY HA3 H 3.53 0.01 1 31 . 8 GLN H H 7.97 0.01 1 32 . 8 GLN HA H 4.34 0.01 1 33 . 8 GLN HB2 H 1.64 0.01 2 34 . 8 GLN HB3 H 2.46 0.01 2 35 . 9 THR H H 8.44 0.01 1 36 . 9 THR HA H 5.57 0.01 1 37 . 9 THR HB H 4.13 0.01 1 38 . 9 THR HG2 H 1.19 0.01 1 39 . 10 LYS H H 8.40 0.01 1 40 . 10 LYS HA H 4.53 0.01 1 41 . 10 LYS HB2 H 1.37 0.01 1 42 . 10 LYS HB3 H 1.37 0.01 1 43 . 10 LYS HG2 H -0.15 0.01 2 44 . 10 LYS HG3 H 0.16 0.01 2 45 . 10 LYS HD2 H 0.58 0.01 2 46 . 10 LYS HD3 H 0.88 0.01 2 47 . 10 LYS HE2 H 0.67 0.01 2 48 . 10 LYS HE3 H 1.89 0.01 2 49 . 10 LYS HZ H 6.94 0.01 1 50 . 11 LYS H H 8.42 0.01 1 51 . 11 LYS HA H 4.66 0.01 1 52 . 11 LYS HE2 H 2.84 0.01 1 53 . 11 LYS HE3 H 2.84 0.01 1 54 . 11 LYS HZ H 7.34 0.01 1 55 . 12 GLN H H 8.09 0.01 1 56 . 12 GLN HA H 4.27 0.01 1 57 . 12 GLN HB2 H 1.73 0.01 2 58 . 12 GLN HB3 H 1.99 0.01 2 59 . 12 GLN HG2 H 1.49 0.01 1 60 . 12 GLN HG3 H 1.49 0.01 1 61 . 13 ASP H H 9.36 0.01 1 62 . 13 ASP HA H 4.05 0.01 1 63 . 13 ASP HB2 H 2.88 0.01 2 64 . 13 ASP HB3 H 3.04 0.01 2 65 . 14 CYS H H 8.37 0.01 1 66 . 14 CYS HA H 4.66 0.01 1 67 . 14 CYS HB2 H 3.08 0.01 2 68 . 14 CYS HB3 H 3.19 0.01 2 69 . 15 ASN H H 8.32 0.01 1 70 . 15 ASN HA H 4.76 0.01 1 71 . 15 ASN HB2 H 2.58 0.01 2 72 . 15 ASN HB3 H 2.84 0.01 2 73 . 15 ASN HD21 H 7.83 0.01 2 74 . 15 ASN HD22 H 8.05 0.01 2 75 . 16 THR H H 8.25 0.01 1 76 . 16 THR HA H 4.63 0.01 1 77 . 16 THR HB H 3.99 0.01 1 78 . 16 THR HG2 H 1.08 0.01 1 79 . 17 CYS H H 8.94 0.01 1 80 . 17 CYS HA H 5.67 0.01 1 81 . 17 CYS HB2 H 2.56 0.01 1 82 . 17 CYS HB3 H 2.56 0.01 1 83 . 18 ASN H H 9.13 0.01 1 84 . 18 ASN HA H 5.53 0.01 1 85 . 18 ASN HB2 H 2.69 0.01 1 86 . 18 ASN HB3 H 2.69 0.01 1 87 . 19 CYS H H 8.89 0.01 1 88 . 19 CYS HA H 4.57 0.01 1 89 . 19 CYS HB2 H 1.49 0.01 2 90 . 19 CYS HB3 H 2.86 0.01 2 91 . 20 THR H H 9.16 0.01 1 92 . 20 THR HA H 4.47 0.01 1 93 . 21 PRO HA H 4.18 0.01 1 94 . 21 PRO HD2 H 3.75 0.01 2 95 . 21 PRO HD3 H 3.86 0.01 2 96 . 22 THR H H 7.25 0.01 1 97 . 22 THR HA H 4.24 0.01 1 98 . 23 GLY H H 8.24 0.01 1 99 . 23 GLY HA2 H 3.86 0.01 1 100 . 23 GLY HA3 H 3.43 0.01 1 101 . 24 VAL H H 6.73 0.01 1 102 . 24 VAL HA H 4.37 0.01 1 103 . 24 VAL HB H 1.90 0.01 1 104 . 24 VAL HG1 H 0.57 0.01 2 105 . 24 VAL HG2 H 0.76 0.01 2 106 . 25 TRP H H 7.97 0.01 1 107 . 25 TRP HA H 4.80 0.01 1 108 . 25 TRP HB2 H 2.94 0.01 2 109 . 25 TRP HB3 H 3.05 0.01 2 110 . 25 TRP HD1 H 7.11 0.01 1 111 . 25 TRP HE1 H 9.91 0.01 1 112 . 25 TRP HE3 H 6.91 0.01 1 113 . 25 TRP HZ2 H 7.38 0.01 1 114 . 25 TRP HZ3 H 6.62 0.01 1 115 . 25 TRP HH2 H 6.77 0.01 1 116 . 26 ALA H H 9.25 0.01 1 117 . 26 ALA HA H 4.78 0.01 1 118 . 26 ALA HB H 1.34 0.01 1 119 . 27 CYS H H 8.92 0.01 1 120 . 27 CYS HA H 5.64 0.01 1 121 . 27 CYS HB2 H 2.82 0.01 2 122 . 27 CYS HB3 H 2.89 0.01 2 123 . 28 THR H H 8.65 0.01 1 124 . 28 THR HA H 4.26 0.01 1 125 . 29 ARG H H 8.58 0.01 1 126 . 29 ARG HA H 4.47 0.01 1 127 . 30 LYS H H 8.58 0.01 1 128 . 30 LYS HA H 4.20 0.01 1 129 . 31 GLY H H 8.61 0.01 1 130 . 31 GLY HA2 H 3.60 0.01 2 131 . 31 GLY HA3 H 3.94 0.01 2 132 . 32 CYS H H 8.49 0.01 1 133 . 32 CYS HA H 5.08 0.01 1 134 . 32 CYS HB2 H 2.66 0.01 2 135 . 32 CYS HB3 H 3.31 0.01 2 136 . 33 PRO HA H 4.61 0.01 1 137 . 33 PRO HB2 H 1.81 0.01 2 138 . 33 PRO HB3 H 2.28 0.01 2 139 . 33 PRO HG2 H 1.66 0.01 1 140 . 33 PRO HG3 H 1.66 0.01 1 141 . 33 PRO HD2 H 3.58 0.01 2 142 . 33 PRO HD3 H 3.76 0.01 2 143 . 34 PRO HD2 H 3.55 0.01 2 144 . 34 PRO HD3 H 3.66 0.01 2 145 . 35 HIS H H 8.05 0.01 1 146 . 35 HIS HA H 4.41 0.01 1 147 . 35 HIS HB2 H 3.04 0.01 2 148 . 35 HIS HB3 H 3.13 0.01 2 stop_ save_