data_5273 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for SGCI[L30R, K31M] ; _BMRB_accession_number 5273 _BMRB_flat_file_name bmr5273.str _Entry_type original _Submission_date 2002-02-05 _Accession_date 2002-02-05 _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 Patthy Andras . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 164 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 for Schistocerca gregaria chymotrypsin inhibitor' 5274 '1H Chemical shift assignments of Schistocerca gregaria trypsin inhibitor' stop_ _Original_release_date 2002-02-05 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 SGCI 'protease inhibitor' specificity stop_ save_ ################################## # Molecular system description # ################################## save_system_SGCI _Saveframe_category molecular_system _Mol_system_name 'Schistocerca gregaria chymotrypsin inhibitor variant L30R,K31M' _Abbreviation_common SGCI[L30R,K31M] _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SGCI[L30R,K31M] $sgci_mutant 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_sgci_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Schistocerca gregaria chymotrypsin inhibitor' _Abbreviation_common SGCI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; EVTCEPGTTFKDKCNTCRCG SDGKSAACTRMACPQ ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 VAL 3 THR 4 CYS 5 GLU 6 PRO 7 GLY 8 THR 9 THR 10 PHE 11 LYS 12 ASP 13 LYS 14 CYS 15 ASN 16 THR 17 CYS 18 ARG 19 CYS 20 GLY 21 SER 22 ASP 23 GLY 24 LYS 25 SER 26 ALA 27 ALA 28 CYS 29 THR 30 ARG 31 MET 32 ALA 33 CYS 34 PRO 35 GLN 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 1KIO 'Solution Structure Of The Small Serine Protease Inhibitor Sgci[l30r, K31m]' 100.00 35 100.00 100.00 1.68e-11 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $sgci_mutant 'desert locust' 7010 Eukaryota Metazoa Schistocerca gregaria brain 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 $sgci_mutant '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 $sgci_mutant 2.8 mM . stop_ save_ ############################ # Computer software used # ############################ 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 temperature 292 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 '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 SGCI[L30R,K31M] _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 VAL H H 8.51 0.01 1 2 . 2 VAL HA H 4.13 0.01 1 3 . 2 VAL HB H 1.85 0.01 1 4 . 2 VAL HG1 H 0.71 0.01 2 5 . 2 VAL HG2 H 0.81 0.01 2 6 . 3 THR H H 7.94 0.01 1 7 . 3 THR HA H 4.72 0.01 1 8 . 3 THR HB H 4.00 0.01 1 9 . 3 THR HG2 H 1.10 0.01 1 10 . 4 CYS H H 8.54 0.01 1 11 . 4 CYS HA H 4.59 0.01 1 12 . 4 CYS HB2 H 2.42 0.01 2 13 . 4 CYS HB3 H 2.81 0.01 2 14 . 5 GLU H H 8.51 0.01 1 15 . 5 GLU HA H 4.69 0.01 1 16 . 5 GLU HB2 H 2.41 0.01 2 17 . 5 GLU HB3 H 2.67 0.01 2 18 . 5 GLU HG2 H 1.96 0.01 2 19 . 5 GLU HG3 H 1.99 0.01 2 20 . 6 PRO HA H 3.99 0.01 1 21 . 6 PRO HB2 H 1.88 0.01 2 22 . 6 PRO HB3 H 2.27 0.01 2 23 . 6 PRO HG2 H 1.75 0.01 2 24 . 6 PRO HG3 H 2.11 0.01 2 25 . 6 PRO HD2 H 3.69 0.01 2 26 . 6 PRO HD3 H 4.28 0.01 2 27 . 7 GLY H H 7.54 0.01 1 28 . 7 GLY HA2 H 3.70 0.01 2 29 . 7 GLY HA3 H 4.18 0.01 2 30 . 8 THR H H 7.66 0.01 1 31 . 8 THR HA H 4.59 0.01 1 32 . 8 THR HB H 4.40 0.01 1 33 . 9 THR H H 8.49 0.01 1 34 . 9 THR HA H 5.50 0.01 1 35 . 9 THR HB H 3.99 0.01 1 36 . 9 THR HG2 H 1.09 0.01 1 37 . 10 PHE H H 8.86 0.01 1 38 . 10 PHE HA H 5.01 0.01 1 39 . 10 PHE HB2 H 3.07 0.01 1 40 . 10 PHE HB3 H 3.07 0.01 1 41 . 10 PHE HD1 H 6.94 0.01 3 42 . 10 PHE HE1 H 7.03 0.01 3 43 . 10 PHE HZ H 6.84 0.01 1 44 . 11 LYS H H 8.74 0.01 1 45 . 11 LYS HA H 4.83 0.01 1 46 . 11 LYS HB2 H 1.74 0.01 2 47 . 11 LYS HB3 H 1.83 0.01 2 48 . 11 LYS HG2 H 1.36 0.01 2 49 . 11 LYS HG3 H 1.48 0.01 2 50 . 11 LYS HD2 H 1.58 0.01 1 51 . 11 LYS HD3 H 1.58 0.01 1 52 . 11 LYS HE2 H 2.83 0.01 2 53 . 11 LYS HE3 H 2.92 0.01 2 54 . 11 LYS HZ H 7.40 0.01 1 55 . 12 ASP H H 8.22 0.01 1 56 . 12 ASP HA H 4.79 0.01 1 57 . 12 ASP HB2 H 2.51 0.01 1 58 . 12 ASP HB3 H 2.69 0.01 1 59 . 13 LYS H H 9.38 0.01 1 60 . 13 LYS HA H 3.75 0.01 1 61 . 13 LYS HB2 H 1.89 0.01 2 62 . 13 LYS HB3 H 2.19 0.01 2 63 . 13 LYS HG2 H 1.46 0.01 2 64 . 13 LYS HG3 H 1.56 0.01 2 65 . 14 CYS H H 8.39 0.01 1 66 . 14 CYS HA H 4.86 0.01 1 67 . 14 CYS HB2 H 3.14 0.01 2 68 . 14 CYS HB3 H 3.30 0.01 2 69 . 15 ASN H H 8.27 0.01 1 70 . 15 ASN HA H 4.77 0.01 1 71 . 15 ASN HB2 H 2.52 0.01 2 72 . 15 ASN HB3 H 2.81 0.01 2 73 . 15 ASN HD21 H 7.94 0.01 2 74 . 15 ASN HD22 H 8.31 0.01 2 75 . 16 THR H H 8.26 0.01 1 76 . 16 THR HA H 4.46 0.01 1 77 . 16 THR HB H 3.85 0.01 1 78 . 16 THR HG2 H 1.05 0.01 1 79 . 17 CYS H H 8.98 0.01 1 80 . 17 CYS HA H 5.20 0.01 1 81 . 17 CYS HB2 H 0.98 0.01 1 82 . 17 CYS HB3 H 1.81 0.01 1 83 . 18 ARG H H 8.57 0.01 1 84 . 18 ARG HA H 4.91 0.01 1 85 . 18 ARG HB2 H 1.64 0.01 2 86 . 18 ARG HB3 H 1.77 0.01 2 87 . 18 ARG HG2 H 1.41 0.01 2 88 . 18 ARG HG3 H 1.48 0.01 2 89 . 18 ARG HD2 H 3.08 0.01 1 90 . 18 ARG HD3 H 3.08 0.01 1 91 . 18 ARG HE H 7.06 0.01 1 92 . 19 CYS H H 9.42 0.01 1 93 . 19 CYS HA H 4.71 0.01 1 94 . 19 CYS HB2 H 2.88 0.01 2 95 . 19 CYS HB3 H 3.34 0.01 2 96 . 20 GLY H H 9.15 0.01 1 97 . 20 GLY HA2 H 3.88 0.01 1 98 . 20 GLY HA3 H 4.23 0.01 1 99 . 21 SER H H 8.67 0.01 1 100 . 21 SER HA H 4.08 0.01 1 101 . 21 SER HB2 H 3.89 0.01 1 102 . 21 SER HB3 H 3.89 0.01 1 103 . 22 ASP H H 7.94 0.01 1 104 . 22 ASP HA H 4.50 0.01 1 105 . 22 ASP HB2 H 2.66 0.01 2 106 . 22 ASP HB3 H 2.94 0.01 2 107 . 23 GLY H H 7.86 0.01 1 108 . 23 GLY HA2 H 3.98 0.01 2 109 . 23 GLY HA3 H 4.16 0.01 2 110 . 24 LYS H H 7.92 0.01 1 111 . 24 LYS HA H 5.01 0.01 1 112 . 24 LYS HB2 H 1.48 0.01 2 113 . 24 LYS HB3 H 1.98 0.01 2 114 . 24 LYS HG2 H 1.30 0.01 1 115 . 24 LYS HG3 H 1.30 0.01 1 116 . 24 LYS HD2 H 1.62 0.01 1 117 . 24 LYS HD3 H 1.62 0.01 1 118 . 24 LYS HE2 H 2.94 0.01 1 119 . 24 LYS HE3 H 2.94 0.01 1 120 . 24 LYS HZ H 7.48 0.01 1 121 . 25 SER H H 7.77 0.01 1 122 . 25 SER HA H 4.51 0.01 1 123 . 25 SER HB2 H 3.75 0.01 2 124 . 25 SER HB3 H 4.00 0.01 2 125 . 26 ALA H H 8.64 0.01 1 126 . 26 ALA HA H 4.95 0.01 1 127 . 26 ALA HB H 1.35 0.01 1 128 . 27 ALA H H 8.08 0.01 1 129 . 27 ALA HA H 4.71 0.01 1 130 . 27 ALA HB H 1.37 0.01 1 131 . 28 CYS H H 8.78 0.01 1 132 . 28 CYS HA H 5.64 0.01 1 133 . 28 CYS HB2 H 2.83 0.01 2 134 . 28 CYS HB3 H 2.99 0.01 2 135 . 29 THR H H 8.46 0.01 1 136 . 29 THR HA H 4.25 0.01 1 137 . 29 THR HB H 4.53 0.01 1 138 . 29 THR HG2 H 1.33 0.01 1 139 . 30 ARG H H 8.55 0.01 1 140 . 30 ARG HA H 4.47 0.01 1 141 . 30 ARG HB2 H 1.45 0.01 2 142 . 30 ARG HB3 H 1.97 0.01 2 143 . 30 ARG HG2 H 1.53 0.01 1 144 . 30 ARG HG3 H 1.53 0.01 1 145 . 30 ARG HD2 H 3.13 0.01 1 146 . 30 ARG HD3 H 3.13 0.01 1 147 . 31 MET H H 8.75 0.01 1 148 . 31 MET HA H 4.32 0.01 1 149 . 31 MET HB2 H 1.95 0.01 2 150 . 31 MET HB3 H 2.05 0.01 2 151 . 32 ALA H H 8.51 0.01 1 152 . 32 ALA HA H 4.30 0.01 1 153 . 32 ALA HB H 1.33 0.01 1 154 . 33 CYS H H 8.53 0.01 1 155 . 33 CYS HA H 5.15 0.01 1 156 . 33 CYS HB2 H 2.75 0.01 2 157 . 33 CYS HB3 H 3.46 0.01 2 158 . 34 PRO HA H 4.41 0.01 1 159 . 34 PRO HB2 H 1.96 0.01 2 160 . 34 PRO HB3 H 2.27 0.01 2 161 . 34 PRO HG2 H 2.02 0.01 1 162 . 34 PRO HG3 H 2.02 0.01 1 163 . 34 PRO HD2 H 3.67 0.01 2 164 . 34 PRO HD3 H 3.81 0.01 2 stop_ save_