data_115 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor E from Dendroaspis polylepis polylepis Two-dimensional Nuclear Magnetic Resonance at 500MHz ; _BMRB_accession_number 115 _BMRB_flat_file_name bmr115.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Arseniev Alexander S. . 2 Wider Gerhard . . 3 Joubert Francois J. . 4 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 3 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Arseniev, Alexander S., Wider, Gerhard, Joubert, Francois J., Wuthrich, Kurt, "Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor E from Dendroaspis polylepis polylepis Two-dimensional Nuclear Magnetic Resonance at 500MHz," J. Mol. Biol. 159, 323-351 (1982). ; _Citation_title ; Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor E from Dendroaspis polylepis polylepis Two-dimensional Nuclear Magnetic Resonance at 500MHz ; _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 Arseniev Alexander S. . 2 Wider Gerhard . . 3 Joubert Francois J. . 4 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 159 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 323 _Page_last 351 _Year 1982 _Details . save_ ################################## # Molecular system description # ################################## save_system_trypsin_inhibitor_E _Saveframe_category molecular_system _Mol_system_name 'trypsin inhibitor E' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'trypsin inhibitor E' $trypsin_inhibitor_E stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_trypsin_inhibitor_E _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'trypsin inhibitor E' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; LQHRTFCKLPAEPGPCKASI PAFYYNWAAKKCQLFHYGGC KGNANRFSTIEKCRHACVG ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 GLN 3 HIS 4 ARG 5 THR 6 PHE 7 CYS 8 LYS 9 LEU 10 PRO 11 ALA 12 GLU 13 PRO 14 GLY 15 PRO 16 CYS 17 LYS 18 ALA 19 SER 20 ILE 21 PRO 22 ALA 23 PHE 24 TYR 25 TYR 26 ASN 27 TRP 28 ALA 29 ALA 30 LYS 31 LYS 32 CYS 33 GLN 34 LEU 35 PHE 36 HIS 37 TYR 38 GLY 39 GLY 40 CYS 41 LYS 42 GLY 43 ASN 44 ALA 45 ASN 46 ARG 47 PHE 48 SER 49 THR 50 ILE 51 GLU 52 LYS 53 CYS 54 ARG 55 HIS 56 ALA 57 CYS 58 VAL 59 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 BMRB 116 "trypsin inhibitor E" 100.00 59 100.00 100.00 4.26e-35 SP P00984 "RecName: Full=Kunitz-type serine protease inhibitor dendrotoxin E; Short=DTX-E; AltName: Full=Venom basic protease inhibitor E" 100.00 59 100.00 100.00 4.26e-35 SP P0DMJ6 "RecName: Full=Kunitz-type serine protease inhibitor dendrotoxin DaE1; Contains: RecName: Full=Kunitz-type protease inhibitor de" 100.00 59 98.31 98.31 4.31e-34 SP Q7LZE3 "RecName: Full=Kunitz-type serine protease inhibitor long epsilon-dendrotoxin His55; Contains: RecName: Full=Kunitz-type serine " 100.00 59 100.00 100.00 4.26e-35 SP Q7LZS8 "RecName: Full=Kunitz-type serine protease inhibitor long epsilon-dendrotoxin Arg55; Contains: RecName: Full=Kunitz-type serine " 100.00 59 98.31 98.31 4.31e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $trypsin_inhibitor_E 'black mamba' 8620 Eukaryota Metazoa Dendroaspis polylepis venom 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 $trypsin_inhibitor_E 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.2 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $entry_citation $entry_citation 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_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'trypsin inhibitor E' _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 . 16 CYS H H 9.12 . 1 2 . 40 CYS HB2 H 3.9 . 2 3 . 40 CYS HB3 H 2.86 . 2 stop_ save_