data_387 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 387 _Entry.Title ; 1H NMR Studies of Bovine and Porcine Phospholipase A2: Assignment of Aromatic Resonances and Evidence for a Conformational Equilibrium in Solution ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 J. Fisher . . . 387 2 William Primrose . U. . 387 3 G. Roberts . C.K. . 387 4 N. Dekker . . . 387 5 Rolf Boelens . . . 387 6 Robert Kaptein . . . 387 7 A. Slotboom . J. . 387 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 387 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 129 387 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 4 . . 2010-06-11 . revision BMRB 'Complete natural source information' 387 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 387 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 387 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 387 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 387 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Fisher, J., Primrose, William U., Roberts, G.C.K., Dekker, N., Boelens, Rolf, Kaptein, Robert, Slotboom, A.J., "1H NMR Studies of Bovine and Porcine Phospholipase A2: Assignment of Aromatic Resonances and Evidence for a Conformational Equilibrium in Solution," Biochemistry 28, 5939-5946 (1989). ; _Citation.Title ; 1H NMR Studies of Bovine and Porcine Phospholipase A2: Assignment of Aromatic Resonances and Evidence for a Conformational Equilibrium in Solution ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 28 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 5939 _Citation.Page_last 5946 _Citation.Year 1989 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 J. Fisher . . . 387 1 2 William Primrose . U. . 387 1 3 G. Roberts . C.K. . 387 1 4 N. Dekker . . . 387 1 5 Rolf Boelens . . . 387 1 6 Robert Kaptein . . . 387 1 7 A. Slotboom . J. . 387 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_phospholipase_A2 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_phospholipase_A2 _Assembly.Entry_ID 387 _Assembly.ID 1 _Assembly.Name 'phospholipase A2' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'phospholipase A2' 1 $phospholipase_A2 . . . . . . . . . 387 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'phospholipase A2' system 387 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_phospholipase_A2 _Entity.Sf_category entity _Entity.Sf_framecode phospholipase_A2 _Entity.Entry_ID 387 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'phospholipase A2' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can ; ALWQFRSMIKCAIPGSHPLM DFNNYGCYCGLGGSGTPVDE LHRCCETHDNCYRDAKNLDS CKFLVDNPYTESYSYSCSNT EITCNSKNNACEAFICNCDR NAAICFSKAPYNKEHKNLDT KKYC ; _Entity.Polymer_seq_one_letter_code ; ALWQFRSMIKCAIPGSHPLM DFNNYGCYCGLGGSGTPVDE LHRCCETHDNCYRDAKNLDS CKFLVDNPYTESYSYSCSNT EITCNSKNNACEAFICNCDR NAAICFSKAPYNKEHKNLDT KKYC ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 124 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number 3.1.1.4 _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1919 . "phospholipase A2" . . . . . 100.00 124 100.00 100.00 3.64e-85 . . . . 387 1 2 no BMRB 1920 . "phospholipase A2" . . . . . 100.00 124 100.00 100.00 3.64e-85 . . . . 387 1 3 no BMRB 1921 . "phospholipase A2" . . . . . 100.00 124 100.00 100.00 3.64e-85 . . . . 387 1 4 no PDB 1FX9 . "Carboxylic Ester Hydrolase Complex (Dimeric Pla2 + Mj33 Inhibitor + Sulphate Ions)" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 5 no PDB 1FXF . "Carboxylic Ester Hydrolase Complex (Dimeric Pla2 + Mj33 Inhibitor + Phosphate Ions)" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 6 no PDB 1HN4 . "Prophospholipase A2 Dimer Complexed With Mj33, Sulfate, And Calcium" . . . . . 100.00 131 99.19 99.19 4.14e-84 . . . . 387 1 7 no PDB 1L8S . "Carboxylic Ester Hydrolase Complex (Dimeric Pla2 + Lpc- Ether + Acetate + Phosphate Ions)" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 8 no PDB 1P2P . "Structure Of Porcine Pancreatic Phospholipase A2 At 2.6 Angstroms Resolution And Comparison With Bovine Phospholipase A2" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 9 no PDB 1PIR . "Solution Structure Of Porcine Pancreatic Phospholipase A2" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 10 no PDB 1PIS . "Solution Structure Of Porcine Pancreatic Phospholipase A2" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 11 no PDB 1SFV . "Porcine Pancreas Phospholipase A2, Nmr, Minimized Average Structure" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 12 no PDB 1SFW . "Porcine Pancreas Phospholipase A2, Nmr, 18 Structures" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 13 no PDB 2AZY . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With Cholate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 14 no PDB 2AZZ . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With Taurocholate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 15 no PDB 2B00 . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With Glycocholate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 16 no PDB 2B01 . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With Taurochenodeoxycholate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 17 no PDB 2B03 . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With Taurochenodeoxycholate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 18 no PDB 2B04 . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With Glycochenodeoxycholate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 19 no PDB 2PHI . "A Large Conformational Change Is Found In The Crystal Structure Of The Porcine Pancreatic Phospholipase A2 Point Mutant F63v" . . . . . 100.00 124 98.39 98.39 4.79e-83 . . . . 387 1 20 no PDB 3FVI . "Crystal Structure Of Complex Of Phospholipase A2 With Octyl Sulfates" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 21 no PDB 3FVJ . "Crystal Structure Of Phospholipase A2 1b Crystallized In The Presence Of Octyl Sulfate" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 22 no PDB 3HSW . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With 2-Methoxycyclohexa-2-5-Diene-1,4-Dione" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 23 no PDB 3L30 . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 Complexed With Dihydroxyberberine" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 24 no PDB 3O4M . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With 1,2-Dihydroxybenzene" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 25 no PDB 3QLM . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With N-Hexadecanoic Acid" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 26 no PDB 4DBK . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 Complexed With Berberine" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 27 no PDB 4G5I . "Crystal Structure Of Porcine Pancreatic Pla2 In Complex With Dbp" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 28 no PDB 4O1Y . "Crystal Structure Of Porcine Pancreatic Phospholipase A2 In Complex With 1-naphthaleneacetic Acid" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 29 no PDB 4P2P . "An Independent Crystallographic Refinement Of Porcine Phospholipase A2 At 2.4 Angstroms Resolution" . . . . . 100.00 124 99.19 99.19 6.79e-84 . . . . 387 1 30 no EMBL CAA68341 . "unnamed protein product [Sus scrofa]" . . . . . 100.00 146 99.19 99.19 6.62e-85 . . . . 387 1 31 no GB AAA31101 . "phospholipase [Sus scrofa]" . . . . . 100.00 146 99.19 99.19 6.62e-85 . . . . 387 1 32 no REF NP_001004037 . "phospholipase A2, major isoenzyme precursor [Sus scrofa]" . . . . . 100.00 146 99.19 99.19 6.62e-85 . . . . 387 1 33 no SP P00592 . "RecName: Full=Phospholipase A2, major isoenzyme; AltName: Full=Group IB phospholipase A2; AltName: Full=Phosphatidylcholine 2-a" . . . . . 100.00 146 99.19 99.19 6.62e-85 . . . . 387 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'phospholipase A2' common 387 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 387 1 2 . LEU . 387 1 3 . TRP . 387 1 4 . GLN . 387 1 5 . PHE . 387 1 6 . ARG . 387 1 7 . SER . 387 1 8 . MET . 387 1 9 . ILE . 387 1 10 . LYS . 387 1 11 . CYS . 387 1 12 . ALA . 387 1 13 . ILE . 387 1 14 . PRO . 387 1 15 . GLY . 387 1 16 . SER . 387 1 17 . HIS . 387 1 18 . PRO . 387 1 19 . LEU . 387 1 20 . MET . 387 1 21 . ASP . 387 1 22 . PHE . 387 1 23 . ASN . 387 1 24 . ASN . 387 1 25 . TYR . 387 1 26 . GLY . 387 1 27 . CYS . 387 1 28 . TYR . 387 1 29 . CYS . 387 1 30 . GLY . 387 1 31 . LEU . 387 1 32 . GLY . 387 1 33 . GLY . 387 1 34 . SER . 387 1 35 . GLY . 387 1 36 . THR . 387 1 37 . PRO . 387 1 38 . VAL . 387 1 39 . ASP . 387 1 40 . GLU . 387 1 41 . LEU . 387 1 42 . HIS . 387 1 43 . ARG . 387 1 44 . CYS . 387 1 45 . CYS . 387 1 46 . GLU . 387 1 47 . THR . 387 1 48 . HIS . 387 1 49 . ASP . 387 1 50 . ASN . 387 1 51 . CYS . 387 1 52 . TYR . 387 1 53 . ARG . 387 1 54 . ASP . 387 1 55 . ALA . 387 1 56 . LYS . 387 1 57 . ASN . 387 1 58 . LEU . 387 1 59 . ASP . 387 1 60 . SER . 387 1 61 . CYS . 387 1 62 . LYS . 387 1 63 . PHE . 387 1 64 . LEU . 387 1 65 . VAL . 387 1 66 . ASP . 387 1 67 . ASN . 387 1 68 . PRO . 387 1 69 . TYR . 387 1 70 . THR . 387 1 71 . GLU . 387 1 72 . SER . 387 1 73 . TYR . 387 1 74 . SER . 387 1 75 . TYR . 387 1 76 . SER . 387 1 77 . CYS . 387 1 78 . SER . 387 1 79 . ASN . 387 1 80 . THR . 387 1 81 . GLU . 387 1 82 . ILE . 387 1 83 . THR . 387 1 84 . CYS . 387 1 85 . ASN . 387 1 86 . SER . 387 1 87 . LYS . 387 1 88 . ASN . 387 1 89 . ASN . 387 1 90 . ALA . 387 1 91 . CYS . 387 1 92 . GLU . 387 1 93 . ALA . 387 1 94 . PHE . 387 1 95 . ILE . 387 1 96 . CYS . 387 1 97 . ASN . 387 1 98 . CYS . 387 1 99 . ASP . 387 1 100 . ARG . 387 1 101 . ASN . 387 1 102 . ALA . 387 1 103 . ALA . 387 1 104 . ILE . 387 1 105 . CYS . 387 1 106 . PHE . 387 1 107 . SER . 387 1 108 . LYS . 387 1 109 . ALA . 387 1 110 . PRO . 387 1 111 . TYR . 387 1 112 . ASN . 387 1 113 . LYS . 387 1 114 . GLU . 387 1 115 . HIS . 387 1 116 . LYS . 387 1 117 . ASN . 387 1 118 . LEU . 387 1 119 . ASP . 387 1 120 . THR . 387 1 121 . LYS . 387 1 122 . LYS . 387 1 123 . TYR . 387 1 124 . CYS . 387 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 387 1 . LEU 2 2 387 1 . TRP 3 3 387 1 . GLN 4 4 387 1 . PHE 5 5 387 1 . ARG 6 6 387 1 . SER 7 7 387 1 . MET 8 8 387 1 . ILE 9 9 387 1 . LYS 10 10 387 1 . CYS 11 11 387 1 . ALA 12 12 387 1 . ILE 13 13 387 1 . PRO 14 14 387 1 . GLY 15 15 387 1 . SER 16 16 387 1 . HIS 17 17 387 1 . PRO 18 18 387 1 . LEU 19 19 387 1 . MET 20 20 387 1 . ASP 21 21 387 1 . PHE 22 22 387 1 . ASN 23 23 387 1 . ASN 24 24 387 1 . TYR 25 25 387 1 . GLY 26 26 387 1 . CYS 27 27 387 1 . TYR 28 28 387 1 . CYS 29 29 387 1 . GLY 30 30 387 1 . LEU 31 31 387 1 . GLY 32 32 387 1 . GLY 33 33 387 1 . SER 34 34 387 1 . GLY 35 35 387 1 . THR 36 36 387 1 . PRO 37 37 387 1 . VAL 38 38 387 1 . ASP 39 39 387 1 . GLU 40 40 387 1 . LEU 41 41 387 1 . HIS 42 42 387 1 . ARG 43 43 387 1 . CYS 44 44 387 1 . CYS 45 45 387 1 . GLU 46 46 387 1 . THR 47 47 387 1 . HIS 48 48 387 1 . ASP 49 49 387 1 . ASN 50 50 387 1 . CYS 51 51 387 1 . TYR 52 52 387 1 . ARG 53 53 387 1 . ASP 54 54 387 1 . ALA 55 55 387 1 . LYS 56 56 387 1 . ASN 57 57 387 1 . LEU 58 58 387 1 . ASP 59 59 387 1 . SER 60 60 387 1 . CYS 61 61 387 1 . LYS 62 62 387 1 . PHE 63 63 387 1 . LEU 64 64 387 1 . VAL 65 65 387 1 . ASP 66 66 387 1 . ASN 67 67 387 1 . PRO 68 68 387 1 . TYR 69 69 387 1 . THR 70 70 387 1 . GLU 71 71 387 1 . SER 72 72 387 1 . TYR 73 73 387 1 . SER 74 74 387 1 . TYR 75 75 387 1 . SER 76 76 387 1 . CYS 77 77 387 1 . SER 78 78 387 1 . ASN 79 79 387 1 . THR 80 80 387 1 . GLU 81 81 387 1 . ILE 82 82 387 1 . THR 83 83 387 1 . CYS 84 84 387 1 . ASN 85 85 387 1 . SER 86 86 387 1 . LYS 87 87 387 1 . ASN 88 88 387 1 . ASN 89 89 387 1 . ALA 90 90 387 1 . CYS 91 91 387 1 . GLU 92 92 387 1 . ALA 93 93 387 1 . PHE 94 94 387 1 . ILE 95 95 387 1 . CYS 96 96 387 1 . ASN 97 97 387 1 . CYS 98 98 387 1 . ASP 99 99 387 1 . ARG 100 100 387 1 . ASN 101 101 387 1 . ALA 102 102 387 1 . ALA 103 103 387 1 . ILE 104 104 387 1 . CYS 105 105 387 1 . PHE 106 106 387 1 . SER 107 107 387 1 . LYS 108 108 387 1 . ALA 109 109 387 1 . PRO 110 110 387 1 . TYR 111 111 387 1 . ASN 112 112 387 1 . LYS 113 113 387 1 . GLU 114 114 387 1 . HIS 115 115 387 1 . LYS 116 116 387 1 . ASN 117 117 387 1 . LEU 118 118 387 1 . ASP 119 119 387 1 . THR 120 120 387 1 . LYS 121 121 387 1 . LYS 122 122 387 1 . TYR 123 123 387 1 . CYS 124 124 387 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 387 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $phospholipase_A2 . 9823 organism . 'Sus scrofa' pig . . Eukaryota Metazoa Sus scrofa generic . . . pancreas . . . . . . . . . . . . . . . . 387 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 387 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $phospholipase_A2 . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 387 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 387 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 387 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 4.1 . na 387 1 temperature 320 . K 387 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 387 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 387 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 387 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 387 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 387 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 387 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 387 1 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 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 387 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 387 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 3 3 TRP HB2 H 1 3.42 . . 2 . . . . . . . . 387 1 2 . 1 1 3 3 TRP HB3 H 1 3.62 . . 2 . . . . . . . . 387 1 3 . 1 1 3 3 TRP HD1 H 1 7.54 . . 1 . . . . . . . . 387 1 4 . 1 1 3 3 TRP HE1 H 1 10.2 . . 1 . . . . . . . . 387 1 5 . 1 1 3 3 TRP HE3 H 1 7.6 . . 1 . . . . . . . . 387 1 6 . 1 1 3 3 TRP HZ2 H 1 7.54 . . 1 . . . . . . . . 387 1 7 . 1 1 3 3 TRP HZ3 H 1 7.37 . . 1 . . . . . . . . 387 1 8 . 1 1 3 3 TRP HH2 H 1 7.33 . . 1 . . . . . . . . 387 1 9 . 1 1 5 5 PHE HA H 1 4.51 . . 1 . . . . . . . . 387 1 10 . 1 1 5 5 PHE HD1 H 1 7.15 . . 1 . . . . . . . . 387 1 11 . 1 1 5 5 PHE HD2 H 1 7.15 . . 1 . . . . . . . . 387 1 12 . 1 1 5 5 PHE HE1 H 1 6.96 . . 1 . . . . . . . . 387 1 13 . 1 1 5 5 PHE HE2 H 1 6.96 . . 1 . . . . . . . . 387 1 14 . 1 1 5 5 PHE HZ H 1 6.29 . . 1 . . . . . . . . 387 1 15 . 1 1 9 9 ILE HG12 H 1 .19 . . 1 . . . . . . . . 387 1 16 . 1 1 9 9 ILE HG13 H 1 .19 . . 1 . . . . . . . . 387 1 17 . 1 1 9 9 ILE HG21 H 1 1.12 . . 1 . . . . . . . . 387 1 18 . 1 1 9 9 ILE HG22 H 1 1.12 . . 1 . . . . . . . . 387 1 19 . 1 1 9 9 ILE HG23 H 1 1.12 . . 1 . . . . . . . . 387 1 20 . 1 1 9 9 ILE HD11 H 1 .02 . . 1 . . . . . . . . 387 1 21 . 1 1 9 9 ILE HD12 H 1 .02 . . 1 . . . . . . . . 387 1 22 . 1 1 9 9 ILE HD13 H 1 .02 . . 1 . . . . . . . . 387 1 23 . 1 1 17 17 HIS HD2 H 1 7.35 . . 1 . . . . . . . . 387 1 24 . 1 1 17 17 HIS HE1 H 1 8.54 . . 1 . . . . . . . . 387 1 25 . 1 1 22 22 PHE HA H 1 4.33 . . 1 . . . . . . . . 387 1 26 . 1 1 22 22 PHE HB2 H 1 3.31 . . 2 . . . . . . . . 387 1 27 . 1 1 22 22 PHE HB3 H 1 3.28 . . 2 . . . . . . . . 387 1 28 . 1 1 22 22 PHE HD1 H 1 6.83 . . 1 . . . . . . . . 387 1 29 . 1 1 22 22 PHE HD2 H 1 6.83 . . 1 . . . . . . . . 387 1 30 . 1 1 22 22 PHE HE1 H 1 7.04 . . 1 . . . . . . . . 387 1 31 . 1 1 22 22 PHE HE2 H 1 7.04 . . 1 . . . . . . . . 387 1 32 . 1 1 22 22 PHE HZ H 1 7.04 . . 1 . . . . . . . . 387 1 33 . 1 1 25 25 TYR HD1 H 1 6.62 . . 1 . . . . . . . . 387 1 34 . 1 1 25 25 TYR HD2 H 1 6.62 . . 1 . . . . . . . . 387 1 35 . 1 1 25 25 TYR HE1 H 1 6.62 . . 1 . . . . . . . . 387 1 36 . 1 1 25 25 TYR HE2 H 1 6.62 . . 1 . . . . . . . . 387 1 37 . 1 1 28 28 TYR HD1 H 1 6.46 . . 1 . . . . . . . . 387 1 38 . 1 1 28 28 TYR HD2 H 1 6.46 . . 1 . . . . . . . . 387 1 39 . 1 1 28 28 TYR HE1 H 1 7.13 . . 1 . . . . . . . . 387 1 40 . 1 1 28 28 TYR HE2 H 1 7.13 . . 1 . . . . . . . . 387 1 41 . 1 1 38 38 VAL HB H 1 1.73 . . 1 . . . . . . . . 387 1 42 . 1 1 38 38 VAL HG11 H 1 .55 . . 2 . . . . . . . . 387 1 43 . 1 1 38 38 VAL HG12 H 1 .55 . . 2 . . . . . . . . 387 1 44 . 1 1 38 38 VAL HG13 H 1 .55 . . 2 . . . . . . . . 387 1 45 . 1 1 38 38 VAL HG21 H 1 .85 . . 2 . . . . . . . . 387 1 46 . 1 1 38 38 VAL HG22 H 1 .85 . . 2 . . . . . . . . 387 1 47 . 1 1 38 38 VAL HG23 H 1 .85 . . 2 . . . . . . . . 387 1 48 . 1 1 41 41 LEU HG H 1 1.19 . . 1 . . . . . . . . 387 1 49 . 1 1 41 41 LEU HD11 H 1 .11 . . 2 . . . . . . . . 387 1 50 . 1 1 41 41 LEU HD12 H 1 .11 . . 2 . . . . . . . . 387 1 51 . 1 1 41 41 LEU HD13 H 1 .11 . . 2 . . . . . . . . 387 1 52 . 1 1 41 41 LEU HD21 H 1 .48 . . 2 . . . . . . . . 387 1 53 . 1 1 41 41 LEU HD22 H 1 .48 . . 2 . . . . . . . . 387 1 54 . 1 1 41 41 LEU HD23 H 1 .48 . . 2 . . . . . . . . 387 1 55 . 1 1 52 52 TYR HA H 1 4.35 . . 1 . . . . . . . . 387 1 56 . 1 1 52 52 TYR HB2 H 1 3 . . 2 . . . . . . . . 387 1 57 . 1 1 52 52 TYR HB3 H 1 3.33 . . 2 . . . . . . . . 387 1 58 . 1 1 52 52 TYR HD1 H 1 6.79 . . 1 . . . . . . . . 387 1 59 . 1 1 52 52 TYR HD2 H 1 6.79 . . 1 . . . . . . . . 387 1 60 . 1 1 52 52 TYR HE1 H 1 6.29 . . 1 . . . . . . . . 387 1 61 . 1 1 52 52 TYR HE2 H 1 6.29 . . 1 . . . . . . . . 387 1 62 . 1 1 55 55 ALA HA H 1 3.42 . . 1 . . . . . . . . 387 1 63 . 1 1 55 55 ALA HB1 H 1 1.53 . . 1 . . . . . . . . 387 1 64 . 1 1 55 55 ALA HB2 H 1 1.53 . . 1 . . . . . . . . 387 1 65 . 1 1 55 55 ALA HB3 H 1 1.53 . . 1 . . . . . . . . 387 1 66 . 1 1 58 58 LEU HG H 1 1.51 . . 1 . . . . . . . . 387 1 67 . 1 1 58 58 LEU HD11 H 1 .45 . . 2 . . . . . . . . 387 1 68 . 1 1 58 58 LEU HD12 H 1 .45 . . 2 . . . . . . . . 387 1 69 . 1 1 58 58 LEU HD13 H 1 .45 . . 2 . . . . . . . . 387 1 70 . 1 1 58 58 LEU HD21 H 1 .61 . . 2 . . . . . . . . 387 1 71 . 1 1 58 58 LEU HD22 H 1 .61 . . 2 . . . . . . . . 387 1 72 . 1 1 58 58 LEU HD23 H 1 .61 . . 2 . . . . . . . . 387 1 73 . 1 1 63 63 PHE HD1 H 1 7.3 . . 1 . . . . . . . . 387 1 74 . 1 1 63 63 PHE HD2 H 1 7.3 . . 1 . . . . . . . . 387 1 75 . 1 1 63 63 PHE HE1 H 1 7.3 . . 1 . . . . . . . . 387 1 76 . 1 1 63 63 PHE HE2 H 1 7.3 . . 1 . . . . . . . . 387 1 77 . 1 1 69 69 TYR HD1 H 1 7.21 . . 1 . . . . . . . . 387 1 78 . 1 1 69 69 TYR HD2 H 1 7.21 . . 1 . . . . . . . . 387 1 79 . 1 1 69 69 TYR HE1 H 1 6.95 . . 1 . . . . . . . . 387 1 80 . 1 1 69 69 TYR HE2 H 1 6.95 . . 1 . . . . . . . . 387 1 81 . 1 1 73 73 TYR HA H 1 4.96 . . 1 . . . . . . . . 387 1 82 . 1 1 73 73 TYR HB2 H 1 3.12 . . 2 . . . . . . . . 387 1 83 . 1 1 73 73 TYR HB3 H 1 2.69 . . 2 . . . . . . . . 387 1 84 . 1 1 73 73 TYR HD1 H 1 6.66 . . 1 . . . . . . . . 387 1 85 . 1 1 73 73 TYR HD2 H 1 6.66 . . 1 . . . . . . . . 387 1 86 . 1 1 73 73 TYR HE1 H 1 6.49 . . 1 . . . . . . . . 387 1 87 . 1 1 73 73 TYR HE2 H 1 6.49 . . 1 . . . . . . . . 387 1 88 . 1 1 74 74 SER HA H 1 5.21 . . 1 . . . . . . . . 387 1 89 . 1 1 74 74 SER HB2 H 1 3.76 . . 2 . . . . . . . . 387 1 90 . 1 1 74 74 SER HB3 H 1 3.79 . . 2 . . . . . . . . 387 1 91 . 1 1 75 75 TYR HA H 1 5.44 . . 1 . . . . . . . . 387 1 92 . 1 1 75 75 TYR HB2 H 1 3.18 . . 2 . . . . . . . . 387 1 93 . 1 1 75 75 TYR HB3 H 1 3.11 . . 2 . . . . . . . . 387 1 94 . 1 1 75 75 TYR HD1 H 1 6.98 . . 1 . . . . . . . . 387 1 95 . 1 1 75 75 TYR HD2 H 1 6.98 . . 1 . . . . . . . . 387 1 96 . 1 1 75 75 TYR HE1 H 1 6.68 . . 1 . . . . . . . . 387 1 97 . 1 1 75 75 TYR HE2 H 1 6.68 . . 1 . . . . . . . . 387 1 98 . 1 1 94 94 PHE HA H 1 4.02 . . 1 . . . . . . . . 387 1 99 . 1 1 94 94 PHE HB2 H 1 3.39 . . 2 . . . . . . . . 387 1 100 . 1 1 94 94 PHE HB3 H 1 3.19 . . 2 . . . . . . . . 387 1 101 . 1 1 94 94 PHE HD1 H 1 7.11 . . 1 . . . . . . . . 387 1 102 . 1 1 94 94 PHE HD2 H 1 7.11 . . 1 . . . . . . . . 387 1 103 . 1 1 94 94 PHE HE1 H 1 7.56 . . 1 . . . . . . . . 387 1 104 . 1 1 94 94 PHE HE2 H 1 7.56 . . 1 . . . . . . . . 387 1 105 . 1 1 94 94 PHE HZ H 1 7.43 . . 1 . . . . . . . . 387 1 106 . 1 1 95 95 ILE HG21 H 1 .94 . . 1 . . . . . . . . 387 1 107 . 1 1 95 95 ILE HG22 H 1 .94 . . 1 . . . . . . . . 387 1 108 . 1 1 95 95 ILE HG23 H 1 .94 . . 1 . . . . . . . . 387 1 109 . 1 1 106 106 PHE HD1 H 1 6.51 . . 1 . . . . . . . . 387 1 110 . 1 1 106 106 PHE HD2 H 1 6.51 . . 1 . . . . . . . . 387 1 111 . 1 1 106 106 PHE HE1 H 1 6.86 . . 1 . . . . . . . . 387 1 112 . 1 1 106 106 PHE HE2 H 1 6.86 . . 1 . . . . . . . . 387 1 113 . 1 1 106 106 PHE HZ H 1 7.2 . . 1 . . . . . . . . 387 1 114 . 1 1 111 111 TYR HA H 1 4.3 . . 1 . . . . . . . . 387 1 115 . 1 1 111 111 TYR HB2 H 1 3.11 . . 2 . . . . . . . . 387 1 116 . 1 1 111 111 TYR HB3 H 1 2.81 . . 2 . . . . . . . . 387 1 117 . 1 1 111 111 TYR HD1 H 1 6.7 . . 1 . . . . . . . . 387 1 118 . 1 1 111 111 TYR HD2 H 1 6.7 . . 1 . . . . . . . . 387 1 119 . 1 1 111 111 TYR HE1 H 1 6.21 . . 1 . . . . . . . . 387 1 120 . 1 1 111 111 TYR HE2 H 1 6.21 . . 1 . . . . . . . . 387 1 121 . 1 1 115 115 HIS HD2 H 1 6.83 . . 1 . . . . . . . . 387 1 122 . 1 1 115 115 HIS HE1 H 1 8.78 . . 1 . . . . . . . . 387 1 123 . 1 1 123 123 TYR HA H 1 4.64 . . 1 . . . . . . . . 387 1 124 . 1 1 123 123 TYR HB2 H 1 3.2 . . 2 . . . . . . . . 387 1 125 . 1 1 123 123 TYR HB3 H 1 2.52 . . 2 . . . . . . . . 387 1 126 . 1 1 123 123 TYR HD1 H 1 7.3 . . 1 . . . . . . . . 387 1 127 . 1 1 123 123 TYR HD2 H 1 7.3 . . 1 . . . . . . . . 387 1 128 . 1 1 123 123 TYR HE1 H 1 6.93 . . 1 . . . . . . . . 387 1 129 . 1 1 123 123 TYR HE2 H 1 6.93 . . 1 . . . . . . . . 387 1 stop_ save_