data_25300 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue ; _BMRB_accession_number 25300 _BMRB_flat_file_name bmr25300.str _Entry_type original _Submission_date 2014-10-28 _Accession_date 2014-10-28 _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 Perekalin Dmitry S. . 2 Pavlov Alexander A. . 3 Novikov Valentin V. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 136 "13C chemical shifts" 22 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-06-29 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 2MW6 'BMRB entry-tracking system' stop_ _Original_release_date 2015-06-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Selective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25688543 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Perekalin Dmitry S. . 2 Novikov Valentin V. . 3 Pavlov Alexander A. . 4 Ivanov Igor A. . 5 Anisimova Natalia Y. . 6 Kopylov Alexey N. . 7 Volkov Dmitry S. . 8 Seregina Irina F. . 9 Bolshov Michail A. . 10 Kudinov Alexander R. . stop_ _Journal_abbreviation Chemistry _Journal_volume 21 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4923 _Page_last 4925 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity entity_3UQ $entity_3UQ stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ru-melittin _Molecular_mass 3028.938 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 26 _Mol_residue_sequence ; GIGAVLKVLTTGLPALISWI KRKRQQ ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 GLY 4 ALA 5 VAL 6 LEU 7 LYS 8 VAL 9 LEU 10 THR 11 THR 12 GLY 13 LEU 14 PRO 15 ALA 16 LEU 17 ILE 18 SER 19 TRP 20 ILE 21 LYS 22 ARG 23 LYS 24 ARG 25 GLN 26 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 2266 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 2267 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 2268 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 245 melittin 100.00 27 100.00 100.00 1.70e-07 BMRB 36 melittin 100.00 27 100.00 100.00 1.70e-07 BMRB 449 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 450 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 451 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 452 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 453 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 454 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 455 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 456 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 457 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 458 melittin 96.15 26 100.00 100.00 1.09e-06 BMRB 459 melittin 96.15 26 100.00 100.00 1.09e-06 PDB 1BH1 "Structural Studies Of D-Pro Melittin, Nmr, 20 Structures" 100.00 27 100.00 100.00 1.70e-07 PDB 2MLT Melittin 100.00 27 100.00 100.00 1.70e-07 PDB 2MW6 "Structure Of The Bee Venom Toxin Melittin With [(c5h5)ru]+ Fragment Attached To The Tryptophan Residue" 100.00 27 100.00 100.00 1.70e-07 PDB 3QRX "Chlamydomonas Reinhardtii Centrin Bound To Melittin" 100.00 26 100.00 100.00 1.69e-07 EMBL CAA26038 "prepromelittin [Apis mellifera]" 100.00 70 100.00 100.00 3.36e-08 EMBL CAC42164 "melittin [Polistes sp. HQL-2001]" 100.00 67 100.00 100.00 3.83e-08 EMBL CAD33921 "melittin protein [Apis cerana]" 100.00 77 100.00 100.00 7.28e-08 EMBL CAH05131 "melittin precursor [Apis cerana cerana]" 100.00 70 100.00 100.00 3.29e-08 GB AAO12202 "prepromelittin [Vespa velutina nigrithorax]" 100.00 70 100.00 100.00 3.29e-08 GB AAO12204 "prepromelittin [Vespa magnifica]" 100.00 70 100.00 100.00 3.29e-08 GB AAO12205 "prepromelittin [Vespula maculifrons]" 100.00 70 100.00 100.00 3.36e-08 GB ABB29918 "cecropin A-melittin hybrid protein [synthetic construct]" 69.23 26 100.00 100.00 4.11e-01 GB ADN88075 "ADAM15 disintegrin [synthetic construct]" 80.77 125 100.00 100.00 4.38e-03 PRF 0404199A melittin,prepro 100.00 70 100.00 100.00 3.66e-08 PRF 670043A melittin 100.00 26 100.00 100.00 1.69e-07 REF NP_001011607 "melittin precursor [Apis mellifera]" 100.00 70 100.00 100.00 3.36e-08 SP P01501 "RecName: Full=Melittin; AltName: Full=Allergen Api m 3; AltName: Full=Allergen Api m III; AltName: Allergen=Api m 4; Flags: Pre" 100.00 70 100.00 100.00 3.36e-08 SP P59262 "RecName: Full=Melittin; Flags: Precursor" 100.00 70 100.00 100.00 3.36e-08 SP P68408 "RecName: Full=Melittin; Flags: Precursor" 100.00 70 100.00 100.00 3.29e-08 SP P68409 "RecName: Full=Melittin; Flags: Precursor" 100.00 70 100.00 100.00 3.29e-08 SP Q8LW54 "RecName: Full=Melittin; Flags: Precursor" 100.00 77 100.00 100.00 7.28e-08 stop_ save_ ############# # Ligands # ############# save_3UQ _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "[(1,2,3,4,5-eta)-cyclopentadienyl][(1,2,3,4,4a,8a-eta)-naphthalene-1,2,3,4-tetrayl]ruthenium ([(1,2,3,4,5-eta)-cyclopentadienyl][(1,2,3,4,4a,8a-eta)-naphthalene]ruthenium(1+))" _BMRB_code 3UQ _PDB_code 3UQ _Molecular_mass "285.262 (294.334)" _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons RU RU RU . 1 . ? CC1 CC1 C . 0 . ? CC2 CC2 C . 0 . ? CC3 CC3 C . 0 . ? CC4 CC4 C . 0 . ? CC5 CC5 C . 0 . ? CA1 CA1 C . 0 . ? CA2 CA2 C . 0 . ? CA3 CA3 C . 0 . ? CA4 CA4 C . 0 . ? CA5 CA5 C . 0 . ? CA6 CA6 C . 0 . ? CA7 CA7 C . 0 . ? CA8 CA8 C . 0 . ? CA9 CA9 C . 0 . ? CA0 CA0 C . 0 . ? HC1 HC1 H . 0 . ? HC2 HC2 H . 0 . ? HC3 HC3 H . 0 . ? HC4 HC4 H . 0 . ? HC5 HC5 H . 0 . ? HA1 HA1 H . 0 . ? HA2 HA2 H . 0 . ? HA3 HA3 H . 0 . ? HA4 HA4 H . 0 . ? HA7 HA7 H . 0 . ? HA8 HA8 H . 0 . ? HA9 HA9 H . 0 . ? HA0 HA0 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB CC1 CC2 ? ? SING CC2 CC3 ? ? DOUB CC3 CC5 ? ? SING CC5 CC4 ? ? SING CC4 CC1 ? ? SING HC3 CC3 ? ? SING CC1 HC1 ? ? SING CC2 HC2 ? ? SING HC4 CC4 ? ? SING HC5 CC5 ? ? DOUB CA1 CA2 ? ? SING CA2 CA3 ? ? DOUB CA3 CA4 ? ? SING CA4 CA5 ? ? DOUB CA5 CA6 ? ? SING CA6 CA1 ? ? SING CA6 CA7 ? ? DOUB CA7 CA8 ? ? SING CA8 CA9 ? ? DOUB CA9 CA0 ? ? SING CA0 CA5 ? ? SING CA1 HA1 ? ? SING CA2 HA2 ? ? SING CA3 HA3 ? ? SING CA4 HA4 ? ? SING CA7 HA7 ? ? SING CA8 HA8 ? ? SING CA9 HA9 ? ? SING CA0 HA0 ? ? SING CC1 RU ? ? SING CC2 RU ? ? SING CC3 RU ? ? SING CC4 RU ? ? SING CC5 RU ? ? SING CA1 RU ? ? SING CA2 RU ? ? SING CA3 RU ? ? SING CA4 RU ? ? SING CA5 RU ? ? SING CA6 RU ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $entity 'honey bee' 7460 Eukaryota Metazoa Apis Mellifera 'natural toxin from Apis Mellifera with [(C5H5)Ru]+ fragment coordinated to tryptophan residue' 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 'purified from the natural source' . . . . . 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 $entity 6 mM 'natural abundance' CD3OH 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS_SOLVE _Saveframe_category software _Name CNS_SOLVE _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 0.3 pH pressure 1 . atm temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 methanol C 13 'methyl carbon' ppm 49.00 internal direct . . . 1 methanol H 1 'methyl protons' ppm 3.31 internal direct . . . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D DQF-COSY' '2D 1H-1H NOESY' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _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 HA2 H 3.893 . . 2 1 1 GLY HA3 H 4.306 . . 3 1 1 GLY CA C 40.53 . 1 4 2 2 ILE H H 9.067 . 1 5 2 2 ILE HA H 4.042 . 1 6 2 2 ILE HB H 1.893 . 1 7 2 2 ILE HG12 H 1.371 . . 8 2 2 ILE HG13 H 1.604 . . 9 2 2 ILE HG2 H 0.995 . 1 10 2 2 ILE HD1 H 1.024 . 1 11 2 2 ILE CA C 60.43 . 1 12 2 2 ILE CB C 36.14 . 1 13 3 3 GLY H H 8.961 . 1 14 3 3 GLY HA2 H 3.768 . . 15 3 3 GLY HA3 H 3.866 . . 16 4 4 ALA H H 7.928 . 1 17 4 4 ALA HA H 4.080 . 1 18 4 4 ALA HB H 1.546 . 1 19 4 4 ALA CA C 52.65 . 1 20 5 5 VAL H H 7.493 . 1 21 5 5 VAL HA H 3.579 . 1 22 5 5 VAL HB H 2.317 . 1 23 5 5 VAL HG1 H 1.101 . . 24 5 5 VAL HG2 H 0.983 . . 25 5 5 VAL CA C 63.91 . 1 26 6 6 LEU H H 8.26 . 1 27 6 6 LEU HA H 4.09 . 1 28 7 7 LYS H H 8.26 . 1 29 7 7 LYS HA H 4.09 . 1 30 8 8 VAL H H 8.153 . 1 31 8 8 VAL HA H 3.699 . 1 32 8 8 VAL HB H 2.352 . 1 33 8 8 VAL HG1 H 1.151 . . 34 8 8 VAL HG2 H 1.010 . . 35 8 8 VAL CA C 64.40 . 1 36 9 9 LEU H H 8.324 . 1 37 9 9 LEU HA H 4.157 . 1 38 9 9 LEU HB2 H 2.019 . . 39 9 9 LEU HB3 H 2.019 . . 40 9 9 LEU HG H 1.988 . 1 41 9 9 LEU HD1 H 0.916 . . 42 9 9 LEU HD2 H 0.916 . . 43 10 10 THR H H 8.132 . 1 44 10 10 THR HA H 4.150 . 1 45 10 10 THR HB H 4.337 . 1 46 10 10 THR CA C 62.65 . 1 47 10 10 THR HG2 H 1.323 . 1 48 10 10 THR CB C 66.90 . 1 49 11 11 THR HG2 H 1.323 . 1 50 11 11 THR H H 7.869 . 1 51 11 11 THR HA H 4.313 . 1 52 11 11 THR HB H 4.313 . 1 53 11 11 THR CA C 61.73 . 1 54 11 11 THR CB C 67.41 . 1 55 12 12 GLY H H 8.188 . 1 56 12 12 GLY HA2 H 4.120 . . 57 12 12 GLY HA3 H 3.958 . . 58 12 12 GLY CA C 43.24 . 1 59 13 13 LEU H H 8.321 . 1 60 13 13 LEU HA H 4.388 . 1 61 13 13 LEU HB2 H 1.989 . . 62 13 13 LEU HB3 H 1.921 . . 63 13 13 LEU HG H 1.815 . 1 64 13 13 LEU HD1 H 1.060 . . 65 13 13 LEU HD2 H 0.994 . . 66 13 13 LEU CA C 56.76 . 1 67 14 14 PRO HA H 4.240 . 1 68 14 14 PRO HB2 H 2.357 . . 69 14 14 PRO HB3 H 1.962 . . 70 14 14 PRO HG2 H 2.248 . . 71 14 14 PRO HG3 H 1.962 . . 72 14 14 PRO HD2 H 3.796 . . 73 14 14 PRO HD3 H 3.796 . . 74 14 14 PRO CA C 64.11 . 1 75 14 14 PRO CD C 47.31 . 1 76 15 15 ALA H H 7.554 . 1 77 15 15 ALA HA H 4.189 . 1 78 15 15 ALA HB H 1.579 . 1 79 16 16 LEU H H 8.166 . 1 80 16 16 LEU HA H 4.235 . 1 81 16 16 LEU HB2 H 2.085 . . 82 16 16 LEU HB3 H 1.780 . . 83 16 16 LEU HG H 1.780 . 1 84 16 16 LEU HD1 H 0.961 . . 85 16 16 LEU HD2 H 0.961 . . 86 16 16 LEU CA C 55.95 . 1 87 17 17 ILE H H 8.611 . 1 88 17 17 ILE HA H 3.728 . 1 89 17 17 ILE HB H 2.078 . 1 90 17 17 ILE HG12 H 1.783 . . 91 17 17 ILE HG13 H 1.307 . . 92 17 17 ILE HG2 H 0.897 . 1 93 17 17 ILE HD1 H 0.979 . 1 94 17 17 ILE CA C 62.46 . 1 95 18 18 SER H H 8.395 . 1 96 18 18 SER HA H 4.123 . 1 97 18 18 SER HB2 H 4.053 . . 98 18 18 SER HB3 H 4.053 . . 99 18 18 SER CA C 54.95 . 1 100 18 18 SER CB C 55.83 . 1 101 19 19 TRP H H 8.436 . 1 102 19 19 TRP HA H 4.148 . 1 103 19 19 TRP HB2 H 3.581 . . 104 19 19 TRP HB3 H 3.446 . . 105 19 19 TRP HD1 H 7.628 . 1 106 19 19 TRP HE1 H 8.593 . 1 107 19 19 TRP HE3 H 7.044 . 1 108 19 19 TRP HZ2 H 6.845 . 1 109 19 19 TRP HZ3 H 5.959 . 1 110 19 19 TRP HH2 H 5.865 . 1 111 19 19 TRP CA C 58.82 . 1 112 20 20 ILE H H 8.564 . 1 113 20 20 ILE HA H 3.540 . 1 114 20 20 ILE HB H 2.112 . 1 115 20 20 ILE HG12 H 2.141 . . 116 20 20 ILE HG13 H 1.209 . . 117 20 20 ILE HG2 H 0.964 . 1 118 20 20 ILE CA C 63.30 . 1 119 21 21 LYS H H 8.594 . 1 120 21 21 LYS HA H 3.890 . 1 121 21 21 LYS HB2 H 1.929 . . 122 21 21 LYS HB3 H 1.995 . . 123 21 21 LYS HG2 H 1.434 . . 124 21 21 LYS HG3 H 1.434 . . 125 21 21 LYS HD2 H 1.671 . . 126 21 21 LYS HD3 H 1.671 . . 127 21 21 LYS HE2 H 2.891 . . 128 21 21 LYS HE3 H 2.891 . . 129 21 21 LYS CA C 57.90 . 1 130 22 22 ARG H H 8.26 . 1 131 22 22 ARG HA H 4.091 . 1 132 22 22 ARG HB2 H 1.977 . . 133 22 22 ARG HB3 H 1.977 . . 134 22 22 ARG HD2 H 3.188 . . 135 22 22 ARG HD3 H 3.188 . . 136 22 22 ARG HE H 7.364 . 1 137 23 23 LYS H H 8.325 . 1 138 23 23 LYS HA H 4.15 . 1 139 24 24 ARG H H 8.222 . 1 140 24 24 ARG HA H 4.094 . 1 141 24 24 ARG HB2 H 1.984 . . 142 24 24 ARG HB3 H 1.984 . . 143 24 24 ARG HD2 H 3.139 . . 144 24 24 ARG HD3 H 3.139 . . 145 24 24 ARG HE H 7.536 . 1 146 25 25 GLN H H 7.986 . 1 147 25 25 GLN HA H 4.120 . 1 148 25 25 GLN HB2 H 2.332 . . 149 25 25 GLN HB3 H 2.301 . . 150 25 25 GLN HG2 H 2.611 . . 151 25 25 GLN HG3 H 2.168 . . 152 26 26 GLN H H 7.777 . 1 153 26 26 GLN HA H 4.199 . 1 154 26 26 GLN HB2 H 2.178 . . 155 26 26 GLN HB3 H 2.178 . . 156 26 26 GLN HG2 H 2.564 . . 157 26 26 GLN HG3 H 2.551 . . 158 26 26 GLN CA C 53.77 . 1 stop_ save_