data_25084 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Sp Cdc5-D3 ; _BMRB_accession_number 25084 _BMRB_flat_file_name bmr25084.str _Entry_type original _Submission_date 2014-07-10 _Accession_date 2014-07-10 _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 Collier Scott E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 60 "13C chemical shifts" 184 "15N chemical shifts" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-11 original BMRB . stop_ _Original_release_date 2014-07-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and functional insights into the N-terminus of Schizosaccharomyces pombe Cdc5 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25263959 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Collier Scott E. . 2 Voehler Markus . . 3 Peng Dungeng . . 4 Ohi Ryomi . . 5 Gould Kathleen L. . 6 Reiter Nicholas J. . 7 Ohi Melanie D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 53 _Journal_issue 41 _Journal_ISSN 1520-4995 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6439 _Page_last 6451 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Cdc5-D3 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Cdc5-D3 monomer' $Cdc5-D3_(aa_155-214) stop_ _System_molecular_weight 7471.6 _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cdc5-D3_(aa_155-214) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Cdc5-D3_(aa_155-214) _Molecular_mass 7471.6 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 63 _Mol_residue_sequence ; GSHMDEDEKEMLSEARARLA NTQGKKAKRKDREKQLELTR RLSHLQKRRELKAAGINIKL FRR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 ASP 6 GLU 7 ASP 8 GLU 9 LYS 10 GLU 11 MET 12 LEU 13 SER 14 GLU 15 ALA 16 ARG 17 ALA 18 ARG 19 LEU 20 ALA 21 ASN 22 THR 23 GLN 24 GLY 25 LYS 26 LYS 27 ALA 28 LYS 29 ARG 30 LYS 31 ASP 32 ARG 33 GLU 34 LYS 35 GLN 36 LEU 37 GLU 38 LEU 39 THR 40 ARG 41 ARG 42 LEU 43 SER 44 HIS 45 LEU 46 GLN 47 LYS 48 ARG 49 ARG 50 GLU 51 LEU 52 LYS 53 ALA 54 ALA 55 GLY 56 ILE 57 ASN 58 ILE 59 LYS 60 LEU 61 PHE 62 ARG 63 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP P39964 'Pre-mRNA-splicing factor cdc5' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Cdc5-D3_(aa_155-214) E.coli 562 Bacteria . Escherichia coli 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 $Cdc5-D3_(aa_155-214) 'recombinant technology' . Escherichia coli . pET15-b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Cdc5-D3_(aa_155-214)_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Cdc5-D3_(aa_155-214) 370 uM '[U-99% 13C; U-99% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 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-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $Cdc5-D3_(aa_155-214)_sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6 . pH pressure 1 . atm temperature 293 . 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 DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 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-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HN(CA)CO' stop_ loop_ _Sample_label $Cdc5-D3_(aa_155-214)_sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Cdc5-D3 monomer' _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 2 SER C C 174.66 . . 2 2 2 SER CA C 58.57 . . 3 2 2 SER CB C 64.42 . . 4 3 3 HIS H H 8.696 . . 5 3 3 HIS C C 174.6 . . 6 3 3 HIS CA C 55.81 . . 7 3 3 HIS CB C 29.08 . . 8 3 3 HIS N N 120.7 . . 9 4 4 MET H H 8.434 . . 10 4 4 MET C C 175.9 . . 11 4 4 MET CA C 55.98 . . 12 4 4 MET CB C 32.915 . . 13 4 4 MET N N 121.8 . . 14 5 5 ASP H H 8.451 . . 15 5 5 ASP C C 176.5 . . 16 5 5 ASP CA C 54.87 . . 17 5 5 ASP CB C 41.115 . . 18 5 5 ASP N N 121.4 . . 19 6 6 GLU H H 8.367 . . 20 6 6 GLU C C 176.7 . . 21 6 6 GLU CA C 57.435 . . 22 6 6 GLU CB C 30.175 . . 23 6 6 GLU N N 120.6 . . 24 7 7 ASP H H 8.341 . . 25 7 7 ASP C C 177 . . 26 7 7 ASP CA C 55.07 . . 27 7 7 ASP CB C 41.14 . . 28 7 7 ASP N N 120.9 . . 29 8 8 GLU H H 8.334 . . 30 8 8 GLU C C 177.3 . . 31 8 8 GLU CA C 57.505 . . 32 8 8 GLU CB C 28.85 . . 33 8 8 GLU N N 121.7 . . 34 9 9 LYS H H 8.201 . . 35 9 9 LYS C C 178.4 . . 36 9 9 LYS CA C 56.625 . . 37 9 9 LYS CB C 42.13 . . 38 9 9 LYS N N 122.3 . . 39 10 10 GLU H H 8.204 . . 40 10 10 GLU C C 177.75 . . 41 10 10 GLU CA C 57.64 . . 42 10 10 GLU CB C 32.62 . . 43 10 10 GLU N N 120.7 . . 44 11 11 MET H H 8.235 . . 45 11 11 MET C C 177.3 . . 46 11 11 MET CA C 57.36 . . 47 11 11 MET CB C 29.905 . . 48 11 11 MET N N 120.5 . . 49 12 12 LEU H H 8.191 . . 50 12 12 LEU C C 178.2 . . 51 12 12 LEU CA C 56.16 . . 52 12 12 LEU CB C 42.03 . . 53 12 12 LEU N N 121.3 . . 54 13 13 SER H H 8.189 . . 55 13 13 SER C C 176.1 . . 56 13 13 SER CA C 59.89 . . 57 13 13 SER CB C 63.46 . . 58 13 13 SER N N 116.00 . . 59 14 14 GLU H H 8.44 . . 60 14 14 GLU C C 177.7 . . 61 14 14 GLU CA C 58.28 . . 62 14 14 GLU CB C 29.58 . . 63 14 14 GLU N N 122.8 . . 64 15 15 ALA H H 8.084 . . 65 15 15 ALA C C 179.5 . . 66 15 15 ALA CA C 54.28 . . 67 15 15 ALA CB C 18.57 . . 68 15 15 ALA N N 122.8 . . 69 16 16 ARG H H 8.057 . . 70 16 16 ARG C C 177.8 . . 71 16 16 ARG CA C 57.895 . . 72 16 16 ARG CB C 30.29 . . 73 16 16 ARG N N 118.3 . . 74 17 17 ALA H H 8.047 . . 75 17 17 ALA C C 178.9 . . 76 17 17 ALA CA C 53.85 . . 77 17 17 ALA CB C 18.605 . . 78 17 17 ALA N N 123.1 . . 79 18 18 ARG H H 7.99 . . 80 18 18 ARG C C 177.6 . . 81 18 18 ARG CA C 57.585 . . 82 18 18 ARG CB C 30.41 . . 83 18 18 ARG N N 118.5 . . 84 19 19 LEU H H 7.898 . . 85 19 19 LEU C C 177.8 . . 86 19 19 LEU CA C 55.93 . . 87 19 19 LEU CB C 42.16 . . 88 19 19 LEU N N 121.1 . . 89 20 20 ALA H H 8.011 . . 90 20 20 ALA C C 178.1 . . 91 20 20 ALA CA C 53.29 . . 92 20 20 ALA CB C 18.95 . . 93 20 20 ALA N N 122.9 . . 94 21 21 ASN H H 8.212 . . 95 21 21 ASN C C 176 . . 96 21 21 ASN CA C 53.68 . . 97 21 21 ASN CB C 38.755 . . 98 21 21 ASN N N 116.9 . . 99 22 22 THR H H 8.065 . . 100 22 22 THR C C 175.1 . . 101 22 22 THR CA C 62.73 . . 102 22 22 THR CB C 69.735 . . 103 22 22 THR N N 113.5 . . 104 23 23 GLN H H 8.348 . . 105 23 23 GLN C C 176.8 . . 106 23 23 GLN CA C 56.605 . . 107 23 23 GLN CB C 29.425 . . 108 23 23 GLN N N 121.8 . . 109 24 24 GLY H H 8.363 . . 110 24 24 GLY C C 174.4 . . 111 24 24 GLY CA C 45.543 . . 112 24 24 GLY N N 109.4 . . 113 25 25 LYS H H 8.134 . . 114 25 25 LYS C C 177 . . 115 25 25 LYS CA C 56.705 . . 116 25 25 LYS CB C 33.055 . . 117 25 25 LYS N N 120.8 . . 118 26 26 LYS H H 8.279 . . 119 26 26 LYS C C 176.5 . . 120 26 26 LYS CA C 56.73 . . 121 26 26 LYS CB C 32.96 . . 122 26 26 LYS N N 122 . . 123 27 27 ALA H H 8.224 . . 124 27 27 ALA C C 177.8 . . 125 27 27 ALA CA C 52.63 . . 126 27 27 ALA CB C 19.28 . . 127 27 27 ALA N N 125.1 . . 128 28 28 LYS H H 8.306 . . 129 28 28 LYS C C 177 . . 130 28 28 LYS CA C 56.735 . . 131 28 28 LYS CB C 33 . . 132 28 28 LYS N N 121 . . 133 29 29 ARG H H 8.363 . . 134 29 29 ARG C C 176.8 . . 135 29 29 ARG CA C 56.765 . . 136 29 29 ARG CB C 31.825 . . 137 29 29 ARG N N 122.8 . . 138 30 30 LYS H H 8.499 . . 139 30 30 LYS C C 176.9 . . 140 30 30 LYS CA C 56.99 . . 141 30 30 LYS CB C 32.69 . . 142 30 30 LYS N N 122.5 . . 143 31 31 ASP H H 8.297 . . 144 31 31 ASP C C 176.95 . . 145 31 31 ASP CA C 55.26 . . 146 31 31 ASP CB C 41.065 . . 147 31 31 ASP N N 121.2 . . 148 32 32 ARG H H 8.263 . . 149 32 32 ARG C C 177.3 . . 150 32 32 ARG CA C 57.54 . . 151 32 32 ARG CB C 30.335 . . 152 32 32 ARG N N 121.1 . . 153 33 33 GLU H H 8.16 . . 154 33 33 GLU C C 177.3 . . 155 33 33 GLU CA C 57.64 . . 156 33 33 GLU CB C 30.4 . . 157 33 33 GLU N N 121.0 . . 158 34 34 LYS H H 8.365 . . 159 34 34 LYS C C 177.8 . . 160 34 34 LYS CA C 58.06 . . 161 34 34 LYS CB C 39.54 . . 162 34 34 LYS N N 120.6 . . 163 35 35 GLN H H 8.252 . . 164 35 35 GLN C C 177.35 . . 165 35 35 GLN CA C 57.22 . . 166 35 35 GLN CB C 29.385 . . 167 35 35 GLN N N 120.7 . . 168 36 36 LEU H H 8.228 . . 169 36 36 LEU C C 176.9 . . 170 36 36 LEU CA C 56.625 . . 171 36 36 LEU CB C 42.125 . . 172 36 36 LEU N N 122.3 . . 173 37 37 GLU C C 177.7 . . 174 37 37 GLU CA C 58.03 . . 175 37 37 GLU CB C 29.71 . . 176 38 38 LEU H H 8.072 . . 177 38 38 LEU C C 178.5 . . 178 38 38 LEU CA C 57.05 . . 179 38 38 LEU CB C 42.04 . . 180 38 38 LEU N N 121.5 . . 181 39 39 THR H H 8.051 . . 182 39 39 THR C C 175.8 . . 183 39 39 THR CA C 64.25 . . 184 39 39 THR CB C 69.45 . . 185 39 39 THR N N 113.6 . . 186 40 40 ARG H H 8.127 . . 187 40 40 ARG C C 177.4 . . 188 40 40 ARG CA C 57.755 . . 189 40 40 ARG CB C 30.39 . . 190 40 40 ARG N N 122.7 . . 191 41 41 ARG H H 8.191 . . 192 41 41 ARG C C 177.3 . . 193 41 41 ARG CA C 56.15 . . 194 41 41 ARG CB C 29.36 . . 195 41 41 ARG N N 121.3 . . 196 42 42 LEU H H 8.226 . . 197 42 42 LEU C C 178.3 . . 198 42 42 LEU CA C 56.28 . . 199 42 42 LEU CB C 42.17 . . 200 42 42 LEU N N 122.1 . . 201 43 43 SER H H 8.155 . . 202 43 43 SER C C 175.2 . . 203 43 43 SER CA C 59.52 . . 204 43 43 SER CB C 63.64 . . 205 43 43 SER N N 115.6 . . 206 44 44 HIS H H 8.239 . . 207 44 44 HIS C C 175.5 . . 208 44 44 HIS CA C 56.78 . . 209 44 44 HIS CB C 29.57 . . 210 44 44 HIS N N 120.3 . . 211 45 45 LEU H H 7.983 . . 212 45 45 LEU C C 177.7 . . 213 45 45 LEU CA C 56.04 . . 214 45 45 LEU CB C 42.21 . . 215 45 45 LEU N N 121.6 . . 216 46 46 GLN H H 8.201 . . 217 46 46 GLN C C 176.3 . . 218 46 46 GLN CA C 57.52 . . 219 46 46 GLN CB C 29.03 . . 220 46 46 GLN N N 120.4 . . 221 47 47 LYS H H 8.225 . . 222 47 47 LYS C C 176.9 . . 223 47 47 LYS CA C 56.71 . . 224 47 47 LYS CB C 32.83 . . 225 47 47 LYS N N 122.3 . . 226 48 48 ARG H H 8.252 . . 227 48 48 ARG C C 176.6 . . 228 48 48 ARG CA C 56.68 . . 229 48 48 ARG CB C 30.64 . . 230 48 48 ARG N N 121.8 . . 231 49 49 ARG H H 8.328 . . 232 49 49 ARG C C 176.5 . . 233 49 49 ARG CA C 56.67 . . 234 49 49 ARG CB C 30.64 . . 235 49 49 ARG N N 122.3 . . 236 50 50 GLU H H 8.425 . . 237 50 50 GLU C C 176.6 . . 238 50 50 GLU CA C 56.77 . . 239 50 50 GLU CB C 30.165 . . 240 50 50 GLU N N 122.2 . . 241 51 51 LEU H H 8.251 . . 242 51 51 LEU C C 177.5 . . 243 51 51 LEU CA C 55.605 . . 244 51 51 LEU CB C 42.275 . . 245 51 51 LEU N N 123.6 . . 246 52 52 LYS H H 8.243 . . 247 52 52 LYS C C 176.55 . . 248 52 52 LYS CA C 56.625 . . 249 52 52 LYS CB C 32.9 . . 250 52 52 LYS N N 122 . . 251 53 53 ALA H H 8.21 . . 252 53 53 ALA C C 177.4 . . 253 53 53 ALA CA C 52.615 . . 254 53 53 ALA CB C 19.255 . . 255 53 53 ALA N N 125 . . 256 54 54 ALA H H 8.204 . . 257 54 54 ALA C C 178.2 . . 258 54 54 ALA CA C 52.62 . . 259 54 54 ALA CB C 19.24 . . 260 54 54 ALA N N 123.1 . . 261 55 55 GLY H H 8.261 . . 262 55 55 GLY C C 174.1 . . 263 55 55 GLY CA C 45.39 . . 264 55 55 GLY N N 107.7 . . 265 56 56 ILE H H 7.907 . . 266 56 56 ILE C C 175.9 . . 267 56 56 ILE CA C 61.145 . . 268 56 56 ILE CB C 38.83 . . 269 56 56 ILE N N 119.5 . . 270 57 57 ASN H H 8.509 . . 271 57 57 ASN C C 175.2 . . 272 57 57 ASN CA C 53.245 . . 273 57 57 ASN CB C 38.74 . . 274 57 57 ASN N N 122.6 . . 275 58 58 ILE H H 8.034 . . 276 58 58 ILE C C 176.2 . . 277 58 58 ILE CA C 61.54 . . 278 58 58 ILE CB C 38.475 . . 279 58 58 ILE N N 121.5 . . 280 59 59 LYS H H 8.212 . . 281 59 59 LYS C C 176.3 . . 282 59 59 LYS CA C 55.89 . . 283 59 59 LYS CB C 32.85 . . 284 59 59 LYS N N 124.5 . . 285 60 60 LEU H H 7.97 . . 286 60 60 LEU C C 176.8 . . 287 60 60 LEU CA C 55.095 . . 288 60 60 LEU CB C 42.475 . . 289 60 60 LEU N N 122.4 . . 290 61 61 PHE H H 8.104 . . 291 61 61 PHE C C 175.2 . . 292 61 61 PHE CA C 57.675 . . 293 61 61 PHE CB C 39.66 . . 294 61 61 PHE N N 120.9 . . 295 62 62 ARG H H 8.126 . . 296 62 62 ARG C C 174.8 . . 297 62 62 ARG CA C 55.94 . . 298 62 62 ARG CB C 30.645 . . 299 62 62 ARG N N 123.5 . . 300 63 63 ARG H H 7.936 . . 301 63 63 ARG C C 173 . . 302 63 63 ARG CA C 57.6 . . 303 63 63 ARG CB C 31.32 . . 304 63 63 ARG N N 127.9 . . stop_ save_