data_50408 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; V98A EcRNHI 15N-1H Backbone Chemical Shifts ; _BMRB_accession_number 50408 _BMRB_flat_file_name bmr50408.str _Entry_type original _Submission_date 2020-07-24 _Accession_date 2020-07-24 _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 Martin James A. . 2 Robustelli Paul . . 3 Palmer Arthur G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "15N chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-07-30 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 50407 'V98A EcRNHI* (Cys-free) 15N-1H Backbone Chemical Shifts' 50409 'SoRNHI 15N-1H Backbone Chemical Shifts' stop_ _Original_release_date 2020-07-24 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Quantifying the relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues ; _Citation_status submitted _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 Martin James A. . 2 Robustelli Paul . . 3 Palmer Arthur G. . stop_ _Journal_abbreviation Biochemistry _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'V98A EcRNHI' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'V98A EcRNHI' $entity_1 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_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; MLKQVEIFTDGSCLGNPGPG GYGAILRYRGREKTFSAGYT RTTNNRMELMAAIVALEALK EHCEVILSTDSQYVRQGITQ WIHNWKKRGWKTADKKPAKN VDLWQRLDAALGQHQIKWEW VKGHAGHPENERCDELARAA AMNPTLEDTGYQVEV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 LYS 4 GLN 5 VAL 6 GLU 7 ILE 8 PHE 9 THR 10 ASP 11 GLY 12 SER 13 CYS 14 LEU 15 GLY 16 ASN 17 PRO 18 GLY 19 PRO 20 GLY 21 GLY 22 TYR 23 GLY 24 ALA 25 ILE 26 LEU 27 ARG 28 TYR 29 ARG 30 GLY 31 ARG 32 GLU 33 LYS 34 THR 35 PHE 36 SER 37 ALA 38 GLY 39 TYR 40 THR 41 ARG 42 THR 43 THR 44 ASN 45 ASN 46 ARG 47 MET 48 GLU 49 LEU 50 MET 51 ALA 52 ALA 53 ILE 54 VAL 55 ALA 56 LEU 57 GLU 58 ALA 59 LEU 60 LYS 61 GLU 62 HIS 63 CYS 64 GLU 65 VAL 66 ILE 67 LEU 68 SER 69 THR 70 ASP 71 SER 72 GLN 73 TYR 74 VAL 75 ARG 76 GLN 77 GLY 78 ILE 79 THR 80 GLN 81 TRP 82 ILE 83 HIS 84 ASN 85 TRP 86 LYS 87 LYS 88 ARG 89 GLY 90 TRP 91 LYS 92 THR 93 ALA 94 ASP 95 LYS 96 LYS 97 PRO 98 ALA 99 LYS 100 ASN 101 VAL 102 ASP 103 LEU 104 TRP 105 GLN 106 ARG 107 LEU 108 ASP 109 ALA 110 ALA 111 LEU 112 GLY 113 GLN 114 HIS 115 GLN 116 ILE 117 LYS 118 TRP 119 GLU 120 TRP 121 VAL 122 LYS 123 GLY 124 HIS 125 ALA 126 GLY 127 HIS 128 PRO 129 GLU 130 ASN 131 GLU 132 ARG 133 CYS 134 ASP 135 GLU 136 LEU 137 ALA 138 ARG 139 ALA 140 ALA 141 ALA 142 MET 143 ASN 144 PRO 145 THR 146 LEU 147 GLU 148 ASP 149 THR 150 GLY 151 TYR 152 GLN 153 VAL 154 GLU 155 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli . plasmid pET-25b(+) 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $entity_1 325 uM 250 400 '[U-100% 13C; U-100% 15N]' 'deuterated sodium acetate' 50 mM . . 'natural abundance' 'sodium chloride' 50 mM . . 'natural abundance' 'sodium azide' 0.02 '% (w/v)' . . 'natural abundance' DTT 1 mM . . 'natural abundance' DSS 3 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRFAM-SPARKY _Version . loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N 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 'ionic strength' 0.050 . M pH 5.5 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CA)CO' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'V98A EcRNHI' _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 3 3 LYS H H 8.723 . . 2 3 3 LYS N N 123.5 . . 3 4 4 GLN H H 8.288 . . 4 4 4 GLN N N 122.9 . . 5 5 5 VAL H H 8.822 . . 6 5 5 VAL N N 122.3 . . 7 6 6 GLU H H 8.615 . . 8 6 6 GLU N N 124.1 . . 9 7 7 ILE H H 8.587 . . 10 7 7 ILE N N 121.9 . . 11 8 8 PHE H H 9.156 . . 12 8 8 PHE N N 128.4 . . 13 9 9 THR H H 8.01 . . 14 9 9 THR N N 109.5 . . 15 10 10 ASP H H 9.026 . . 16 10 10 ASP N N 120.2 . . 17 11 11 GLY H H 8.605 . . 18 11 11 GLY N N 106.6 . . 19 12 12 SER H H 8.784 . . 20 12 12 SER N N 113.6 . . 21 13 13 CYS H H 8.437 . . 22 13 13 CYS N N 123.6 . . 23 14 14 LEU H H 9.033 . . 24 14 14 LEU N N 128.5 . . 25 15 15 GLY H H 7.837 . . 26 15 15 GLY N N 107.7 . . 27 16 16 ASN H H 8.244 . . 28 16 16 ASN N N 116.3 . . 29 18 18 GLY H H 8.3 . . 30 18 18 GLY N N 105.3 . . 31 20 20 GLY H H 8.96 . . 32 20 20 GLY N N 108.5 . . 33 21 21 GLY H H 9.037 . . 34 21 21 GLY N N 106.6 . . 35 22 22 TYR H H 7.866 . . 36 22 22 TYR N N 113.4 . . 37 23 23 GLY H H 8.958 . . 38 23 23 GLY N N 106.2 . . 39 24 24 ALA H H 9.502 . . 40 24 24 ALA N N 126.1 . . 41 25 25 ILE H H 9.03 . . 42 25 25 ILE N N 120.9 . . 43 26 26 LEU H H 9.198 . . 44 26 26 LEU N N 129.1 . . 45 27 27 ARG H H 9.929 . . 46 27 27 ARG N N 126.6 . . 47 28 28 TYR H H 8.623 . . 48 28 28 TYR N N 125.3 . . 49 29 29 ARG H H 9.368 . . 50 29 29 ARG N N 127.1 . . 51 30 30 GLY H H 8.717 . . 52 30 30 GLY N N 105.1 . . 53 31 31 ARG H H 7.962 . . 54 31 31 ARG N N 121.1 . . 55 32 32 GLU H H 8.726 . . 56 32 32 GLU N N 122.4 . . 57 33 33 LYS H H 9.198 . . 58 33 33 LYS N N 125 . . 59 34 34 THR H H 8.14 . . 60 34 34 THR N N 114.7 . . 61 35 35 PHE H H 9.294 . . 62 35 35 PHE N N 120.6 . . 63 36 36 SER H H 8.392 . . 64 36 36 SER N N 113.9 . . 65 37 37 ALA H H 6.345 . . 66 37 37 ALA N N 120.7 . . 67 38 38 GLY H H 8.599 . . 68 38 38 GLY N N 106.3 . . 69 39 39 TYR H H 9.676 . . 70 39 39 TYR N N 122.9 . . 71 40 40 THR H H 8.795 . . 72 40 40 THR N N 113.5 . . 73 41 41 ARG H H 7.766 . . 74 41 41 ARG N N 120.1 . . 75 42 42 THR H H 8.825 . . 76 42 42 THR N N 125.2 . . 77 43 43 THR H H 8.533 . . 78 43 43 THR N N 106.5 . . 79 44 44 ASN H H 9.187 . . 80 44 44 ASN N N 120.7 . . 81 45 45 ASN H H 8.574 . . 82 45 45 ASN N N 116.5 . . 83 46 46 ARG H H 7.347 . . 84 46 46 ARG N N 116.5 . . 85 47 47 MET H H 7.697 . . 86 47 47 MET N N 118.2 . . 87 48 48 GLU H H 8.413 . . 88 48 48 GLU N N 119.4 . . 89 49 49 LEU H H 7.245 . . 90 49 49 LEU N N 116.5 . . 91 50 50 MET H H 8.695 . . 92 50 50 MET N N 118.9 . . 93 51 51 ALA H H 7.698 . . 94 51 51 ALA N N 117.1 . . 95 52 52 ALA H H 6.454 . . 96 52 52 ALA N N 113.9 . . 97 53 53 ILE H H 7.92 . . 98 53 53 ILE N N 116.7 . . 99 54 54 VAL H H 8.25 . . 100 54 54 VAL N N 116.9 . . 101 55 55 ALA H H 6.876 . . 102 55 55 ALA N N 119.5 . . 103 56 56 LEU H H 7.589 . . 104 56 56 LEU N N 112.8 . . 105 57 57 GLU H H 8.735 . . 106 57 57 GLU N N 118.6 . . 107 58 58 ALA H H 7.072 . . 108 58 58 ALA N N 119.7 . . 109 59 59 LEU H H 7.146 . . 110 59 59 LEU N N 118.3 . . 111 60 60 LYS H H 8.564 . . 112 60 60 LYS N N 122.1 . . 113 61 61 GLU H H 7.647 . . 114 61 61 GLU N N 116.6 . . 115 62 62 HIS H H 8.462 . . 116 62 62 HIS N N 119.3 . . 117 64 64 GLU H H 8.773 . . 118 64 64 GLU N N 122.7 . . 119 65 65 VAL H H 8.83 . . 120 65 65 VAL N N 125.7 . . 121 66 66 ILE H H 8.215 . . 122 66 66 ILE N N 127.6 . . 123 67 67 LEU H H 8.562 . . 124 67 67 LEU N N 134.4 . . 125 68 68 SER H H 8.725 . . 126 68 68 SER N N 120.9 . . 127 69 69 THR H H 8.503 . . 128 69 69 THR N N 119.7 . . 129 70 70 ASP H H 8.93 . . 130 70 70 ASP N N 127.6 . . 131 71 71 SER H H 8.31 . . 132 71 71 SER N N 115.5 . . 133 72 72 GLN H H 9.372 . . 134 72 72 GLN N N 132.7 . . 135 73 73 TYR H H 8.725 . . 136 73 73 TYR N N 123.6 . . 137 74 74 VAL H H 8.021 . . 138 74 74 VAL N N 117.5 . . 139 75 75 ARG H H 6.954 . . 140 75 75 ARG N N 117.7 . . 141 76 76 GLN H H 8.102 . . 142 76 76 GLN N N 120.6 . . 143 77 77 GLY H H 7.67 . . 144 77 77 GLY N N 106.7 . . 145 78 78 ILE H H 8.316 . . 146 78 78 ILE N N 120.4 . . 147 79 79 THR H H 7.714 . . 148 79 79 THR N N 107.9 . . 149 80 80 GLN H H 7.531 . . 150 80 80 GLN N N 117.6 . . 151 81 81 TRP H H 7.189 . . 152 81 81 TRP N N 118.4 . . 153 82 82 ILE H H 8.387 . . 154 82 82 ILE N N 117.8 . . 155 83 83 HIS H H 8.081 . . 156 83 83 HIS N N 118.4 . . 157 84 84 ASN H H 7.459 . . 158 84 84 ASN N N 117.4 . . 159 85 85 TRP H H 8.131 . . 160 85 85 TRP N N 120.4 . . 161 86 86 LYS H H 8.093 . . 162 86 86 LYS N N 119.1 . . 163 87 87 LYS H H 7.303 . . 164 87 87 LYS N N 118.3 . . 165 88 88 ARG H H 7.389 . . 166 88 88 ARG N N 117 . . 167 89 89 GLY H H 7.843 . . 168 89 89 GLY N N 109.6 . . 169 90 90 TRP H H 8.201 . . 170 90 90 TRP N N 114.3 . . 171 91 91 LYS H H 7.077 . . 172 91 91 LYS N N 117.6 . . 173 92 92 THR H H 8.658 . . 174 92 92 THR N N 110.8 . . 175 93 93 ALA H H 8.899 . . 176 93 93 ALA N N 124.1 . . 177 94 94 ASP H H 8.023 . . 178 94 94 ASP N N 115.6 . . 179 95 95 LYS H H 8.083 . . 180 95 95 LYS N N 113.8 . . 181 96 96 LYS H H 7.599 . . 182 96 96 LYS N N 120 . . 183 98 98 ALA H H 7.679 . . 184 98 98 ALA N N 124.7 . . 185 99 99 LYS H H 8.198 . . 186 99 99 LYS N N 121.8 . . 187 100 100 ASN H H 9.299 . . 188 100 100 ASN N N 114.9 . . 189 101 101 VAL H H 7.824 . . 190 101 101 VAL N N 118.7 . . 191 102 102 ASP H H 8.712 . . 192 102 102 ASP N N 119.2 . . 193 103 103 LEU H H 7.272 . . 194 103 103 LEU N N 118.9 . . 195 104 104 TRP H H 8.538 . . 196 104 104 TRP N N 121.2 . . 197 105 105 GLN H H 8.44 . . 198 105 105 GLN N N 116.4 . . 199 106 106 ARG H H 6.981 . . 200 106 106 ARG N N 121.1 . . 201 107 107 LEU H H 8.73 . . 202 107 107 LEU N N 121.7 . . 203 108 108 ASP H H 8.743 . . 204 108 108 ASP N N 118.5 . . 205 109 109 ALA H H 7.832 . . 206 109 109 ALA N N 119.3 . . 207 110 110 ALA H H 7.62 . . 208 110 110 ALA N N 121 . . 209 111 111 LEU H H 8.694 . . 210 111 111 LEU N N 117.6 . . 211 112 112 GLY H H 7.534 . . 212 112 112 GLY N N 101.7 . . 213 113 113 GLN H H 7.522 . . 214 113 113 GLN N N 117.3 . . 215 115 115 GLN H H 8.458 . . 216 115 115 GLN N N 121 . . 217 116 116 ILE H H 8.567 . . 218 116 116 ILE N N 125.9 . . 219 117 117 LYS H H 8.752 . . 220 117 117 LYS N N 129.8 . . 221 118 118 TRP H H 8.267 . . 222 118 118 TRP N N 126.1 . . 223 119 119 GLU H H 8.941 . . 224 119 119 GLU N N 126.6 . . 225 120 120 TRP H H 7.921 . . 226 120 120 TRP N N 125.9 . . 227 121 121 VAL H H 8.023 . . 228 121 121 VAL N N 123.6 . . 229 122 122 LYS H H 8.468 . . 230 122 122 LYS N N 124.4 . . 231 123 123 GLY H H 8.449 . . 232 123 123 GLY N N 111.4 . . 233 124 124 HIS H H 8.573 . . 234 124 124 HIS N N 116.6 . . 235 125 125 ALA H H 8.126 . . 236 125 125 ALA N N 123.7 . . 237 126 126 GLY H H 8.649 . . 238 126 126 GLY N N 109.8 . . 239 127 127 HIS H H 8.377 . . 240 127 127 HIS N N 118.5 . . 241 129 129 GLU H H 9.301 . . 242 129 129 GLU N N 117.8 . . 243 130 130 ASN H H 7.628 . . 244 130 130 ASN N N 117.2 . . 245 131 131 GLU H H 7.823 . . 246 131 131 GLU N N 120.2 . . 247 132 132 ARG H H 7.999 . . 248 132 132 ARG N N 119.9 . . 249 133 133 CYS H H 8.103 . . 250 133 133 CYS N N 117.9 . . 251 134 134 ASP H H 7.782 . . 252 134 134 ASP N N 120.7 . . 253 135 135 GLU H H 7.821 . . 254 135 135 GLU N N 119.1 . . 255 136 136 LEU H H 8.28 . . 256 136 136 LEU N N 120.3 . . 257 137 137 ALA H H 8.316 . . 258 137 137 ALA N N 122.7 . . 259 138 138 ARG H H 8.21 . . 260 138 138 ARG N N 116.6 . . 261 139 139 ALA H H 7.864 . . 262 139 139 ALA N N 120.5 . . 263 140 140 ALA H H 7.861 . . 264 140 140 ALA N N 121.8 . . 265 141 141 ALA H H 7.757 . . 266 141 141 ALA N N 119.3 . . 267 142 142 MET H H 7.079 . . 268 142 142 MET N N 111 . . 269 143 143 ASN H H 7.4 . . 270 143 143 ASN N N 117 . . 271 145 145 THR H H 7.472 . . 272 145 145 THR N N 108.6 . . 273 146 146 LEU H H 8.062 . . 274 146 146 LEU N N 123.5 . . 275 147 147 GLU H H 8.351 . . 276 147 147 GLU N N 118 . . 277 148 148 ASP H H 10.03 . . 278 148 148 ASP N N 125.7 . . 279 149 149 THR H H 7.857 . . 280 149 149 THR N N 116.6 . . 281 150 150 GLY H H 8.019 . . 282 150 150 GLY N N 106.8 . . 283 151 151 TYR H H 7.239 . . 284 151 151 TYR N N 121.4 . . 285 152 152 GLN H H 7.578 . . 286 152 152 GLN N N 126.1 . . 287 153 153 VAL H H 7.863 . . 288 153 153 VAL N N 120.7 . . 289 154 154 GLU H H 8.247 . . 290 154 154 GLU N N 125.4 . . 291 155 155 VAL H H 7.739 . . 292 155 155 VAL N N 125.5 . . stop_ save_