data_26028 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain ; _BMRB_accession_number 26028 _BMRB_flat_file_name bmr26028.str _Entry_type original _Submission_date 2016-04-10 _Accession_date 2016-04-14 _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 Wittwer Matthias . . 2 Dames Sonja A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 "13C chemical shifts" 394 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-10-14 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26027 ; Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG) ; 26029 ; Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; 26030 ; Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; stop_ _Original_release_date 2016-10-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27632081 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wittwer Matthias . . 2 Dames Sonja A. . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 401 _Page_last 406 _Year 2016 _Details . loop_ _Keyword 'Mycobacterium tuberculosis' 'natively disordered protein' 'protein kinase G' 'redox-sensitive metal binding motif' rubredoxin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Protein kinase G (PknG) 1-147 natively disordered region + rubredoxin domain reduced, metal bound form' _Enzyme_commission_number 2.7.11.1 loop_ _Mol_system_component_name _Mol_label 'NORS & rubredoxin-domain (RD)' $His-PknG_1-147 ZN $entity_ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; The eukaryotic like serine /threonine protein kinase G promotes cellular survival of pathogenic mycobacteria by inhibiting phagosome-lysosome fusion within host macophages. ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_His-PknG_1-147 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common His-PknG_1-147 _Molecular_mass 18001.98 _Mol_thiol_state 'all other bound' _Details 'His-PknG 1-147 contains the NORS region & rubredoxin motif of mycobacterial protein kinase G' ############################## # Polymer residue sequence # ############################## _Residue_count 167 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MAKASETERSGPGTQPADAQ TATSATVRPLSTQAVFRPDF GDEDNFPHPTLGPDTEPQDR MATTSRVRPPVRRLGGGLVE IPRAPDIDPLEALMTNPVVP ESKRFCWNCGRPVGRSDSET KGASEGWCPYCGSPYSFLPQ LNPGDIV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 GLY 3 3 SER 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 SER 12 12 SER 13 13 GLY 14 14 LEU 15 15 VAL 16 16 PRO 17 17 ARG 18 18 GLY 19 19 SER 20 20 HIS 21 21 MET 22 22 ALA 23 23 LYS 24 24 ALA 25 25 SER 26 26 GLU 27 27 THR 28 28 GLU 29 29 ARG 30 30 SER 31 31 GLY 32 32 PRO 33 33 GLY 34 34 THR 35 35 GLN 36 36 PRO 37 37 ALA 38 38 ASP 39 39 ALA 40 40 GLN 41 41 THR 42 42 ALA 43 43 THR 44 44 SER 45 45 ALA 46 46 THR 47 47 VAL 48 48 ARG 49 49 PRO 50 50 LEU 51 51 SER 52 52 THR 53 53 GLN 54 54 ALA 55 55 VAL 56 56 PHE 57 57 ARG 58 58 PRO 59 59 ASP 60 60 PHE 61 61 GLY 62 62 ASP 63 63 GLU 64 64 ASP 65 65 ASN 66 66 PHE 67 67 PRO 68 68 HIS 69 69 PRO 70 70 THR 71 71 LEU 72 72 GLY 73 73 PRO 74 74 ASP 75 75 THR 76 76 GLU 77 77 PRO 78 78 GLN 79 79 ASP 80 80 ARG 81 81 MET 82 82 ALA 83 83 THR 84 84 THR 85 85 SER 86 86 ARG 87 87 VAL 88 88 ARG 89 89 PRO 90 90 PRO 91 91 VAL 92 92 ARG 93 93 ARG 94 94 LEU 95 95 GLY 96 96 GLY 97 97 GLY 98 98 LEU 99 99 VAL 100 100 GLU 101 101 ILE 102 102 PRO 103 103 ARG 104 104 ALA 105 105 PRO 106 106 ASP 107 107 ILE 108 108 ASP 109 109 PRO 110 110 LEU 111 111 GLU 112 112 ALA 113 113 LEU 114 114 MET 115 115 THR 116 116 ASN 117 117 PRO 118 118 VAL 119 119 VAL 120 120 PRO 121 121 GLU 122 122 SER 123 123 LYS 124 124 ARG 125 125 PHE 126 126 CYS 127 127 TRP 128 128 ASN 129 129 CYS 130 130 GLY 131 131 ARG 132 132 PRO 133 133 VAL 134 134 GLY 135 135 ARG 136 136 SER 137 137 ASP 138 138 SER 139 139 GLU 140 140 THR 141 141 LYS 142 142 GLY 143 143 ALA 144 144 SER 145 145 GLU 146 146 GLY 147 147 TRP 148 148 CYS 149 149 PRO 150 150 TYR 151 151 CYS 152 152 GLY 153 153 SER 154 154 PRO 155 155 TYR 156 156 SER 157 157 PHE 158 158 LEU 159 159 PRO 160 160 GLN 161 161 LEU 162 162 ASN 163 163 PRO 164 164 GLY 165 165 ASP 166 166 ILE 167 167 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? 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 _Strain _Gene_mnemonic $His-PknG_1-147 'Mycobacterium tuberculosis' 83332 Bacteria . Mycobacterium tuberculosis H37Rv 'pknG Rv0410c MTCY22G10.06c' 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 $His-PknG_1-147 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'PknG 1-147 / rubredoxin domain in metal bound state (reduced) / with coordinated Zn - ion' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $His-PknG_1-147 . mM 0.4 0.8 '[U-13C; U-15N]' TRIS-HCL 20 mM . . 'natural abundance' 'sodium chloride' 150 mM . . 'natural abundance' H2O 95 % . . 'natural abundance' D2O 5 % . . [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_spectrometer_2 _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 $sample_1 save_ save_3D_C(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(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_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 150 . mM pH 7.5 . pH pressure 1 . atm temperature 298 . 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 water C 13 protons ppm 4.773 na indirect . . . 0.251449530 water H 1 protons ppm 4.773 internal direct . . . 1.000000000 water N 15 protons ppm 4.773 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_assignments_pkng1-147tag_3l _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D C(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' 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 'NORS & rubredoxin-domain (RD)' _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 13 13 GLY CA C 45.319 0.15 1 2 14 14 LEU H H 7.998 0.02 1 3 14 14 LEU CA C 55.098 0.15 1 4 14 14 LEU N N 121.417 0.1 1 5 15 15 VAL H H 8.055 0.02 1 6 15 15 VAL CA C 59.794 0.15 1 7 15 15 VAL N N 122.412 0.1 1 8 16 16 PRO CA C 63.129 0.15 1 9 17 17 ARG H H 8.449 0.02 1 10 17 17 ARG CA C 56.398 0.15 1 11 17 17 ARG N N 121.933 0.1 1 12 26 26 GLU CA C 57.065 0.15 1 13 26 26 GLU CB C 30.264 0.15 1 14 26 26 GLU CG C 36.284 0.15 1 15 27 27 THR H H 8.087 0.02 1 16 27 27 THR C C 174.826 0.15 1 17 27 27 THR CA C 62.321 0.15 1 18 27 27 THR CB C 69.795 0.15 1 19 27 27 THR CG2 C 21.597 0.15 1 20 27 27 THR N N 113.913 0.1 1 21 28 28 GLU H H 8.283 0.02 1 22 28 28 GLU CA C 56.807 0.15 1 23 28 28 GLU CB C 30.243 0.15 1 24 28 28 GLU CG C 36.226 0.15 1 25 28 28 GLU N N 123.248 0.1 1 26 29 29 ARG H H 8.312 0.02 1 27 29 29 ARG C C 176.251 0.15 1 28 29 29 ARG CA C 56.133 0.15 1 29 29 29 ARG CB C 30.557 0.15 1 30 29 29 ARG CG C 26.984 0.15 1 31 29 29 ARG N N 122.045 0.1 1 32 30 30 SER H H 8.314 0.02 1 33 30 30 SER C C 174.558 0.15 1 34 30 30 SER CA C 58.283 0.15 1 35 30 30 SER CB C 64.179 0.15 1 36 30 30 SER N N 116.856 0.1 1 37 31 31 GLY H H 8.251 0.02 1 38 31 31 GLY CA C 44.670 0.15 1 39 31 31 GLY N N 110.500 0.1 1 40 33 33 GLY C C 174.456 0.15 1 41 33 33 GLY CA C 45.350 0.15 1 42 34 34 THR H H 7.959 0.02 1 43 34 34 THR C C 174.500 0.15 1 44 34 34 THR CA C 61.854 0.15 1 45 34 34 THR CB C 70.029 0.15 1 46 34 34 THR CG2 C 21.547 0.15 1 47 34 34 THR N N 113.323 0.1 1 48 35 35 GLN H H 8.450 0.02 1 49 35 35 GLN HE21 H 7.544 0.02 2 50 35 35 GLN HE22 H 6.843 0.02 2 51 35 35 GLN CA C 53.684 0.15 1 52 35 35 GLN CB C 28.907 0.15 1 53 35 35 GLN N N 123.922 0.1 1 54 35 35 GLN NE2 N 112.566 0.1 1 55 36 36 PRO C C 176.930 0.15 1 56 36 36 PRO CA C 63.268 0.15 1 57 36 36 PRO CB C 32.205 0.15 1 58 36 36 PRO CD C 50.657 0.15 1 59 36 36 PRO CG C 27.357 0.15 1 60 37 37 ALA H H 8.451 0.02 1 61 37 37 ALA C C 175.979 0.15 1 62 37 37 ALA CA C 52.843 0.15 1 63 37 37 ALA CB C 19.207 0.15 1 64 37 37 ALA N N 124.069 0.1 1 65 38 38 ASP H H 8.222 0.02 1 66 38 38 ASP C C 176.235 0.15 1 67 38 38 ASP CA C 54.220 0.15 1 68 38 38 ASP CB C 41.194 0.15 1 69 38 38 ASP N N 118.755 0.1 1 70 39 39 ALA H H 8.114 0.02 1 71 39 39 ALA C C 176.267 0.15 1 72 39 39 ALA CA C 52.899 0.15 1 73 39 39 ALA CB C 19.232 0.15 1 74 39 39 ALA N N 123.866 0.1 1 75 40 40 GLN H H 8.347 0.02 1 76 40 40 GLN HE21 H 7.524 0.02 2 77 40 40 GLN HE22 H 6.839 0.02 2 78 40 40 GLN C C 176.490 0.15 1 79 40 40 GLN CA C 56.150 0.15 1 80 40 40 GLN CB C 29.301 0.15 1 81 40 40 GLN CG C 33.887 0.15 1 82 40 40 GLN N N 118.770 0.1 1 83 40 40 GLN NE2 N 112.783 0.1 1 84 41 41 THR H H 8.075 0.02 1 85 41 41 THR C C 174.554 0.15 1 86 41 41 THR CA C 62.116 0.15 1 87 41 41 THR CB C 69.830 0.15 1 88 41 41 THR CG2 C 21.451 0.15 1 89 41 41 THR N N 114.816 0.1 1 90 42 42 ALA H H 8.317 0.02 1 91 42 42 ALA CA C 52.835 0.15 1 92 42 42 ALA CB C 19.277 0.15 1 93 42 42 ALA N N 126.360 0.1 1 94 45 45 ALA C C 177.861 0.15 1 95 45 45 ALA CA C 52.713 0.15 1 96 45 45 ALA CB C 19.299 0.15 1 97 46 46 THR H H 8.074 0.02 1 98 46 46 THR C C 174.490 0.15 1 99 46 46 THR CA C 62.202 0.15 1 100 46 46 THR CB C 69.853 0.15 1 101 46 46 THR CG2 C 21.554 0.15 1 102 46 46 THR N N 113.565 0.1 1 103 47 47 VAL H H 8.084 0.02 1 104 47 47 VAL C C 175.729 0.15 1 105 47 47 VAL CA C 62.207 0.15 1 106 47 47 VAL CB C 32.705 0.15 1 107 47 47 VAL CG1 C 20.782 0.15 2 108 47 47 VAL N N 123.251 0.1 1 109 48 48 ARG H H 8.371 0.02 1 110 48 48 ARG CA C 53.776 0.15 1 111 48 48 ARG CB C 30.271 0.15 1 112 48 48 ARG N N 126.367 0.1 1 113 49 49 PRO C C 176.916 0.15 1 114 49 49 PRO CA C 62.975 0.15 1 115 49 49 PRO CB C 32.167 0.15 1 116 49 49 PRO CD C 50.605 0.15 1 117 49 49 PRO CG C 27.284 0.15 1 118 50 50 LEU H H 8.380 0.02 1 119 50 50 LEU CA C 55.431 0.15 1 120 50 50 LEU CB C 42.410 0.15 1 121 50 50 LEU N N 122.463 0.1 1 122 52 52 THR CA C 62.055 0.15 1 123 52 52 THR CB C 69.596 0.15 1 124 52 52 THR CG2 C 21.555 0.15 1 125 53 53 GLN H H 8.240 0.02 1 126 53 53 GLN HE21 H 7.526 0.02 2 127 53 53 GLN HE22 H 6.840 0.02 2 128 53 53 GLN C C 175.556 0.15 1 129 53 53 GLN CA C 55.881 0.15 1 130 53 53 GLN CB C 29.676 0.15 1 131 53 53 GLN CG C 33.750 0.15 1 132 53 53 GLN N N 122.053 0.1 1 133 53 53 GLN NE2 N 112.535 0.1 1 134 54 54 ALA H H 8.245 0.02 1 135 54 54 ALA C C 177.375 0.15 1 136 54 54 ALA CA C 52.528 0.15 1 137 54 54 ALA CB C 19.353 0.15 1 138 54 54 ALA N N 125.518 0.1 1 139 55 55 VAL H H 7.947 0.02 1 140 55 55 VAL C C 175.642 0.15 1 141 55 55 VAL CA C 62.067 0.15 1 142 55 55 VAL CB C 33.040 0.15 1 143 55 55 VAL N N 118.993 0.1 1 144 56 56 PHE H H 8.318 0.02 1 145 56 56 PHE C C 174.912 0.15 1 146 56 56 PHE CA C 57.620 0.15 1 147 56 56 PHE CB C 39.788 0.15 1 148 56 56 PHE N N 124.615 0.1 1 149 57 57 ARG H H 8.108 0.02 1 150 57 57 ARG CA C 53.260 0.15 1 151 57 57 ARG CB C 30.804 0.15 1 152 57 57 ARG N N 125.210 0.1 1 153 58 58 PRO C C 177.626 0.15 1 154 58 58 PRO CA C 63.119 0.15 1 155 58 58 PRO CB C 32.042 0.15 1 156 58 58 PRO CD C 50.665 0.15 1 157 58 58 PRO CG C 27.090 0.15 1 158 59 59 ASP H H 8.305 0.02 1 159 59 59 ASP C C 175.934 0.15 1 160 59 59 ASP CA C 54.108 0.15 1 161 59 59 ASP CB C 41.101 0.15 1 162 59 59 ASP N N 119.225 0.1 1 163 60 60 PHE H H 8.063 0.02 1 164 60 60 PHE C C 176.245 0.15 1 165 60 60 PHE CA C 57.827 0.15 1 166 60 60 PHE CB C 39.561 0.15 1 167 60 60 PHE N N 120.158 0.1 1 168 61 61 GLY H H 8.388 0.02 1 169 61 61 GLY C C 173.922 0.15 1 170 61 61 GLY CA C 45.399 0.15 1 171 61 61 GLY N N 110.244 0.1 1 172 62 62 ASP H H 8.180 0.02 1 173 62 62 ASP C C 176.588 0.15 1 174 62 62 ASP CA C 54.465 0.15 1 175 62 62 ASP CB C 41.411 0.15 1 176 62 62 ASP N N 120.489 0.1 1 177 63 63 GLU H H 8.469 0.02 1 178 63 63 GLU C C 176.501 0.15 1 179 63 63 GLU CA C 57.153 0.15 1 180 63 63 GLU CB C 30.223 0.15 1 181 63 63 GLU CG C 36.321 0.15 1 182 63 63 GLU N N 120.573 0.1 1 183 64 64 ASP H H 8.289 0.02 1 184 64 64 ASP C C 175.914 0.15 1 185 64 64 ASP CA C 54.581 0.15 1 186 64 64 ASP CB C 41.210 0.15 1 187 64 64 ASP N N 120.337 0.1 1 188 65 65 ASN H H 8.114 0.02 1 189 65 65 ASN HD21 H 7.547 0.02 2 190 65 65 ASN HD22 H 6.839 0.02 2 191 65 65 ASN C C 174.454 0.15 1 192 65 65 ASN CA C 53.090 0.15 1 193 65 65 ASN CB C 39.183 0.15 1 194 65 65 ASN N N 118.323 0.1 1 195 65 65 ASN ND2 N 113.006 0.1 1 196 66 66 PHE H H 8.066 0.02 1 197 66 66 PHE CA C 55.701 0.15 1 198 66 66 PHE CB C 39.190 0.15 1 199 66 66 PHE N N 121.483 0.1 1 200 67 67 PRO C C 176.238 0.15 1 201 67 67 PRO CA C 62.893 0.15 1 202 67 67 PRO CB C 31.716 0.15 1 203 67 67 PRO CD C 50.314 0.15 1 204 67 67 PRO CG C 27.126 0.15 1 205 68 68 HIS H H 8.268 0.02 1 206 68 68 HIS CA C 54.460 0.15 1 207 68 68 HIS CB C 30.276 0.15 1 208 68 68 HIS N N 121.602 0.1 1 209 69 69 PRO C C 177.096 0.15 1 210 69 69 PRO CA C 63.412 0.15 1 211 69 69 PRO CB C 32.224 0.15 1 212 69 69 PRO CD C 50.483 0.15 1 213 69 69 PRO CG C 27.248 0.15 1 214 70 70 THR H H 8.412 0.02 1 215 70 70 THR C C 174.528 0.15 1 216 70 70 THR CA C 61.974 0.15 1 217 70 70 THR CB C 69.925 0.15 1 218 70 70 THR CG2 C 21.584 0.15 1 219 70 70 THR N N 114.914 0.1 1 220 71 71 LEU H H 8.354 0.02 1 221 71 71 LEU C C 177.368 0.15 1 222 71 71 LEU CA C 54.956 0.15 1 223 71 71 LEU CB C 42.649 0.15 1 224 71 71 LEU CD1 C 24.985 0.15 2 225 71 71 LEU CD2 C 23.203 0.15 2 226 71 71 LEU CG C 26.851 0.15 1 227 71 71 LEU N N 125.016 0.1 1 228 72 72 GLY H H 8.232 0.02 1 229 72 72 GLY CA C 44.600 0.15 1 230 72 72 GLY N N 109.907 0.1 1 231 73 73 PRO C C 176.951 0.15 1 232 73 73 PRO CA C 63.431 0.15 1 233 73 73 PRO CB C 32.233 0.15 1 234 73 73 PRO CD C 49.832 0.15 1 235 73 73 PRO CG C 26.959 0.15 1 236 74 74 ASP H H 8.466 0.02 1 237 74 74 ASP CA C 54.461 0.15 1 238 74 74 ASP CB C 40.942 0.15 1 239 74 74 ASP N N 119.621 0.1 1 240 75 75 THR H H 7.925 0.02 1 241 75 75 THR C C 174.445 0.15 1 242 75 75 THR CA C 61.915 0.15 1 243 75 75 THR CB C 70.011 0.15 1 244 75 75 THR CG2 C 21.603 0.15 1 245 75 75 THR N N 113.525 0.1 1 246 76 76 GLU H H 8.351 0.02 1 247 76 76 GLU CA C 54.652 0.15 1 248 76 76 GLU CB C 29.726 0.15 1 249 76 76 GLU N N 124.617 0.1 1 250 77 77 PRO C C 177.371 0.15 1 251 77 77 PRO CA C 63.536 0.15 1 252 77 77 PRO CB C 32.155 0.15 1 253 77 77 PRO CD C 50.639 0.15 1 254 77 77 PRO CG C 27.420 0.15 1 255 78 78 GLN H H 8.545 0.02 1 256 78 78 GLN HE21 H 7.504 0.02 2 257 78 78 GLN HE22 H 6.838 0.02 2 258 78 78 GLN CA C 56.172 0.15 1 259 78 78 GLN CB C 29.450 0.15 1 260 78 78 GLN CG C 33.687 0.15 1 261 78 78 GLN N N 120.129 0.1 1 262 78 78 GLN NE2 N 112.525 0.1 1 263 79 79 ASP H H 8.325 0.02 1 264 79 79 ASP C C 176.531 0.15 1 265 79 79 ASP CA C 54.420 0.15 1 266 79 79 ASP CB C 41.175 0.15 1 267 79 79 ASP N N 120.827 0.1 1 268 80 80 ARG H H 8.200 0.02 1 269 80 80 ARG C C 176.763 0.15 1 270 80 80 ARG CA C 56.641 0.15 1 271 80 80 ARG CB C 30.464 0.15 1 272 80 80 ARG CD C 43.316 0.15 1 273 80 80 ARG CG C 27.025 0.15 1 274 80 80 ARG N N 121.142 0.1 1 275 81 81 MET H H 8.282 0.02 1 276 81 81 MET C C 176.379 0.15 1 277 81 81 MET CA C 55.632 0.15 1 278 81 81 MET CB C 32.505 0.15 1 279 81 81 MET CG C 32.059 0.15 1 280 81 81 MET N N 119.841 0.1 1 281 82 82 ALA H H 8.158 0.02 1 282 82 82 ALA C C 178.126 0.15 1 283 82 82 ALA CA C 52.854 0.15 1 284 82 82 ALA CB C 19.233 0.15 1 285 82 82 ALA N N 124.475 0.1 1 286 83 83 THR H H 8.126 0.02 1 287 83 83 THR CA C 61.987 0.15 1 288 83 83 THR CB C 69.892 0.15 1 289 83 83 THR N N 112.916 0.1 1 290 90 90 PRO C C 175.964 0.15 1 291 90 90 PRO CA C 62.970 0.15 1 292 91 91 VAL H H 8.075 0.02 1 293 91 91 VAL CA C 62.414 0.15 1 294 91 91 VAL N N 120.136 0.1 1 295 96 96 GLY CA C 45.355 0.15 1 296 97 97 GLY H H 8.291 0.02 1 297 97 97 GLY C C 177.620 0.15 1 298 97 97 GLY CA C 45.165 0.15 1 299 97 97 GLY N N 108.672 0.1 1 300 98 98 LEU H H 8.097 0.02 1 301 98 98 LEU C C 177.254 0.15 1 302 98 98 LEU CA C 55.277 0.15 1 303 98 98 LEU CB C 42.642 0.15 1 304 98 98 LEU CD1 C 24.889 0.15 2 305 98 98 LEU CD2 C 23.366 0.15 2 306 98 98 LEU CG C 26.938 0.15 1 307 98 98 LEU N N 121.571 0.1 1 308 99 99 VAL H H 8.083 0.02 1 309 99 99 VAL C C 175.728 0.15 1 310 99 99 VAL CA C 62.133 0.15 1 311 99 99 VAL CB C 32.981 0.15 1 312 99 99 VAL CG1 C 20.796 0.15 2 313 99 99 VAL N N 120.770 0.1 1 314 100 100 GLU H H 8.387 0.02 1 315 100 100 GLU CA C 56.074 0.15 1 316 100 100 GLU CB C 30.706 0.15 1 317 100 100 GLU CG C 36.171 0.15 1 318 100 100 GLU N N 125.002 0.1 1 319 101 101 ILE H H 8.239 0.02 1 320 101 101 ILE CA C 58.538 0.15 1 321 101 101 ILE CB C 38.679 0.15 1 322 101 101 ILE N N 124.432 0.1 1 323 102 102 PRO CA C 63.133 0.15 1 324 102 102 PRO CB C 31.885 0.15 1 325 102 102 PRO CD C 51.073 0.15 1 326 102 102 PRO CG C 27.257 0.15 1 327 103 103 ARG H H 8.333 0.02 1 328 103 103 ARG C C 175.727 0.15 1 329 103 103 ARG CA C 55.671 0.15 1 330 103 103 ARG CB C 31.137 0.15 1 331 103 103 ARG CD C 43.325 0.15 1 332 103 103 ARG CG C 26.947 0.15 1 333 103 103 ARG N N 121.799 0.1 1 334 104 104 ALA H H 8.385 0.02 1 335 104 104 ALA CA C 50.564 0.15 1 336 104 104 ALA CB C 18.223 0.15 1 337 104 104 ALA N N 127.376 0.1 1 338 105 105 PRO C C 176.584 0.15 1 339 105 105 PRO CA C 63.179 0.15 1 340 105 105 PRO CB C 32.107 0.15 1 341 105 105 PRO CD C 50.559 0.15 1 342 105 105 PRO CG C 27.215 0.15 1 343 106 106 ASP H H 8.359 0.02 1 344 106 106 ASP C C 175.891 0.15 1 345 106 106 ASP CA C 54.431 0.15 1 346 106 106 ASP CB C 41.132 0.15 1 347 106 106 ASP N N 120.029 0.1 1 348 107 107 ILE H H 7.890 0.02 1 349 107 107 ILE C C 175.568 0.15 1 350 107 107 ILE CA C 60.537 0.15 1 351 107 107 ILE CB C 39.295 0.15 1 352 107 107 ILE CD1 C 12.658 0.15 1 353 107 107 ILE CG1 C 27.059 0.15 1 354 107 107 ILE CG2 C 17.245 0.15 1 355 107 107 ILE N N 120.095 0.1 1 356 108 108 ASP H H 8.519 0.02 1 357 108 108 ASP CA C 52.092 0.15 1 358 108 108 ASP CB C 41.689 0.15 1 359 108 108 ASP N N 126.838 0.1 1 360 109 109 PRO C C 177.729 0.15 1 361 109 109 PRO CA C 63.980 0.15 1 362 109 109 PRO CB C 32.255 0.15 1 363 109 109 PRO CD C 50.717 0.15 1 364 109 109 PRO CG C 27.174 0.15 1 365 110 110 LEU H H 8.334 0.02 1 366 110 110 LEU C C 178.481 0.15 1 367 110 110 LEU CA C 55.994 0.15 1 368 110 110 LEU CB C 41.606 0.15 1 369 110 110 LEU CD1 C 24.901 0.15 2 370 110 110 LEU CD2 C 23.089 0.15 2 371 110 110 LEU CG C 27.001 0.15 1 372 110 110 LEU N N 119.709 0.1 1 373 111 111 GLU H H 7.950 0.02 1 374 111 111 GLU C C 177.255 0.15 1 375 111 111 GLU CA C 57.548 0.15 1 376 111 111 GLU CB C 30.060 0.15 1 377 111 111 GLU CG C 36.260 0.15 1 378 111 111 GLU N N 120.422 0.1 1 379 112 112 ALA H H 8.041 0.02 1 380 112 112 ALA C C 178.065 0.15 1 381 112 112 ALA CA C 53.126 0.15 1 382 112 112 ALA CB C 18.967 0.15 1 383 112 112 ALA N N 123.144 0.1 1 384 113 113 LEU H H 7.856 0.02 1 385 113 113 LEU C C 177.757 0.15 1 386 113 113 LEU CA C 55.611 0.15 1 387 113 113 LEU CB C 42.347 0.15 1 388 113 113 LEU CD1 C 24.977 0.15 2 389 113 113 LEU CD2 C 23.339 0.15 2 390 113 113 LEU CG C 26.875 0.15 1 391 113 113 LEU N N 119.428 0.1 1 392 114 114 MET H H 8.077 0.02 1 393 114 114 MET C C 176.405 0.15 1 394 114 114 MET CA C 55.672 0.15 1 395 114 114 MET CB C 32.692 0.15 1 396 114 114 MET CG C 32.034 0.15 1 397 114 114 MET N N 119.399 0.1 1 398 115 115 THR H H 7.944 0.02 1 399 115 115 THR CA C 61.988 0.15 1 400 115 115 THR CB C 69.896 0.15 1 401 115 115 THR CG2 C 21.581 0.15 1 402 115 115 THR N N 113.907 0.1 1 403 116 116 ASN H H 8.293 0.02 1 404 116 116 ASN HD21 H 7.596 0.02 2 405 116 116 ASN HD22 H 6.883 0.02 2 406 116 116 ASN CA C 51.442 0.15 1 407 116 116 ASN CB C 39.121 0.15 1 408 116 116 ASN N N 121.827 0.1 1 409 116 116 ASN ND2 N 113.002 0.1 1 410 117 117 PRO C C 176.686 0.15 1 411 117 117 PRO CA C 63.230 0.15 1 412 117 117 PRO CB C 32.686 0.15 1 413 117 117 PRO CD C 50.556 0.15 1 414 117 117 PRO CG C 26.971 0.15 1 415 118 118 VAL H H 8.097 0.02 1 416 118 118 VAL C C 176.145 0.15 1 417 118 118 VAL CA C 62.134 0.15 1 418 118 118 VAL CB C 32.686 0.15 1 419 118 118 VAL CG1 C 20.908 0.15 2 420 118 118 VAL N N 119.637 0.1 1 421 119 119 VAL H H 8.204 0.02 1 422 119 119 VAL CA C 59.980 0.15 1 423 119 119 VAL CB C 32.821 0.15 1 424 119 119 VAL N N 125.958 0.1 1 425 120 120 PRO C C 177.104 0.15 1 426 120 120 PRO CA C 62.959 0.15 1 427 120 120 PRO CB C 32.598 0.15 1 428 120 120 PRO CG C 27.321 0.15 1 429 121 121 GLU H H 8.646 0.02 1 430 121 121 GLU CA C 59.302 0.15 1 431 121 121 GLU CB C 29.938 0.15 1 432 121 121 GLU N N 121.358 0.1 1 433 123 123 LYS CA C 55.294 0.15 1 434 124 124 ARG H H 7.296 0.02 1 435 124 124 ARG CA C 56.120 0.15 1 436 124 124 ARG CB C 31.520 0.15 1 437 124 124 ARG N N 119.824 0.1 1 438 125 125 PHE H H 8.421 0.02 1 439 125 125 PHE CA C 56.302 0.15 1 440 125 125 PHE CB C 42.312 0.15 1 441 125 125 PHE N N 122.898 0.1 1 442 126 126 CYS H H 9.307 0.02 1 443 126 126 CYS CA C 59.889 0.15 1 444 126 126 CYS CB C 31.055 0.15 1 445 126 126 CYS N N 125.209 0.1 1 446 127 127 TRP H H 8.091 0.02 1 447 127 127 TRP HE1 H 10.429 0.02 1 448 127 127 TRP CA C 58.283 0.15 1 449 127 127 TRP CB C 28.423 0.15 1 450 127 127 TRP N N 130.574 0.1 1 451 127 127 TRP NE1 N 129.996 0.1 1 452 128 128 ASN H H 8.430 0.02 1 453 128 128 ASN HD21 H 7.828 0.02 2 454 128 128 ASN HD22 H 7.007 0.02 2 455 128 128 ASN CA C 55.637 0.15 1 456 128 128 ASN CB C 39.839 0.15 1 457 128 128 ASN N N 123.263 0.1 1 458 128 128 ASN ND2 N 117.156 0.1 1 459 129 129 CYS H H 8.754 0.02 1 460 129 129 CYS CA C 58.934 0.15 1 461 129 129 CYS CB C 32.474 0.15 1 462 129 129 CYS N N 118.608 0.1 1 463 130 130 GLY H H 7.728 0.02 1 464 130 130 GLY CA C 46.353 0.15 1 465 130 130 GLY N N 111.982 0.1 1 466 131 131 ARG H H 8.110 0.02 1 467 131 131 ARG CA C 55.685 0.15 1 468 131 131 ARG CB C 29.617 0.15 1 469 131 131 ARG N N 121.907 0.1 1 470 132 132 PRO CA C 63.644 0.15 1 471 133 133 VAL H H 7.391 0.02 1 472 133 133 VAL CA C 59.788 0.15 1 473 133 133 VAL CB C 34.953 0.15 1 474 133 133 VAL N N 115.754 0.1 1 475 134 134 GLY H H 8.237 0.02 1 476 134 134 GLY CA C 46.500 0.15 1 477 134 134 GLY N N 107.543 0.1 1 478 135 135 ARG H H 8.086 0.02 1 479 135 135 ARG CA C 53.963 0.15 1 480 135 135 ARG CB C 30.699 0.15 1 481 135 135 ARG N N 116.059 0.1 1 482 136 136 SER C C 176.090 0.15 1 483 136 136 SER CA C 58.753 0.15 1 484 136 136 SER CB C 63.758 0.15 1 485 137 137 ASP H H 8.490 0.02 1 486 137 137 ASP C C 176.207 0.15 1 487 137 137 ASP CA C 54.041 0.15 1 488 137 137 ASP CB C 41.368 0.15 1 489 137 137 ASP N N 122.435 0.1 1 490 138 138 SER H H 8.163 0.02 1 491 138 138 SER C C 175.745 0.15 1 492 138 138 SER CA C 59.680 0.15 1 493 138 138 SER N N 113.964 0.1 1 494 139 139 GLU H H 8.452 0.02 1 495 139 139 GLU C C 176.871 0.15 1 496 139 139 GLU CA C 57.272 0.15 1 497 139 139 GLU CB C 30.492 0.15 1 498 139 139 GLU N N 121.038 0.1 1 499 140 140 THR H H 8.141 0.02 1 500 140 140 THR C C 174.710 0.15 1 501 140 140 THR CA C 61.955 0.15 1 502 140 140 THR CB C 70.171 0.15 1 503 140 140 THR CG2 C 21.700 0.15 1 504 140 140 THR N N 114.224 0.1 1 505 141 141 LYS H H 8.341 0.02 1 506 141 141 LYS CA C 56.247 0.15 1 507 141 141 LYS CB C 32.548 0.15 1 508 141 141 LYS N N 123.611 0.1 1 509 142 142 GLY H H 8.388 0.02 1 510 142 142 GLY C C 175.930 0.15 1 511 142 142 GLY CA C 45.263 0.15 1 512 142 142 GLY N N 110.254 0.1 1 513 143 143 ALA H H 8.264 0.02 1 514 143 143 ALA CA C 52.510 0.15 1 515 143 143 ALA CB C 19.402 0.15 1 516 143 143 ALA N N 125.532 0.1 1 517 144 144 SER CA C 59.362 0.15 1 518 144 144 SER CB C 64.115 0.15 1 519 145 145 GLU H H 7.757 0.02 1 520 145 145 GLU CA C 55.134 0.15 1 521 145 145 GLU CB C 32.345 0.15 1 522 145 145 GLU N N 119.067 0.1 1 523 146 146 GLY H H 6.927 0.02 1 524 146 146 GLY C C 176.571 0.15 1 525 146 146 GLY CA C 45.469 0.15 1 526 146 146 GLY N N 108.096 0.1 1 527 147 147 TRP H H 8.363 0.02 1 528 147 147 TRP HE1 H 10.185 0.02 1 529 147 147 TRP CA C 56.751 0.15 1 530 147 147 TRP CB C 31.495 0.15 1 531 147 147 TRP N N 121.870 0.1 1 532 147 147 TRP NE1 N 129.424 0.1 1 533 148 148 CYS H H 9.387 0.02 1 534 148 148 CYS CA C 56.908 0.15 1 535 148 148 CYS CB C 31.969 0.15 1 536 148 148 CYS N N 128.204 0.1 1 537 149 149 PRO C C 176.251 0.15 1 538 149 149 PRO CA C 64.121 0.15 1 539 149 149 PRO CB C 32.031 0.15 1 540 149 149 PRO CG C 26.529 0.15 1 541 150 150 TYR H H 9.230 0.02 1 542 150 150 TYR C C 177.042 0.15 1 543 150 150 TYR CA C 60.017 0.15 1 544 150 150 TYR CB C 39.276 0.15 1 545 150 150 TYR N N 121.597 0.1 1 546 151 151 CYS H H 8.889 0.02 1 547 151 151 CYS CA C 58.231 0.15 1 548 151 151 CYS CB C 32.572 0.15 1 549 151 151 CYS N N 118.301 0.1 1 550 152 152 GLY H H 8.068 0.02 1 551 152 152 GLY C C 174.387 0.15 1 552 152 152 GLY CA C 46.281 0.15 1 553 152 152 GLY N N 113.419 0.1 1 554 153 153 SER H H 8.628 0.02 1 555 153 153 SER CA C 59.454 0.15 1 556 153 153 SER CB C 62.284 0.15 1 557 153 153 SER N N 120.049 0.1 1 558 154 154 PRO C C 176.718 0.15 1 559 154 154 PRO CA C 62.727 0.15 1 560 154 154 PRO CB C 32.118 0.15 1 561 155 155 TYR H H 8.184 0.02 1 562 155 155 TYR C C 176.959 0.15 1 563 155 155 TYR CA C 56.226 0.15 1 564 155 155 TYR CB C 40.789 0.15 1 565 155 155 TYR N N 118.505 0.1 1 566 156 156 SER H H 8.099 0.02 1 567 156 156 SER CA C 57.780 0.15 1 568 156 156 SER CB C 64.007 0.15 1 569 156 156 SER N N 113.706 0.1 1 570 157 157 PHE H H 8.806 0.02 1 571 157 157 PHE C C 174.870 0.15 1 572 157 157 PHE CA C 57.182 0.15 1 573 157 157 PHE CB C 39.708 0.15 1 574 157 157 PHE N N 124.766 0.1 1 575 158 158 LEU H H 7.960 0.02 1 576 158 158 LEU CA C 52.984 0.15 1 577 158 158 LEU CB C 41.710 0.15 1 578 158 158 LEU N N 123.191 0.1 1 579 159 159 PRO C C 176.533 0.15 1 580 159 159 PRO CA C 63.066 0.15 1 581 159 159 PRO CB C 32.103 0.15 1 582 159 159 PRO CD C 50.489 0.15 1 583 159 159 PRO CG C 27.261 0.15 1 584 160 160 GLN H H 8.408 0.02 1 585 160 160 GLN HE21 H 7.508 0.02 2 586 160 160 GLN HE22 H 6.833 0.02 2 587 160 160 GLN C C 175.665 0.15 1 588 160 160 GLN CA C 55.459 0.15 1 589 160 160 GLN CB C 29.694 0.15 1 590 160 160 GLN CG C 33.732 0.15 1 591 160 160 GLN N N 120.568 0.1 1 592 160 160 GLN NE2 N 112.671 0.1 1 593 161 161 LEU H H 8.253 0.02 1 594 161 161 LEU C C 176.691 0.15 1 595 161 161 LEU CA C 55.007 0.15 1 596 161 161 LEU CB C 42.671 0.15 1 597 161 161 LEU CD1 C 24.930 0.15 2 598 161 161 LEU CD2 C 23.316 0.15 2 599 161 161 LEU CG C 26.942 0.15 1 600 161 161 LEU N N 123.938 0.1 1 601 162 162 ASN H H 8.610 0.02 1 602 162 162 ASN HD21 H 7.682 0.02 2 603 162 162 ASN HD22 H 6.934 0.02 2 604 162 162 ASN CA C 51.224 0.15 1 605 162 162 ASN CB C 38.966 0.15 1 606 162 162 ASN N N 120.933 0.1 1 607 162 162 ASN ND2 N 113.919 0.1 1 608 163 163 PRO C C 177.569 0.15 1 609 163 163 PRO CA C 64.037 0.15 1 610 163 163 PRO CB C 31.856 0.15 1 611 163 163 PRO CD C 50.615 0.15 1 612 163 163 PRO CG C 27.191 0.15 1 613 164 164 GLY H H 8.389 0.02 1 614 164 164 GLY C C 174.004 0.15 1 615 164 164 GLY CA C 45.146 0.15 1 616 164 164 GLY N N 108.203 0.1 1 617 165 165 ASP H H 8.027 0.02 1 618 165 165 ASP C C 176.056 0.15 1 619 165 165 ASP CA C 54.558 0.15 1 620 165 165 ASP CB C 41.338 0.15 1 621 165 165 ASP N N 120.297 0.1 1 622 166 166 ILE H H 7.977 0.02 1 623 166 166 ILE C C 175.424 0.15 1 624 166 166 ILE CA C 61.329 0.15 1 625 166 166 ILE CB C 38.689 0.15 1 626 166 166 ILE CD1 C 12.695 0.15 1 627 166 166 ILE CG1 C 27.071 0.15 1 628 166 166 ILE CG2 C 17.438 0.15 1 629 166 166 ILE N N 120.766 0.1 1 630 167 167 VAL H H 7.685 0.02 1 631 167 167 VAL CA C 63.678 0.15 1 632 167 167 VAL CB C 33.351 0.15 1 633 167 167 VAL N N 128.484 0.1 1 stop_ save_