data_26030 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) ; _BMRB_accession_number 26030 _BMRB_flat_file_name bmr26030.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" 100 "13C chemical shifts" 224 "15N chemical shifts" 63 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) ; 26028 ; 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 ; 26029 ; Chemical shift assignment of the oxidized, unfolded 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) 74-147 rubredoxin domain reduced, metal bound form' _Enzyme_commission_number 2.7.11.1 loop_ _Mol_system_component_name _Mol_label 'Rubredoxin domain (RD)' $PknG_74-147 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_PknG_74-147 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PknG_74-147 _Molecular_mass 7949.01 _Mol_thiol_state 'all other bound' loop_ _Biological_function 'metal coordination' stop_ _Details 'PknG 74-147 contains the rubredoxin like metal binding site of mycobacterial protein kinase G' ############################## # Polymer residue sequence # ############################## _Residue_count 74 _Mol_residue_sequence ; LGGGLVEIPRAPDIDPLEAL MTNPVVPESKRFCWNCGRPV GRSDSETKGASEGWCPYCGS PYSFLPQLNPGDIV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 74 LEU 2 75 GLY 3 76 GLY 4 77 GLY 5 78 LEU 6 79 VAL 7 80 GLU 8 81 ILE 9 82 PRO 10 83 ARG 11 84 ALA 12 85 PRO 13 86 ASP 14 87 ILE 15 88 ASP 16 89 PRO 17 90 LEU 18 91 GLU 19 92 ALA 20 93 LEU 21 94 MET 22 95 THR 23 96 ASN 24 97 PRO 25 98 VAL 26 99 VAL 27 100 PRO 28 101 GLU 29 102 SER 30 103 LYS 31 104 ARG 32 105 PHE 33 106 CYS 34 107 TRP 35 108 ASN 36 109 CYS 37 110 GLY 38 111 ARG 39 112 PRO 40 113 VAL 41 114 GLY 42 115 ARG 43 116 SER 44 117 ASP 45 118 SER 46 119 GLU 47 120 THR 48 121 LYS 49 122 GLY 50 123 ALA 51 124 SER 52 125 GLU 53 126 GLY 54 127 TRP 55 128 CYS 56 129 PRO 57 130 TYR 58 131 CYS 59 132 GLY 60 133 SER 61 134 PRO 62 135 TYR 63 136 SER 64 137 PHE 65 138 LEU 66 139 PRO 67 140 GLN 68 141 LEU 69 142 ASN 70 143 PRO 71 144 GLY 72 145 ASP 73 146 ILE 74 147 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 $PknG_74-147 '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 $PknG_74-147 '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 74-147 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 $PknG_74-147 . mM 0.4 0.8 '[U-13C; U-15N]' TRIS-HCL 20 mM . . 'natural abundance' 'sodium chloride' 150 mM . . 'natural abundance' TCEP . mM 0.02 0.06 'natural abundance' 'zinc chloride' . mM 0.02 0.05 '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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _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_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 HNHA' '3D C(CO)NH' 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 '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 77 4 GLY H H 8.319 0.02 1 2 77 4 GLY C C 177.426 0.15 1 3 77 4 GLY CA C 45.173 0.15 1 4 77 4 GLY N N 108.687 0.1 1 5 78 5 LEU H H 8.090 0.02 1 6 78 5 LEU C C 177.423 0.15 1 7 78 5 LEU CA C 55.297 0.15 1 8 78 5 LEU CB C 42.461 0.15 1 9 78 5 LEU CD1 C 24.746 0.15 2 10 78 5 LEU CD2 C 23.478 0.15 2 11 78 5 LEU CG C 26.861 0.15 1 12 78 5 LEU N N 121.790 0.1 1 13 79 6 VAL H H 8.083 0.02 1 14 79 6 VAL HA H 4.088 0.02 1 15 79 6 VAL C C 175.922 0.15 1 16 79 6 VAL CA C 62.118 0.15 1 17 79 6 VAL CB C 32.903 0.15 1 18 79 6 VAL CG1 C 20.633 0.15 2 19 79 6 VAL N N 121.159 0.1 1 20 80 7 GLU H H 8.394 0.02 1 21 80 7 GLU HA H 4.299 0.02 1 22 80 7 GLU CA C 56.130 0.15 1 23 80 7 GLU CB C 30.631 0.15 1 24 80 7 GLU CG C 36.109 0.15 1 25 80 7 GLU N N 125.174 0.1 1 26 81 8 ILE H H 8.248 0.02 1 27 81 8 ILE HA H 4.422 0.02 1 28 81 8 ILE CA C 58.543 0.15 1 29 81 8 ILE CB C 38.662 0.15 1 30 81 8 ILE N N 124.576 0.1 1 31 82 9 PRO CA C 63.133 0.15 1 32 82 9 PRO CB C 31.977 0.15 1 33 82 9 PRO CD C 50.975 0.15 1 34 82 9 PRO CG C 27.201 0.15 1 35 83 10 ARG H H 8.344 0.02 1 36 83 10 ARG C C 175.901 0.15 1 37 83 10 ARG CA C 55.631 0.15 1 38 83 10 ARG CB C 31.297 0.15 1 39 83 10 ARG CD C 43.331 0.15 1 40 83 10 ARG CG C 26.918 0.15 1 41 83 10 ARG N N 121.890 0.1 1 42 84 11 ALA H H 8.409 0.02 1 43 84 11 ALA HA H 4.539 0.02 1 44 84 11 ALA CA C 50.548 0.15 1 45 84 11 ALA CB C 18.176 0.15 1 46 84 11 ALA N N 127.542 0.1 1 47 85 12 PRO C C 176.741 0.15 1 48 85 12 PRO CA C 63.132 0.15 1 49 85 12 PRO CB C 32.164 0.15 1 50 85 12 PRO CD C 50.711 0.15 1 51 85 12 PRO CG C 27.136 0.15 1 52 86 13 ASP H H 8.355 0.02 1 53 86 13 ASP C C 176.044 0.15 1 54 86 13 ASP CA C 54.418 0.15 1 55 86 13 ASP CB C 41.111 0.15 1 56 86 13 ASP N N 120.018 0.1 1 57 87 14 ILE H H 7.911 0.02 1 58 87 14 ILE HA H 4.128 0.02 1 59 87 14 ILE C C 175.704 0.15 1 60 87 14 ILE CA C 60.531 0.15 1 61 87 14 ILE CB C 39.292 0.15 1 62 87 14 ILE CD1 C 12.712 0.15 1 63 87 14 ILE CG1 C 26.892 0.15 1 64 87 14 ILE CG2 C 17.215 0.15 1 65 87 14 ILE N N 120.158 0.1 1 66 88 15 ASP H H 8.523 0.02 1 67 88 15 ASP HA H 4.844 0.02 1 68 88 15 ASP CA C 52.111 0.15 1 69 88 15 ASP CB C 41.654 0.15 1 70 88 15 ASP N N 126.868 0.1 1 71 89 16 PRO C C 177.871 0.15 1 72 89 16 PRO CA C 63.971 0.15 1 73 89 16 PRO CB C 32.257 0.15 1 74 89 16 PRO CD C 50.772 0.15 1 75 89 16 PRO CG C 27.140 0.15 1 76 90 17 LEU H H 8.330 0.02 1 77 90 17 LEU HA H 4.212 0.02 1 78 90 17 LEU C C 178.638 0.15 1 79 90 17 LEU CA C 56.004 0.15 1 80 90 17 LEU CB C 41.571 0.15 1 81 90 17 LEU CD1 C 24.761 0.15 2 82 90 17 LEU CD2 C 23.178 0.15 2 83 90 17 LEU CG C 26.985 0.15 1 84 90 17 LEU N N 119.657 0.1 1 85 91 18 GLU H H 7.957 0.02 1 86 91 18 GLU C C 177.397 0.15 1 87 91 18 GLU CA C 57.534 0.15 1 88 91 18 GLU CB C 30.042 0.15 1 89 91 18 GLU CG C 36.203 0.15 1 90 91 18 GLU N N 120.436 0.1 1 91 92 19 ALA H H 8.044 0.02 1 92 92 19 ALA HA H 4.207 0.02 1 93 92 19 ALA C C 178.179 0.15 1 94 92 19 ALA CA C 53.080 0.15 1 95 92 19 ALA CB C 18.942 0.15 1 96 92 19 ALA N N 123.183 0.1 1 97 93 20 LEU H H 7.864 0.02 1 98 93 20 LEU HA H 4.283 0.02 1 99 93 20 LEU C C 177.897 0.15 1 100 93 20 LEU CA C 55.559 0.15 1 101 93 20 LEU CB C 42.319 0.15 1 102 93 20 LEU CD1 C 24.874 0.15 2 103 93 20 LEU CD2 C 23.453 0.15 2 104 93 20 LEU CG C 26.963 0.15 1 105 93 20 LEU N N 119.470 0.1 1 106 94 21 MET H H 8.101 0.02 1 107 94 21 MET C C 176.590 0.15 1 108 94 21 MET CA C 55.641 0.15 1 109 94 21 MET CB C 32.644 0.15 1 110 94 21 MET CG C 32.023 0.15 1 111 94 21 MET N N 119.637 0.1 1 112 95 22 THR H H 7.956 0.02 1 113 95 22 THR CA C 61.954 0.15 1 114 95 22 THR CB C 69.860 0.15 1 115 95 22 THR CG2 C 21.548 0.15 1 116 95 22 THR N N 113.982 0.1 1 117 96 23 ASN H H 8.315 0.02 1 118 96 23 ASN HD21 H 7.595 0.02 2 119 96 23 ASN CA C 51.441 0.15 1 120 96 23 ASN CB C 39.038 0.15 1 121 96 23 ASN N N 121.832 0.1 1 122 96 23 ASN ND2 N 112.940 0.1 1 123 97 24 PRO C C 176.826 0.15 1 124 97 24 PRO CA C 63.240 0.15 1 125 97 24 PRO CB C 32.026 0.15 1 126 97 24 PRO CD C 50.514 0.15 1 127 97 24 PRO CG C 27.026 0.15 1 128 98 25 VAL H H 8.102 0.02 1 129 98 25 VAL C C 176.253 0.15 1 130 98 25 VAL CA C 62.172 0.15 1 131 98 25 VAL CB C 32.644 0.15 1 132 98 25 VAL CG1 C 20.834 0.15 2 133 98 25 VAL N N 119.777 0.1 1 134 99 26 VAL H H 8.227 0.02 1 135 99 26 VAL HA H 4.358 0.02 1 136 99 26 VAL CA C 59.934 0.15 1 137 99 26 VAL CB C 32.797 0.15 1 138 99 26 VAL N N 126.021 0.1 1 139 100 27 PRO C C 177.230 0.15 1 140 100 27 PRO CA C 62.991 0.15 1 141 100 27 PRO CB C 32.285 0.15 1 142 100 27 PRO CD C 51.073 0.15 1 143 100 27 PRO CG C 27.185 0.15 1 144 101 28 GLU H H 8.639 0.02 1 145 101 28 GLU HA H 3.648 0.02 1 146 101 28 GLU CA C 58.937 0.15 1 147 101 28 GLU CB C 29.917 0.15 1 148 101 28 GLU N N 121.313 0.1 1 149 103 30 LYS CA C 55.370 0.15 1 150 103 30 LYS CB C 33.043 0.15 1 151 104 31 ARG H H 7.317 0.02 1 152 104 31 ARG CA C 55.970 0.15 1 153 104 31 ARG CB C 31.471 0.15 1 154 104 31 ARG CD C 43.691 0.15 1 155 104 31 ARG CG C 26.104 0.15 1 156 104 31 ARG N N 119.818 0.1 1 157 105 32 PHE H H 8.359 0.02 1 158 105 32 PHE C C 174.664 0.15 1 159 105 32 PHE CA C 56.231 0.15 1 160 105 32 PHE CB C 42.369 0.15 1 161 105 32 PHE N N 122.759 0.1 1 162 106 33 CYS H H 9.291 0.02 1 163 106 33 CYS CA C 59.936 0.15 1 164 106 33 CYS CB C 31.036 0.15 1 165 106 33 CYS N N 125.119 0.1 1 166 107 34 TRP H H 8.098 0.02 1 167 107 34 TRP HE1 H 10.414 0.02 1 168 107 34 TRP CA C 58.266 0.15 1 169 107 34 TRP CB C 28.350 0.15 1 170 107 34 TRP N N 130.479 0.1 1 171 107 34 TRP NE1 N 129.951 0.1 1 172 108 35 ASN H H 8.429 0.02 1 173 108 35 ASN HA H 4.439 0.02 1 174 108 35 ASN HD21 H 7.834 0.02 2 175 108 35 ASN HD22 H 6.994 0.02 2 176 108 35 ASN C C 175.722 0.15 1 177 108 35 ASN CA C 55.592 0.15 1 178 108 35 ASN CB C 39.832 0.15 1 179 108 35 ASN N N 123.221 0.1 1 180 108 35 ASN ND2 N 117.148 0.1 1 181 109 36 CYS H H 8.753 0.02 1 182 109 36 CYS HA H 4.874 0.02 1 183 109 36 CYS CA C 58.958 0.15 1 184 109 36 CYS CB C 32.472 0.15 1 185 109 36 CYS N N 118.584 0.1 1 186 110 37 GLY H H 7.726 0.02 1 187 110 37 GLY C C 174.159 0.15 1 188 110 37 GLY CA C 46.323 0.15 1 189 110 37 GLY N N 112.041 0.1 1 190 111 38 ARG H H 8.108 0.02 1 191 111 38 ARG CA C 55.564 0.15 1 192 111 38 ARG CB C 29.608 0.15 1 193 111 38 ARG N N 121.790 0.1 1 194 112 39 PRO CA C 63.555 0.15 1 195 112 39 PRO CB C 31.785 0.15 1 196 113 40 VAL H H 7.415 0.02 1 197 113 40 VAL CA C 60.056 0.15 1 198 113 40 VAL CB C 35.105 0.15 1 199 113 40 VAL N N 115.819 0.1 1 200 114 41 GLY H H 8.235 0.02 1 201 114 41 GLY CA C 46.294 0.15 1 202 114 41 GLY N N 107.627 0.1 1 203 115 42 ARG H H 8.102 0.02 1 204 115 42 ARG HA H 4.088 0.02 1 205 115 42 ARG CA C 54.259 0.15 1 206 115 42 ARG CB C 30.646 0.15 1 207 115 42 ARG N N 116.219 0.1 1 208 116 43 SER C C 176.348 0.15 1 209 116 43 SER CA C 58.781 0.15 1 210 116 43 SER CB C 63.914 0.15 1 211 117 44 ASP H H 8.486 0.02 1 212 117 44 ASP HA H 4.212 0.02 1 213 117 44 ASP CA C 54.188 0.15 1 214 117 44 ASP CB C 41.222 0.15 1 215 117 44 ASP N N 122.301 0.1 1 216 118 45 SER H H 8.162 0.02 1 217 118 45 SER CA C 59.519 0.15 1 218 118 45 SER CB C 63.685 0.15 1 219 118 45 SER N N 114.011 0.1 1 220 119 46 GLU H H 8.463 0.02 1 221 119 46 GLU HA H 4.240 0.02 1 222 119 46 GLU C C 177.049 0.15 1 223 119 46 GLU CA C 57.307 0.15 1 224 119 46 GLU CB C 30.675 0.15 1 225 119 46 GLU CG C 36.396 0.15 1 226 119 46 GLU N N 120.916 0.1 1 227 120 47 THR H H 8.132 0.02 1 228 120 47 THR C C 174.652 0.15 1 229 120 47 THR CA C 62.003 0.15 1 230 120 47 THR CB C 70.206 0.15 1 231 120 47 THR CG2 C 21.631 0.15 1 232 120 47 THR N N 114.155 0.1 1 233 121 48 LYS H H 8.336 0.02 1 234 121 48 LYS HA H 4.252 0.02 1 235 121 48 LYS C C 177.247 0.15 1 236 121 48 LYS CA C 56.377 0.15 1 237 121 48 LYS CB C 32.516 0.15 1 238 121 48 LYS CD C 28.871 0.15 1 239 121 48 LYS CG C 24.549 0.15 1 240 121 48 LYS N N 123.534 0.1 1 241 122 49 GLY H H 8.394 0.02 1 242 122 49 GLY HA2 H 4.293 0.02 2 243 122 49 GLY HA3 H 4.293 0.02 2 244 122 49 GLY C C 176.012 0.15 1 245 122 49 GLY CA C 45.234 0.15 1 246 122 49 GLY N N 110.294 0.1 1 247 123 50 ALA H H 8.242 0.02 1 248 123 50 ALA CA C 52.440 0.15 1 249 123 50 ALA CB C 19.692 0.15 1 250 123 50 ALA N N 125.358 0.1 1 251 124 51 SER CA C 59.412 0.15 1 252 124 51 SER CB C 64.116 0.15 1 253 125 52 GLU H H 7.768 0.02 1 254 125 52 GLU HA H 4.488 0.02 1 255 125 52 GLU CA C 55.254 0.15 1 256 125 52 GLU CB C 32.312 0.15 1 257 125 52 GLU N N 119.154 0.1 1 258 126 53 GLY H H 6.946 0.02 1 259 126 53 GLY C C 176.738 0.15 1 260 126 53 GLY CA C 45.414 0.15 1 261 126 53 GLY N N 108.047 0.1 1 262 127 54 TRP H H 8.314 0.02 1 263 127 54 TRP HE1 H 10.179 0.02 1 264 127 54 TRP C C 175.208 0.15 1 265 127 54 TRP CA C 56.644 0.15 1 266 127 54 TRP CB C 31.859 0.15 1 267 127 54 TRP N N 121.882 0.1 1 268 127 54 TRP NE1 N 129.354 0.1 1 269 128 55 CYS H H 9.359 0.02 1 270 128 55 CYS CA C 56.866 0.15 1 271 128 55 CYS CB C 32.068 0.15 1 272 128 55 CYS N N 128.017 0.1 1 273 129 56 PRO C C 176.446 0.15 1 274 129 56 PRO CA C 64.077 0.15 1 275 129 56 PRO CB C 32.193 0.15 1 276 129 56 PRO CD C 51.494 0.15 1 277 129 56 PRO CG C 26.369 0.15 1 278 130 57 TYR H H 9.228 0.02 1 279 130 57 TYR HA H 4.533 0.02 1 280 130 57 TYR C C 177.242 0.15 1 281 130 57 TYR CA C 59.961 0.15 1 282 130 57 TYR CB C 39.246 0.15 1 283 130 57 TYR N N 121.561 0.1 1 284 131 58 CYS H H 8.882 0.02 1 285 131 58 CYS HA H 5.010 0.02 1 286 131 58 CYS C C 175.084 0.15 1 287 131 58 CYS CA C 58.229 0.15 1 288 131 58 CYS CB C 32.511 0.15 1 289 131 58 CYS N N 118.306 0.1 1 290 132 59 GLY H H 8.058 0.02 1 291 132 59 GLY C C 174.545 0.15 1 292 132 59 GLY CA C 46.258 0.15 1 293 132 59 GLY N N 113.491 0.1 1 294 133 60 SER H H 8.619 0.02 1 295 133 60 SER HA H 4.787 0.02 1 296 133 60 SER CA C 59.414 0.15 1 297 133 60 SER CB C 62.278 0.15 1 298 133 60 SER N N 120.025 0.1 1 299 134 61 PRO C C 176.870 0.15 1 300 134 61 PRO CA C 62.755 0.15 1 301 134 61 PRO CB C 31.856 0.15 1 302 134 61 PRO CD C 50.913 0.15 1 303 134 61 PRO CG C 27.161 0.15 1 304 135 62 TYR H H 8.153 0.02 1 305 135 62 TYR HA H 4.903 0.02 1 306 135 62 TYR C C 177.175 0.15 1 307 135 62 TYR CA C 56.411 0.15 1 308 135 62 TYR CB C 40.575 0.15 1 309 135 62 TYR N N 118.529 0.1 1 310 136 63 SER H H 8.095 0.02 1 311 136 63 SER CA C 57.771 0.15 1 312 136 63 SER CB C 63.983 0.15 1 313 136 63 SER N N 113.694 0.1 1 314 137 64 PHE H H 8.782 0.02 1 315 137 64 PHE HA H 4.889 0.02 1 316 137 64 PHE C C 175.056 0.15 1 317 137 64 PHE CA C 57.113 0.15 1 318 137 64 PHE CB C 39.676 0.15 1 319 137 64 PHE N N 124.681 0.1 1 320 138 65 LEU H H 7.950 0.02 1 321 138 65 LEU HA H 4.580 0.02 1 322 138 65 LEU CA C 52.967 0.15 1 323 138 65 LEU CB C 41.704 0.15 1 324 138 65 LEU N N 123.249 0.1 1 325 139 66 PRO C C 176.692 0.15 1 326 139 66 PRO CA C 63.092 0.15 1 327 139 66 PRO CB C 32.072 0.15 1 328 139 66 PRO CD C 50.450 0.15 1 329 139 66 PRO CG C 27.176 0.15 1 330 140 67 GLN H H 8.409 0.02 1 331 140 67 GLN HA H 4.282 0.02 1 332 140 67 GLN HE21 H 7.506 0.02 2 333 140 67 GLN HE22 H 6.831 0.02 2 334 140 67 GLN C C 175.749 0.15 1 335 140 67 GLN CA C 55.258 0.15 1 336 140 67 GLN CB C 29.675 0.15 1 337 140 67 GLN CG C 33.728 0.15 1 338 140 67 GLN N N 120.515 0.1 1 339 140 67 GLN NE2 N 112.686 0.1 1 340 141 68 LEU H H 8.255 0.02 1 341 141 68 LEU HA H 4.312 0.02 1 342 141 68 LEU C C 176.789 0.15 1 343 141 68 LEU CA C 54.993 0.15 1 344 141 68 LEU CB C 42.668 0.15 1 345 141 68 LEU CD1 C 24.777 0.15 2 346 141 68 LEU CD2 C 23.456 0.15 2 347 141 68 LEU CG C 26.897 0.15 1 348 141 68 LEU N N 123.912 0.1 1 349 142 69 ASN H H 8.608 0.02 1 350 142 69 ASN HA H 4.979 0.02 1 351 142 69 ASN HD21 H 7.683 0.02 2 352 142 69 ASN HD22 H 6.912 0.02 2 353 142 69 ASN CA C 51.180 0.15 1 354 142 69 ASN CB C 38.939 0.15 1 355 142 69 ASN N N 120.867 0.1 1 356 142 69 ASN ND2 N 113.529 0.1 1 357 143 70 PRO C C 177.707 0.15 1 358 143 70 PRO CA C 64.016 0.15 1 359 143 70 PRO CB C 32.067 0.15 1 360 143 70 PRO CD C 50.689 0.15 1 361 143 70 PRO CG C 27.170 0.15 1 362 144 71 GLY H H 8.389 0.02 1 363 144 71 GLY HA2 H 3.880 0.02 2 364 144 71 GLY HA3 H 3.880 0.02 2 365 144 71 GLY C C 174.153 0.15 1 366 144 71 GLY CA C 45.235 0.15 1 367 144 71 GLY N N 108.179 0.1 1 368 145 72 ASP H H 8.030 0.02 1 369 145 72 ASP HA H 4.621 0.02 1 370 145 72 ASP C C 176.204 0.15 1 371 145 72 ASP CA C 54.533 0.15 1 372 145 72 ASP CB C 41.323 0.15 1 373 145 72 ASP N N 120.240 0.1 1 374 146 73 ILE H H 7.983 0.02 1 375 146 73 ILE HA H 4.172 0.02 1 376 146 73 ILE C C 175.534 0.15 1 377 146 73 ILE CA C 61.349 0.15 1 378 146 73 ILE CB C 38.683 0.15 1 379 146 73 ILE CD1 C 12.688 0.15 1 380 146 73 ILE CG1 C 26.882 0.15 1 381 146 73 ILE CG2 C 17.426 0.15 1 382 146 73 ILE N N 120.795 0.1 1 383 147 74 VAL H H 7.689 0.02 1 384 147 74 VAL HA H 4.031 0.02 1 385 147 74 VAL CA C 63.656 0.15 1 386 147 74 VAL CB C 33.332 0.15 1 387 147 74 VAL N N 128.487 0.1 1 stop_ save_