data_25566 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for oxidized peroxiredoxin Q from the plant pathogen Xanthomonas campestris ; _BMRB_accession_number 25566 _BMRB_flat_file_name bmr25566.str _Entry_type original _Submission_date 2015-04-08 _Accession_date 2015-04-08 _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 Buchko Garry W. . 2 Perkins Arden . . 3 Karplus P. Andrew . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 69 "13C chemical shifts" 189 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-25 update BMRB 'update entry citation' 2015-05-08 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25557 'Same protein but in the oxidized state.' stop_ _Original_release_date 2015-05-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26438558 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Buchko Garry W. . 2 Perkins Arden . . 3 Parsonage Derek . . 4 Poole Leslie B. . 5 Karplus P. Andrew . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 57 _Page_last 61 _Year 2016 _Details . loop_ _Keyword 'atypical 2-Cys' 'peroxide oxidoreduction' 'plant disease' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PrxQ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PrxQ $PrxQ 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_PrxQ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PrxQ _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 160 _Mol_residue_sequence ; MTDAVLELPAATFDLPLSLS GGTQTTLRAHAGHWLVIYFY PKDSTPGCTTEGLDFNALLP EFDKAGAKILGVSRDSVKSH DNFCAKQGFAFPLVSDGDEA LCRAFDVIKEKNMYGKQVLG IERSTFLLSPEGQVVQAWRK VKVAGHADAVLAALKAHAKQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 THR 3 3 ASP 4 4 ALA 5 5 VAL 6 6 LEU 7 7 GLU 8 8 LEU 9 9 PRO 10 10 ALA 11 11 ALA 12 12 THR 13 13 PHE 14 14 ASP 15 15 LEU 16 16 PRO 17 17 LEU 18 18 SER 19 19 LEU 20 20 SER 21 21 GLY 22 22 GLY 23 23 THR 24 24 GLN 25 25 THR 26 26 THR 27 27 LEU 28 28 ARG 29 29 ALA 30 30 HIS 31 31 ALA 32 32 GLY 33 33 HIS 34 34 TRP 35 35 LEU 36 36 VAL 37 37 ILE 38 38 TYR 39 39 PHE 40 40 TYR 41 41 PRO 42 42 LYS 43 43 ASP 44 44 SER 45 45 THR 46 46 PRO 47 47 GLY 48 48 CYS 49 49 THR 50 50 THR 51 51 GLU 52 52 GLY 53 53 LEU 54 54 ASP 55 55 PHE 56 56 ASN 57 57 ALA 58 58 LEU 59 59 LEU 60 60 PRO 61 61 GLU 62 62 PHE 63 63 ASP 64 64 LYS 65 65 ALA 66 66 GLY 67 67 ALA 68 68 LYS 69 69 ILE 70 70 LEU 71 71 GLY 72 72 VAL 73 73 SER 74 74 ARG 75 75 ASP 76 76 SER 77 77 VAL 78 78 LYS 79 79 SER 80 80 HIS 81 81 ASP 82 82 ASN 83 83 PHE 84 84 CYS 85 85 ALA 86 86 LYS 87 87 GLN 88 88 GLY 89 89 PHE 90 90 ALA 91 91 PHE 92 92 PRO 93 93 LEU 94 94 VAL 95 95 SER 96 96 ASP 97 97 GLY 98 98 ASP 99 99 GLU 100 100 ALA 101 101 LEU 102 102 CYS 103 103 ARG 104 104 ALA 105 105 PHE 106 106 ASP 107 107 VAL 108 108 ILE 109 109 LYS 110 110 GLU 111 111 LYS 112 112 ASN 113 113 MET 114 114 TYR 115 115 GLY 116 116 LYS 117 117 GLN 118 118 VAL 119 119 LEU 120 120 GLY 121 121 ILE 122 122 GLU 123 123 ARG 124 124 SER 125 125 THR 126 126 PHE 127 127 LEU 128 128 LEU 129 129 SER 130 130 PRO 131 131 GLU 132 132 GLY 133 133 GLN 134 134 VAL 135 135 VAL 136 136 GLN 137 137 ALA 138 138 TRP 139 139 ARG 140 140 LYS 141 141 VAL 142 142 LYS 143 143 VAL 144 144 ALA 145 145 GLY 146 146 HIS 147 147 ALA 148 148 ASP 149 149 ALA 150 150 VAL 151 151 LEU 152 152 ALA 153 153 ALA 154 154 LEU 155 155 LYS 156 156 ALA 157 157 HIS 158 158 ALA 159 159 LYS 160 160 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_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 $PrxQ g-proteobacteria 339 Bacteria . Xanthomonas campestris 17 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 $PrxQ 'recombinant technology' . Escherichia coli BL21(DE3) pTHC stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PrxQ 1.0 mM '[U-99% 13C; U-99% 15N]' 'sodium chloride' 100 mM 'natural abundance' TRIS 20 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 2007 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model VNMRS _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model VNMRS _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model VNMRS _Field_strength 500 _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_HNN_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNN _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' 0.120 0.005 M pH 7 0.2 pH pressure 1 . atm temperature 293 0.5 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 0.00 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '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 PrxQ _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET C C 177.4 0.2 1 2 2 2 THR H H 8.26 0.02 1 3 2 2 THR C C 174.6 0.2 1 4 2 2 THR CA C 62 0.2 1 5 2 2 THR CB C 69.7 0.2 1 6 2 2 THR N N 119.3 0.2 1 7 3 3 ASP H H 8.44 0.02 1 8 3 3 ASP C C 175.5 0.2 1 9 3 3 ASP CA C 54.5 0.2 1 10 3 3 ASP CB C 41.3 0.2 1 11 3 3 ASP N N 122.4 0.2 1 12 4 4 ALA H H 8.49 0.02 1 13 4 4 ALA CA C 52.7 0.2 1 14 4 4 ALA CB C 19.7 0.2 1 15 4 4 ALA C C 178.2 0.2 1 16 4 4 ALA N N 124 0.2 1 17 5 5 VAL H H 8.52 0.02 1 18 5 5 VAL C C 175.4 0.2 1 19 5 5 VAL CA C 62.4 0.2 1 20 5 5 VAL CB C 32.4 0.2 1 21 5 5 VAL N N 117.3 0.2 1 22 6 6 LEU H H 7.62 0.02 1 23 6 6 LEU C C 174 0.2 1 24 6 6 LEU CA C 55.2 0.2 1 25 6 6 LEU CB C 44.4 0.2 1 26 6 6 LEU N N 121.5 0.2 1 27 7 7 GLU H H 8.71 0.02 1 28 7 7 GLU C C 175 0.2 1 29 7 7 GLU CA C 55.3 0.2 1 30 7 7 GLU CB C 30.5 0.2 1 31 7 7 GLU N N 125.6 0.2 1 32 8 8 LEU H H 8.37 0.02 1 33 8 8 LEU CA C 52 0.2 1 34 8 8 LEU CB C 43.1 0.2 1 35 8 8 LEU N N 125.9 0.2 1 36 9 9 PRO C C 178.5 0.2 1 37 9 9 PRO CA C 62.5 0.2 1 38 9 9 PRO CB C 31.9 0.2 1 39 10 10 ALA H H 9.06 0.02 1 40 10 10 ALA C C 179.8 0.2 1 41 10 10 ALA CA C 56 0.2 1 42 10 10 ALA CB C 18.4 0.2 1 43 10 10 ALA N N 129.5 0.2 1 44 11 11 ALA H H 8.71 0.02 1 45 11 11 ALA C C 180 0.2 1 46 11 11 ALA CA C 54.6 0.2 1 47 11 11 ALA CB C 18.4 0.2 1 48 11 11 ALA N N 117.2 0.2 1 49 12 12 THR H H 8.04 0.02 1 50 12 12 THR C C 176 0.2 1 51 12 12 THR CA C 65.7 0.2 1 52 12 12 THR CB C 68.9 0.2 1 53 12 12 THR N N 113.6 0.2 1 54 13 13 PHE H H 7.67 0.02 1 55 13 13 PHE C C 173.5 0.2 1 56 13 13 PHE CA C 61.2 0.2 1 57 13 13 PHE CB C 38.2 0.2 1 58 13 13 PHE N N 115.8 0.2 1 59 14 14 ASP H H 7.32 0.02 1 60 14 14 ASP C C 175.2 0.2 1 61 14 14 ASP CA C 53.8 0.2 1 62 14 14 ASP CB C 43 0.2 1 63 14 14 ASP N N 113.5 0.2 1 64 15 15 LEU H H 6.98 0.02 1 65 15 15 LEU N N 123.7 0.2 1 66 19 19 LEU C C 179 0.2 1 67 20 20 SER H H 8.76 0.02 1 68 20 20 SER CB C 62.9 0.2 1 69 20 20 SER N N 117 0.2 1 70 21 21 GLY C C 175.4 0.2 1 71 22 22 GLY H H 8.21 0.02 1 72 22 22 GLY N N 107 0.2 1 73 25 25 THR C C 172 0.2 1 74 26 26 THR H H 8.43 0.02 1 75 26 26 THR CA C 59.7 0.2 1 76 26 26 THR CB C 73.6 0.2 1 77 26 26 THR N N 109.6 0.2 1 78 30 30 HIS C C 173.1 0.2 1 79 31 31 ALA H H 7.48 0.02 1 80 31 31 ALA C C 178.6 0.2 1 81 31 31 ALA CA C 54 0.2 1 82 31 31 ALA CB C 18.6 0.2 1 83 31 31 ALA N N 122.8 0.2 1 84 32 32 GLY H H 8.91 0.02 1 85 32 32 GLY N N 109.5 0.2 1 86 34 34 TRP C C 175.7 0.2 1 87 34 34 TRP CA C 59 0.2 1 88 35 35 LEU H H 9.29 0.02 1 89 35 35 LEU C C 174.3 0.2 1 90 35 35 LEU CA C 53.9 0.2 1 91 35 35 LEU CB C 46.6 0.2 1 92 35 35 LEU N N 124.3 0.2 1 93 36 36 VAL H H 8.96 0.02 1 94 36 36 VAL CA C 60.9 0.2 1 95 36 36 VAL CB C 32.7 0.2 1 96 36 36 VAL N N 127.6 0.2 1 97 57 57 ALA H H 8.18 0.02 1 98 57 57 ALA C C 179.1 0.2 1 99 57 57 ALA CA C 54.7 0.2 1 100 57 57 ALA CB C 18.5 0.2 1 101 57 57 ALA N N 120.3 0.2 1 102 58 58 LEU H H 7.31 0.02 1 103 58 58 LEU C C 177.5 0.2 1 104 58 58 LEU CA C 54.1 0.2 1 105 58 58 LEU CB C 44.4 0.2 1 106 58 58 LEU N N 115 0.2 1 107 59 59 LEU H H 7.68 0.02 1 108 59 59 LEU CA C 60.5 0.2 1 109 59 59 LEU CB C 39.9 0.2 1 110 59 59 LEU N N 125.1 0.2 1 111 60 60 PRO C C 180 0.2 1 112 60 60 PRO CA C 66.1 0.2 1 113 61 61 GLU H H 7.76 0.02 1 114 61 61 GLU C C 180.1 0.2 1 115 61 61 GLU CA C 58.5 0.2 1 116 61 61 GLU CB C 29.8 0.2 1 117 61 61 GLU N N 115.6 0.2 1 118 62 62 PHE H H 8.18 0.02 1 119 62 62 PHE CB C 38.4 0.2 1 120 62 62 PHE N N 120.8 0.2 1 121 63 63 ASP C C 180.7 0.2 1 122 64 64 LYS H H 7.84 0.02 1 123 64 64 LYS C C 177.6 0.2 1 124 64 64 LYS CA C 59.4 0.2 1 125 64 64 LYS CB C 32.7 0.2 1 126 64 64 LYS N N 120.4 0.2 1 127 65 65 ALA H H 7.36 0.02 1 128 65 65 ALA CA C 52.3 0.2 1 129 65 65 ALA CB C 18.5 0.2 1 130 65 65 ALA N N 119.2 0.2 1 131 66 66 GLY H H 7.95 0.02 1 132 66 66 GLY C C 174.4 0.2 1 133 66 66 GLY N N 105.5 0.2 1 134 67 67 ALA H H 8.36 0.02 1 135 67 67 ALA CA C 50.4 0.2 1 136 67 67 ALA CB C 24.4 0.2 1 137 67 67 ALA N N 121.5 0.2 1 138 68 68 LYS C C 173.8 0.2 1 139 69 69 ILE H H 8.1 0.02 1 140 69 69 ILE CA C 59.7 0.2 1 141 69 69 ILE CB C 39.9 0.2 1 142 69 69 ILE N N 119.8 0.2 1 143 90 90 ALA C C 175.5 0.2 1 144 90 90 ALA CA C 52.4 0.2 1 145 90 90 ALA CB C 19.2 0.2 1 146 91 91 PHE H H 6.81 0.02 1 147 91 91 PHE CA C 54 0.2 1 148 91 91 PHE CB C 38.7 0.2 1 149 91 91 PHE N N 116.2 0.2 1 150 105 105 PHE C C 173.9 0.2 1 151 105 105 PHE CA C 58.9 0.2 1 152 106 106 ASP H H 7.8 0.02 1 153 106 106 ASP CA C 54.8 0.2 1 154 106 106 ASP CB C 39.7 0.2 1 155 106 106 ASP N N 121.4 0.2 1 156 107 107 VAL C C 175 0.2 1 157 108 108 ILE H H 7.69 0.02 1 158 108 108 ILE C C 175.7 0.2 1 159 108 108 ILE N N 121 0.2 1 160 109 109 LYS H H 8.73 0.02 1 161 109 109 LYS C C 175.3 0.2 1 162 109 109 LYS CA C 53.4 0.2 1 163 109 109 LYS CB C 36.2 0.2 1 164 109 109 LYS N N 127.7 0.2 1 165 110 110 GLU H H 8.62 0.02 1 166 110 110 GLU C C 176 0.2 1 167 110 110 GLU CA C 56.7 0.2 1 168 110 110 GLU CB C 30.9 0.2 1 169 110 110 GLU N N 121.4 0.2 1 170 111 111 LYS H H 9 0.02 1 171 111 111 LYS C C 174.1 0.2 1 172 111 111 LYS CA C 55.2 0.2 1 173 111 111 LYS CB C 35.2 0.2 1 174 111 111 LYS N N 124.3 0.2 1 175 112 112 ASN H H 8.54 0.02 1 176 112 112 ASN C C 175.2 0.2 1 177 112 112 ASN CA C 53 0.2 1 178 112 112 ASN CB C 39.5 0.2 1 179 112 112 ASN N N 120.5 0.2 1 180 113 113 MET H H 8.96 0.02 1 181 113 113 MET CA C 54.8 0.2 1 182 113 113 MET CB C 33.9 0.2 1 183 113 113 MET N N 124.8 0.1 1 184 114 114 TYR H H 8.88 0.02 1 185 114 114 TYR C C 175.3 2 1 186 114 114 TYR CA C 58.2 0.2 1 187 114 114 TYR CB C 36 0.2 1 188 114 114 TYR N N 122.5 0.2 1 189 115 115 GLY H H 8.3 0.02 1 190 115 115 GLY C C 173.9 0.2 1 191 115 115 GLY N N 105.7 0.2 1 192 116 116 LYS H H 7.76 0.02 1 193 116 116 LYS C C 174.8 0.2 1 194 116 116 LYS CA C 54.8 0.2 1 195 116 116 LYS CB C 34.7 0.2 1 196 116 116 LYS N N 120.6 0.2 1 197 117 117 GLN H H 8.51 0.02 1 198 117 117 GLN C C 175.9 0.2 1 199 117 117 GLN CB C 29.6 0.2 1 200 117 117 GLN CA C 55.8 0.2 1 201 117 117 GLN N N 121.6 0.2 1 202 118 118 VAL H H 8.96 0.02 1 203 118 118 VAL C C 174.5 0.2 1 204 118 118 VAL CA C 60.5 0.2 1 205 118 118 VAL CB C 35.3 0.2 1 206 118 118 VAL N N 123.6 0.2 1 207 119 119 LEU H H 8.51 0.02 1 208 119 119 LEU C C 177.4 0.2 1 209 119 119 LEU CA C 54.3 0.2 1 210 119 119 LEU CB C 43 0.2 1 211 119 119 LEU N N 125.2 0.2 1 212 120 120 GLY H H 8.5 0.02 1 213 120 120 GLY N N 109 0.2 1 214 126 126 PHE C C 172.8 0.2 1 215 126 126 PHE CA C 57.1 0.2 1 216 127 127 LEU H H 8.98 0.02 1 217 127 127 LEU C C 174.1 0.2 1 218 127 127 LEU CA C 53.9 0.2 1 219 127 127 LEU N N 122.7 0.2 1 220 128 128 LEU H H 10.27 0.02 1 221 128 128 LEU C C 175.8 0.2 1 222 128 128 LEU CA C 54.7 0.2 1 223 128 128 LEU CB C 44.4 0.2 1 224 128 128 LEU N N 130.5 0.2 1 225 129 129 SER H H 9.29 0.02 1 226 129 129 SER CA C 55.8 0.2 1 227 129 129 SER CB C 63.2 0.2 1 228 129 129 SER N N 116.8 0.2 1 229 130 130 PRO C C 177 0.2 1 230 130 130 PRO CA C 64.2 0.2 1 231 130 130 PRO CB C 31.9 0.2 1 232 131 131 GLU H H 7.21 0.02 1 233 131 131 GLU C C 176.2 0.2 1 234 131 131 GLU CA C 56.3 0.2 1 235 131 131 GLU CB C 29.5 0.2 1 236 131 131 GLU N N 112.7 0.2 1 237 132 132 GLY H H 8.39 0.02 1 238 132 132 GLY C C 172.9 0.2 1 239 132 132 GLY N N 109.5 0.2 1 240 133 133 GLN H H 7.21 0.02 1 241 133 133 GLN C C 176 0.2 1 242 133 133 GLN CA C 54.6 0.2 1 243 133 133 GLN CB C 30.2 0.2 1 244 133 133 GLN N N 115.6 0.2 1 245 134 134 VAL H H 9.42 0.02 1 246 134 134 VAL CA C 63.2 0.2 1 247 134 134 VAL N N 124.7 0.2 1 248 135 135 VAL C C 175.6 0.2 1 249 135 135 VAL CA C 62.2 0.2 1 250 136 136 GLN H H 7.75 0.02 1 251 136 136 GLN C C 171.5 0.2 1 252 136 136 GLN CA C 57.3 0.2 1 253 136 136 GLN CB C 30 0.2 1 254 136 136 GLN N N 119.4 0.2 1 255 137 137 ALA H H 8.32 0.02 1 256 137 137 ALA CA C 51 0.2 1 257 137 137 ALA CB C 24.1 0.2 1 258 137 137 ALA N N 125.9 0.2 1 259 138 138 TRP HE1 H 10.35 0.2 1 260 138 138 TRP NE1 N 129.7 0.2 1 261 140 140 LYS C C 177.3 0.2 1 262 141 141 VAL H H 7.59 0.02 1 263 141 141 VAL CB C 31.9 0.2 1 264 141 141 VAL N N 118.4 0.2 1 265 146 146 HIS C C 175.8 0.2 1 266 146 146 HIS CA C 59.5 0.2 1 267 147 147 ALA H H 8.25 0.02 1 268 147 147 ALA C C 178.7 0.2 1 269 147 147 ALA CA C 56.1 0.2 1 270 147 147 ALA CB C 18.2 0.2 1 271 147 147 ALA N N 120.7 0.2 1 272 148 148 ASP H H 7.79 0.02 1 273 148 148 ASP C C 178.7 0.2 1 274 148 148 ASP CA C 57.2 0.2 1 275 148 148 ASP CB C 40.9 0.2 1 276 148 148 ASP N N 114.7 0.2 1 277 149 149 ALA H H 7.55 0.02 1 278 149 149 ALA CB C 17.6 0.2 1 279 149 149 ALA N N 124 0.2 1 280 150 150 VAL C C 177.5 0.2 1 281 150 150 VAL CA C 65.4 0.2 1 282 151 151 LEU H H 8.11 0.02 1 283 151 151 LEU C C 177.8 0.2 1 284 151 151 LEU CA C 57.9 0.2 1 285 151 151 LEU CB C 40.4 0.2 1 286 151 151 LEU N N 120.6 0.2 1 287 152 152 ALA H H 7.85 0.02 1 288 152 152 ALA C C 180.7 0.2 1 289 152 152 ALA CA C 55.3 0.2 1 290 152 152 ALA CB C 17.7 0.2 1 291 152 152 ALA N N 119.2 0.2 1 292 153 153 ALA H H 8 0.02 1 293 153 153 ALA C C 179.5 0.2 1 294 153 153 ALA CA C 55 0.2 1 295 153 153 ALA CB C 18.4 0.2 1 296 153 153 ALA N N 122 0.2 1 297 154 154 LEU H H 8.7 0.02 1 298 154 154 LEU CA C 58.7 0.2 1 299 154 154 LEU CB C 41.2 0.2 1 300 154 154 LEU N N 120.8 0.2 1 301 155 155 LYS H H 8.2 0.02 1 302 155 155 LYS C C 178.7 0.2 1 303 155 155 LYS CA C 60.1 0.2 1 304 155 155 LYS CB C 32.2 0.2 1 305 155 155 LYS N N 116.4 0.2 1 306 156 156 ALA H H 7.51 0.02 1 307 156 156 ALA CA C 54.8 0.2 1 308 156 156 ALA CB C 18.1 0.2 1 309 156 156 ALA N N 119.9 0.2 1 310 157 157 HIS H H 8.19 0.02 1 311 157 157 HIS C C 176.7 0.2 1 312 157 157 HIS CA C 59.5 0.2 1 313 157 157 HIS N N 117.2 0.2 1 314 158 158 ALA H H 8.26 0.02 1 315 158 158 ALA C C 177.3 0.2 1 316 158 158 ALA CA C 53.4 0.2 1 317 158 158 ALA CB C 18.2 0.2 1 318 158 158 ALA N N 120.3 0.2 1 319 159 159 LYS H H 7.55 0.02 1 320 159 159 LYS C C 175.6 0.2 1 321 159 159 LYS CA C 56.9 0.2 1 322 159 159 LYS CB C 31.9 0.2 1 323 159 159 LYS N N 118.4 0.2 1 324 160 160 GLN H H 8.05 0.02 1 325 160 160 GLN CB C 30.6 0.2 1 326 160 160 GLN CA C 57.4 0.2 1 327 160 160 GLN N N 126 0.2 1 stop_ save_