data_25557 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for reduced peroxiredoxin Q from the plant pathogen Xanthomonas campestris. ; _BMRB_accession_number 25557 _BMRB_flat_file_name bmr25557.str _Entry_type original _Submission_date 2015-03-28 _Accession_date 2015-04-02 _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" 151 "13C chemical shifts" 504 "15N chemical shifts" 151 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 25566 'Same protein but in the reduced state.' stop_ _Original_release_date 2015-05-11 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 dynamics peroxidases 'plant pathogens' 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 . loop_ _Biological_function peroxidase stop_ _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 free' loop_ _Biological_function peroxidase stop_ _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 'Xanthomonas campestris' 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 . 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' DTT 1 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version 2007 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_HNCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _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_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_ save_2D_1H-13C_HSQC_aliphatic_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _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' 120 50 mM 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 HNCACO' '3D HNCACB' '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 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 2 2 THR H H 8.27 0.02 1 2 2 2 THR CA C 61.9 0.2 1 3 2 2 THR CB C 69.8 0.2 1 4 2 2 THR CG2 C 21.4 0.2 1 5 2 2 THR N N 119.0 0.2 1 6 3 3 ASP H H 8.44 0.02 1 7 3 3 ASP C C 175.3 0.2 1 8 3 3 ASP CA C 54.2 0.2 1 9 3 3 ASP CB C 41.3 0.2 1 10 3 3 ASP N N 122.3 0.2 1 11 4 4 ALA H H 8.48 0.02 1 12 4 4 ALA C C 178.4 0.2 1 13 4 4 ALA CA C 52.2 0.2 1 14 4 4 ALA CB C 19.9 0.2 1 15 4 4 ALA N N 123.8 0.2 1 16 5 5 VAL H H 8.52 0.02 1 17 5 5 VAL C C 175.5 0.2 1 18 5 5 VAL CA C 62.4 0.2 1 19 5 5 VAL CB C 32.3 0.2 1 20 5 5 VAL CG1 C 21.5 0.2 2 21 5 5 VAL CG2 C 19.9 0.2 2 22 5 5 VAL N N 116.9 0.2 1 23 6 6 LEU H H 7.61 0.02 1 24 6 6 LEU C C 174.1 0.2 1 25 6 6 LEU CA C 54.9 0.2 1 26 6 6 LEU CB C 44.3 0.2 1 27 6 6 LEU CD1 C 24.0 0.2 2 28 6 6 LEU CD2 C 24.0 0.2 2 29 6 6 LEU CG C 27.1 0.2 1 30 6 6 LEU N N 121.5 0.2 1 31 7 7 GLU H H 8.72 0.02 1 32 7 7 GLU C C 175.1 0.2 1 33 7 7 GLU CA C 55.0 0.2 1 34 7 7 GLU CB C 30.3 0.2 1 35 7 7 GLU CG C 35.9 0.2 1 36 7 7 GLU N N 125.6 0.2 1 37 8 8 LEU H H 8.36 0.02 1 38 8 8 LEU C C 174.9 0.2 1 39 8 8 LEU CA C 51.8 0.2 1 40 8 8 LEU CB C 43.0 0.2 1 41 8 8 LEU N N 126.1 0.2 1 42 9 9 PRO C C 178.7 0.2 1 43 9 9 PRO CA C 62.7 0.2 1 44 9 9 PRO CB C 31.9 0.2 1 45 9 9 PRO CG C 27.7 0.2 1 46 10 10 ALA H H 9.08 0.02 1 47 10 10 ALA C C 180.0 0.2 1 48 10 10 ALA CA C 55.8 0.2 1 49 10 10 ALA CB C 18.3 0.2 1 50 10 10 ALA N N 129.6 0.2 1 51 11 11 ALA H H 8.74 0.02 1 52 11 11 ALA C C 180.1 0.2 1 53 11 11 ALA CA C 54.3 0.2 1 54 11 11 ALA CB C 18.3 0.2 1 55 11 11 ALA N N 117.3 0.2 1 56 12 12 THR H H 8.07 0.02 1 57 12 12 THR C C 176.1 0.2 1 58 12 12 THR CA C 65.8 0.02 1 59 12 12 THR CB C 68.8 0.02 1 60 12 12 THR CG2 C 21.8 0.02 1 61 12 12 THR N N 113.5 0.2 1 62 13 13 PHE H H 7.66 0.02 1 63 13 13 PHE C C 173.5 0.2 1 64 13 13 PHE CA C 61.2 0.02 1 65 13 13 PHE CB C 38.3 0.02 1 66 13 13 PHE N N 115.7 0.2 1 67 14 14 ASP H H 7.31 0.02 1 68 14 14 ASP C C 175.4 0.2 1 69 14 14 ASP CA C 53.4 0.2 1 70 14 14 ASP CB C 43.0 0.2 1 71 14 14 ASP N N 113.3 0.2 1 72 15 15 LEU H H 6.99 0.02 1 73 15 15 LEU C C 174.8 0.2 1 74 15 15 LEU CA C 53.4 0.2 1 75 15 15 LEU CB C 42.0 0.2 1 76 15 15 LEU N N 123.6 0.2 1 77 16 16 PRO C C 176.7 0.2 1 78 16 16 PRO CA C 62.6 0.2 1 79 16 16 PRO CB C 31.1 0.2 1 80 16 16 PRO CG C 27.7 0.2 1 81 17 17 LEU H H 9.31 0.02 1 82 17 17 LEU C C 176.4 0.2 1 83 17 17 LEU CA C 52.7 0.2 1 84 17 17 LEU CB C 41.6 0.2 1 85 17 17 LEU N N 127.1 0.2 1 86 18 18 SER H H 9.21 0.02 1 87 18 18 SER C C 173.0 0.2 1 88 18 18 SER CA C 59.2 0.2 1 89 18 18 SER CB C 63.3 0.2 1 90 18 18 SER N N 120.6 0.2 1 91 19 19 LEU H H 8.55 0.02 1 92 19 19 LEU C C 179.3 0.2 1 93 19 19 LEU CA C 53.4 0.2 1 94 19 19 LEU CB C 44.6 0.2 1 95 19 19 LEU N N 125.3 0.2 1 96 20 20 SER H H 8.83 0.02 1 97 20 20 SER C C 174.4 0.2 1 98 20 20 SER CA C 59.4 0.2 1 99 20 20 SER CB C 62.9 0.2 1 100 20 20 SER N N 115.2 0.2 1 101 21 21 GLY H H 10.55 0.02 1 102 21 21 GLY C C 176.7 0.2 1 103 21 21 GLY CA C 45.3 0.2 1 104 21 21 GLY N N 114.3 0.2 1 105 22 22 GLY H H 8.10 0.02 1 106 22 22 GLY C C 175.0 0.2 1 107 22 22 GLY CA C 46.8 0.2 1 108 22 22 GLY N N 105.7 0.2 1 109 23 23 THR H H 7.02 0.02 1 110 23 23 THR C C 172.8 0.2 1 111 23 23 THR CA C 60.4 0.2 1 112 23 23 THR CB C 70.7 0.2 1 113 23 23 THR N N 110.3 0.2 1 114 24 24 GLN H H 8.47 0.02 1 115 24 24 GLN C C 175.7 0.2 1 116 24 24 GLN CA C 54.2 0.2 1 117 24 24 GLN CB C 33.6 0.2 1 118 24 24 GLN CG C 34.4 0.2 1 119 24 24 GLN N N 117.6 0.2 1 120 25 25 THR H H 8.71 0.02 1 121 25 25 THR C C 172.2 0.2 1 122 25 25 THR CA C 59.9 0.2 1 123 25 25 THR CB C 69.5 0.2 1 124 25 25 THR N N 116.8 0.2 1 125 26 26 THR H H 8.54 0.02 1 126 26 26 THR C C 175.5 0.2 1 127 26 26 THR CA C 59.7 0.2 1 128 26 26 THR CB C 73.4 0.2 1 129 26 26 THR N N 109.6 0.2 1 130 27 27 LEU H H 10.31 0.02 1 131 27 27 LEU C C 181.4 0.2 1 132 27 27 LEU CA C 58.5 0.2 1 133 27 27 LEU CB C 41.8 0.2 1 134 27 27 LEU N N 120.2 0.2 1 135 28 28 ARG H H 9.03 0.02 1 136 28 28 ARG C C 178.7 0.2 1 137 28 28 ARG CA C 59.1 0.2 1 138 28 28 ARG CB C 29.5 0.2 1 139 28 28 ARG CD C 42.4 0.2 1 140 28 28 ARG CG C 27.1 0.2 1 141 28 28 ARG N N 121.6 0.2 1 142 29 29 ALA H H 7.94 0.02 1 143 29 29 ALA C C 178.6 0.2 1 144 29 29 ALA CA C 53.9 0.2 1 145 29 29 ALA CB C 17.9 0.2 1 146 29 29 ALA N N 120.6 0.2 1 147 30 30 HIS H H 7.76 0.02 1 148 30 30 HIS C C 173.1 0.2 1 149 30 30 HIS CA C 57.1 0.2 1 150 30 30 HIS CB C 30.7 0.2 1 151 30 30 HIS N N 116.4 0.2 1 152 31 31 ALA H H 7.43 0.02 1 153 31 31 ALA C C 178.8 0.2 1 154 31 31 ALA CA C 53.7 0.2 1 155 31 31 ALA CB C 18.4 0.2 1 156 31 31 ALA N N 122.7 0.2 1 157 32 32 GLY H H 8.97 0.02 1 158 32 32 GLY C C 173.9 0.2 1 159 32 32 GLY CA C 44.9 0.2 1 160 32 32 GLY N N 109.5 0.2 1 161 33 33 HIS H H 7.97 0.02 1 162 33 33 HIS C C 173.1 0.2 1 163 33 33 HIS CA C 54.7 0.2 1 164 33 33 HIS CB C 30.8 0.2 1 165 33 33 HIS N N 116.7 0.2 1 166 34 34 TRP H H 8.18 0.02 1 167 34 34 TRP HE1 H 10.65 0.02 1 168 34 34 TRP C C 176.0 0.2 1 169 34 34 TRP CA C 56.7 0.2 1 170 34 34 TRP CB C 30.5 0.2 1 171 34 34 TRP N N 119.6 0.2 1 172 34 34 TRP NE1 N 130.4 0.2 1 173 35 35 LEU H H 9.32 0.02 1 174 35 35 LEU C C 174.6 0.2 1 175 35 35 LEU CA C 53.7 0.2 1 176 35 35 LEU CB C 46.8 0.2 1 177 35 35 LEU N N 123.9 0.2 1 178 36 36 VAL H H 8.90 0.02 1 179 36 36 VAL C C 173.9 0.2 1 180 36 36 VAL CA C 61.1 0.2 1 181 36 36 VAL CB C 32.5 0.2 1 182 36 36 VAL CG1 C 21.0 0.2 2 183 36 36 VAL CG2 C 21.0 0.2 2 184 36 36 VAL N N 127.2 0.2 1 185 37 37 ILE H H 8.82 0.02 1 186 37 37 ILE C C 174.3 0.2 1 187 37 37 ILE CA C 58.9 0.2 1 188 37 37 ILE CB C 40.2 0.2 1 189 37 37 ILE CG1 C 27.4 0.2 1 190 37 37 ILE N N 125.3 0.2 1 191 38 38 TYR H H 8.93 0.02 1 192 38 38 TYR C C 171.7 0.2 1 193 38 38 TYR CA C 54.5 0.2 1 194 38 38 TYR CB C 42.3 0.2 1 195 38 38 TYR N N 128.8 0.2 1 196 39 39 PHE H H 10.02 0.02 1 197 39 39 PHE C C 175.8 0.2 1 198 39 39 PHE CA C 56.1 0.2 1 199 39 39 PHE CB C 41.2 0.2 1 200 39 39 PHE N N 122.4 0.2 1 201 40 40 TYR H H 9.61 0.02 1 202 40 40 TYR N N 122.6 0.2 1 203 41 41 PRO C C 178.7 0.2 1 204 42 42 LYS H H 9.61 0.02 1 205 42 42 LYS C C 173.2 0.2 1 206 42 42 LYS CA C 56.7 0.2 1 207 42 42 LYS N N 122.6 0.2 1 208 43 43 ASP H H 9.01 0.02 1 209 43 43 ASP C C 176.4 0.2 1 210 43 43 ASP CA C 55.9 0.2 1 211 43 43 ASP N N 126.8 0.2 1 212 47 47 GLY C C 175.3 0.2 1 213 47 47 GLY CA C 47.4 0.2 1 214 48 48 CYS H H 7.43 0.02 1 215 48 48 CYS C C 180.6 0.2 1 216 48 48 CYS CA C 64.9 0.2 1 217 48 48 CYS CB C 32.2 0.2 1 218 48 48 CYS N N 124.8 0.2 1 219 49 49 THR H H 8.80 0.02 1 220 49 49 THR C C 174.8 0.2 1 221 49 49 THR CA C 68.4 0.2 1 222 49 49 THR N N 119.4 0.2 1 223 50 50 THR H H 8.23 0.02 1 224 50 50 THR C C 174.9 0.2 1 225 50 50 THR N N 118.7 0.2 1 226 51 51 GLU H H 8.40 0.02 1 227 51 51 GLU C C 177.5 0.2 1 228 51 51 GLU CA C 59.5 0.2 1 229 51 51 GLU CB C 28.4 0.2 1 230 51 51 GLU N N 119.1 0.2 1 231 52 52 GLY H H 7.71 0.02 1 232 52 52 GLY C C 176.0 0.2 1 233 52 52 GLY CA C 48.1 0.2 1 234 52 52 GLY N N 103.3 0.2 1 235 53 53 LEU H H 8.83 0.02 1 236 53 53 LEU C C 180.2 0.2 1 237 53 53 LEU CA C 58.0 0.2 1 238 53 53 LEU CB C 42.1 0.2 1 239 53 53 LEU N N 122.3 0.2 1 240 54 54 ASP H H 8.65 0.02 1 241 54 54 ASP C C 179.9 0.2 1 242 54 54 ASP CA C 56.8 0.2 1 243 54 54 ASP CB C 39.6 0.2 1 244 54 54 ASP N N 123.2 0.2 1 245 55 55 PHE H H 7.74 0.02 1 246 55 55 PHE C C 178.2 0.2 1 247 55 55 PHE CA C 63.9 0.2 1 248 55 55 PHE CB C 38.5 0.2 1 249 55 55 PHE N N 117.6 0.2 1 250 56 56 ASN H H 8.89 0.02 1 251 56 56 ASN C C 179.0 0.2 1 252 56 56 ASN CA C 57.0 0.2 1 253 56 56 ASN CB C 40.3 0.2 1 254 56 56 ASN N N 116.5 0.2 1 255 57 57 ALA H H 8.39 0.02 1 256 57 57 ALA C C 179.5 0.2 1 257 57 57 ALA CA C 54.3 0.2 1 258 57 57 ALA CB C 18.4 0.2 1 259 57 57 ALA N N 119.4 0.2 1 260 58 58 LEU H H 7.27 0.02 1 261 58 58 LEU C C 177.7 0.2 1 262 58 58 LEU CA C 53.8 0.2 1 263 58 58 LEU CB C 44.4 0.2 1 264 58 58 LEU N N 114.9 0.2 1 265 59 59 LEU H H 7.77 0.02 1 266 59 59 LEU C C 174.6 0.2 1 267 59 59 LEU CA C 60.5 0.2 1 268 59 59 LEU CB C 40.2 0.2 1 269 59 59 LEU N N 125.3 0.2 1 270 60 60 PRO C C 180.2 0.2 1 271 60 60 PRO CA C 66.3 0.2 1 272 60 60 PRO CB C 31.3 0.2 1 273 60 60 PRO CG C 28.6 0.2 1 274 61 61 GLU H H 7.71 0.02 1 275 61 61 GLU C C 180.2 0.2 1 276 61 61 GLU CA C 58.3 0.2 1 277 61 61 GLU CB C 29.8 0.2 1 278 61 61 GLU CG C 35.6 0.2 1 279 61 61 GLU N N 115.7 0.2 1 280 62 62 PHE H H 8.30 0.02 1 281 62 62 PHE C C 178.1 0.2 1 282 62 62 PHE CA C 64.0 0.2 1 283 62 62 PHE CB C 38.4 0.2 1 284 62 62 PHE N N 120.8 0.2 1 285 63 63 ASP H H 9.20 0.02 1 286 63 63 ASP C C 180.7 0.2 1 287 63 63 ASP CA C 57.7 0.2 1 288 63 63 ASP CB C 41.3 0.2 1 289 63 63 ASP N N 119.6 0.2 1 290 64 64 LYS H H 7.79 0.02 1 291 64 64 LYS C C 177.7 0.2 1 292 64 64 LYS CA C 59.3 0.2 1 293 64 64 LYS CB C 32.6 0.2 1 294 64 64 LYS CD C 29.4 0.2 1 295 64 64 LYS CG C 25.1 0.2 1 296 64 64 LYS N N 120.4 0.2 1 297 65 65 ALA H H 7.40 0.02 1 298 65 65 ALA C C 176.5 0.2 1 299 65 65 ALA CA C 52.0 0.2 1 300 65 65 ALA CB C 18.5 0.2 1 301 65 65 ALA N N 119.2 0.2 1 302 66 66 GLY H H 7.96 0.02 1 303 66 66 GLY C C 174.4 0.2 1 304 66 66 GLY CA C 46.1 0.2 1 305 66 66 GLY N N 105.5 0.2 1 306 67 67 ALA H H 8.44 0.02 1 307 67 67 ALA C C 176.8 0.2 1 308 67 67 ALA CA C 49.8 0.2 1 309 67 67 ALA CB C 24.7 0.2 1 310 67 67 ALA N N 121.5 0.2 1 311 68 68 LYS H H 8.17 0.02 1 312 68 68 LYS C C 173.9 0.2 1 313 68 68 LYS CA C 53.5 0.2 1 314 68 68 LYS CB C 34.6 0.2 1 315 68 68 LYS N N 119.1 0.2 1 316 69 69 ILE H H 8.05 0.02 1 317 69 69 ILE C C 174.9 0.2 1 318 69 69 ILE CA C 59.5 0.2 1 319 69 69 ILE CB C 40.2 0.2 1 320 69 69 ILE CG1 C 26.9 0.2 1 321 69 69 ILE N N 119.3 0.2 1 322 70 70 LEU H H 8.43 0.02 1 323 70 70 LEU C C 175.1 0.2 1 324 70 70 LEU CA C 53.9 0.2 1 325 70 70 LEU CB C 46.5 0.2 1 326 70 70 LEU N N 124.1 0.2 1 327 71 71 GLY H H 7.48 0.02 1 328 71 71 GLY C C 173.4 0.2 1 329 71 71 GLY CA C 43.6 0.2 1 330 71 71 GLY N N 106.8 0.2 1 331 72 72 VAL H H 8.89 0.02 1 332 72 72 VAL C C 174.0 0.2 1 333 72 72 VAL CA C 61.8 0.2 1 334 72 72 VAL CB C 34.8 0.2 1 335 72 72 VAL CG1 C 22.3 0.2 2 336 72 72 VAL CG2 C 19.3 0.2 2 337 72 72 VAL N N 122.4 0.2 1 338 73 73 SER H H 7.76 0.02 1 339 73 73 SER C C 173.4 0.2 1 340 73 73 SER CA C 56.9 0.2 1 341 73 73 SER CB C 66.2 0.2 1 342 73 73 SER N N 117.8 0.2 1 343 74 74 ARG H H 8.19 0.02 1 344 74 74 ARG C C 175.2 0.2 1 345 74 74 ARG CA C 56.1 0.2 1 346 74 74 ARG CB C 30.0 0.2 1 347 74 74 ARG CG C 26.4 0.2 1 348 74 74 ARG N N 116.4 0.2 1 349 75 75 ASP H H 7.93 0.02 1 350 75 75 ASP C C 174.7 0.2 1 351 75 75 ASP CA C 55.2 0.2 1 352 75 75 ASP CB C 43.7 0.2 1 353 75 75 ASP N N 117.2 0.2 1 354 76 76 SER H H 8.46 0.02 1 355 76 76 SER C C 173.6 0.2 1 356 76 76 SER CA C 57.6 0.2 1 357 76 76 SER CB C 65.3 0.2 1 358 76 76 SER N N 115.1 0.2 1 359 77 77 VAL H H 8.76 0.02 1 360 77 77 VAL C C 177.4 0.2 1 361 77 77 VAL CA C 68.4 0.2 1 362 77 77 VAL CB C 31.7 0.2 1 363 77 77 VAL N N 121.1 0.2 1 364 78 78 LYS H H 8.25 0.02 1 365 78 78 LYS C C 179.3 0.2 1 366 78 78 LYS CA C 59.7 0.2 1 367 78 78 LYS CB C 32.0 0.2 1 368 78 78 LYS CD C 29.0 0.2 1 369 78 78 LYS CG C 24.7 0.2 1 370 78 78 LYS N N 118.8 0.2 1 371 79 79 SER H H 8.05 0.02 1 372 79 79 SER C C 179.1 0.2 1 373 79 79 SER CA C 61.2 0.2 1 374 79 79 SER CB C 62.8 0.2 1 375 79 79 SER N N 114.5 0.2 1 376 80 80 HIS H H 8.96 0.02 1 377 80 80 HIS C C 176.9 0.2 1 378 80 80 HIS CA C 56.4 0.2 1 379 80 80 HIS CB C 28.7 0.2 1 380 80 80 HIS N N 118.5 0.2 1 381 81 81 ASP H H 9.77 0.02 1 382 81 81 ASP C C 179.6 0.2 1 383 81 81 ASP CA C 58.0 0.2 1 384 81 81 ASP CB C 39.6 0.2 1 385 81 81 ASP N N 122.9 0.2 1 386 82 82 ASN H H 7.99 0.02 1 387 82 82 ASN C C 176.4 0.2 1 388 82 82 ASN CA C 56.8 0.2 1 389 82 82 ASN CB C 38.8 0.2 1 390 82 82 ASN N N 120.3 0.2 1 391 83 83 PHE H H 8.51 0.02 1 392 83 83 PHE C C 177.2 0.2 1 393 83 83 PHE CA C 56.9 0.2 1 394 83 83 PHE CB C 40.1 0.2 1 395 83 83 PHE N N 122.3 0.2 1 396 84 84 CYS H H 9.13 0.02 1 397 84 84 CYS C C 177.7 0.2 1 398 84 84 CYS CA C 63.9 0.2 1 399 84 84 CYS CB C 26.9 0.2 1 400 84 84 CYS N N 114.5 0.2 1 401 85 85 ALA H H 8.01 0.02 1 402 85 85 ALA C C 180.2 0.2 1 403 85 85 ALA CA C 54.7 0.2 1 404 85 85 ALA CB C 18.3 0.2 1 405 85 85 ALA N N 121.2 0.2 1 406 86 86 LYS H H 8.12 0.02 1 407 86 86 LYS C C 178.6 0.2 1 408 86 86 LYS CA C 58.2 0.2 1 409 86 86 LYS CB C 32.5 0.2 1 410 86 86 LYS CD C 28.3 0.2 1 411 86 86 LYS CG C 24.9 0.2 1 412 86 86 LYS N N 117.1 0.2 1 413 87 87 GLN H H 7.32 0.02 1 414 87 87 GLN C C 176.1 0.2 1 415 87 87 GLN CA C 53.8 0.2 1 416 87 87 GLN CB C 27.8 0.2 1 417 87 87 GLN CG C 33.1 0.2 1 418 87 87 GLN N N 111.4 0.2 1 419 88 88 GLY H H 7.60 0.02 1 420 88 88 GLY C C 175.7 0.2 1 421 88 88 GLY CA C 46.0 0.2 1 422 88 88 GLY N N 106.7 0.2 1 423 89 89 PHE H H 6.64 0.02 1 424 89 89 PHE C C 177.3 0.2 1 425 89 89 PHE CA C 55.0 0.2 1 426 89 89 PHE CB C 37.3 0.2 1 427 89 89 PHE N N 116.1 0.2 1 428 90 90 ALA H H 9.18 0.02 1 429 90 90 ALA C C 175.1 0.2 1 430 90 90 ALA CA C 51.1 0.2 1 431 90 90 ALA CB C 18.9 0.2 1 432 90 90 ALA N N 125.8 0.2 1 433 91 91 PHE H H 6.63 0.02 1 434 91 91 PHE C C 171.3 0.2 1 435 91 91 PHE CA C 53.1 0.2 1 436 91 91 PHE CB C 39.0 0.2 1 437 91 91 PHE N N 117.0 0.2 1 438 92 92 PRO C C 174.5 0.2 1 439 92 92 PRO CA C 61.7 0.2 1 440 92 92 PRO CB C 33.4 0.2 1 441 93 93 LEU H H 7.72 0.02 1 442 93 93 LEU C C 177.3 0.2 1 443 93 93 LEU CA C 51.2 0.2 1 444 93 93 LEU CB C 44.1 0.2 1 445 93 93 LEU N N 114.6 0.2 1 446 94 94 VAL H H 9.99 0.02 1 447 94 94 VAL C C 179.6 0.2 1 448 94 94 VAL CA C 61.3 0.2 1 449 94 94 VAL CB C 33.4 0.2 1 450 94 94 VAL CG1 C 21.9 0.2 2 451 94 94 VAL CG2 C 21.9 0.2 2 452 94 94 VAL N N 122.9 0.2 1 453 95 95 SER H H 9.64 0.02 1 454 95 95 SER C C 172.8 0.2 1 455 95 95 SER CA C 56.1 0.2 1 456 95 95 SER CB C 63.0 0.2 1 457 95 95 SER N N 126.2 0.2 1 458 96 96 ASP H H 9.08 0.02 1 459 96 96 ASP C C 178.2 0.2 1 460 96 96 ASP CA C 52.3 0.2 1 461 96 96 ASP CB C 42.1 0.2 1 462 96 96 ASP N N 133.1 0.2 1 463 97 97 GLY H H 7.88 0.02 1 464 97 97 GLY C C 174.9 0.2 1 465 97 97 GLY CA C 48.0 0.2 1 466 97 97 GLY N N 108.1 0.2 1 467 98 98 ASP H H 8.27 0.02 1 468 98 98 ASP C C 176.3 0.2 1 469 98 98 ASP CA C 52.8 0.2 1 470 98 98 ASP CB C 40.1 0.2 1 471 98 98 ASP N N 117.0 0.2 1 472 99 99 GLU H H 7.94 0.02 1 473 99 99 GLU C C 174.8 0.2 1 474 99 99 GLU CA C 57.7 0.2 1 475 99 99 GLU CB C 27.3 0.2 1 476 99 99 GLU CG C 37.2 0.2 1 477 99 99 GLU N N 112.2 0.2 1 478 100 100 ALA H H 7.75 0.02 1 479 100 100 ALA C C 181.3 0.2 1 480 100 100 ALA CA C 56.3 0.2 1 481 100 100 ALA CB C 20.0 0.2 1 482 100 100 ALA N N 122.9 0.2 1 483 101 101 LEU H H 10.60 0.02 1 484 101 101 LEU C C 179.9 0.2 1 485 101 101 LEU CA C 57.8 0.2 1 486 101 101 LEU CB C 41.8 0.2 1 487 101 101 LEU N N 123.8 0.2 1 488 102 102 CYS H H 10.10 0.02 1 489 102 102 CYS C C 178.2 0.2 1 490 102 102 CYS CA C 63.3 0.2 1 491 102 102 CYS CB C 27.6 0.2 1 492 102 102 CYS N N 119.9 0.2 1 493 103 103 ARG H H 8.67 0.02 1 494 103 103 ARG C C 179.7 0.2 1 495 103 103 ARG CA C 59.2 0.2 1 496 103 103 ARG CB C 30.0 0.2 1 497 103 103 ARG CD C 43.2 0.2 1 498 103 103 ARG CG C 28.8 0.2 1 499 103 103 ARG N N 117.0 0.2 1 500 104 104 ALA H H 7.69 0.02 1 501 104 104 ALA C C 178.0 0.2 1 502 104 104 ALA CA C 55.4 0.2 1 503 104 104 ALA CB C 18.4 0.2 1 504 104 104 ALA N N 123.9 0.2 1 505 105 105 PHE H H 7.58 0.02 1 506 105 105 PHE C C 174.0 0.2 1 507 105 105 PHE CA C 58.8 0.2 1 508 105 105 PHE CB C 39.2 0.2 1 509 105 105 PHE N N 111.8 0.2 1 510 106 106 ASP H H 7.76 0.02 1 511 106 106 ASP C C 175.6 0.2 1 512 106 106 ASP N N 121.2 0.2 1 513 107 107 VAL H H 7.59 0.02 1 514 107 107 VAL C C 175.3 0.2 1 515 107 107 VAL CA C 60.5 0.2 1 516 107 107 VAL CB C 30.8 0.2 1 517 107 107 VAL CG1 C 21.0 0.2 2 518 107 107 VAL CG2 C 19.6 0.2 2 519 107 107 VAL N N 121.2 0.2 1 520 108 108 ILE H H 7.76 0.02 1 521 108 108 ILE C C 175.8 0.2 1 522 108 108 ILE CA C 59.3 0.2 1 523 108 108 ILE CB C 36.1 0.2 1 524 108 108 ILE N N 121.2 0.2 1 525 109 109 LYS H H 8.65 0.02 1 526 109 109 LYS C C 175.4 0.2 1 527 109 109 LYS CA C 53.0 0.2 1 528 109 109 LYS CB C 36.1 0.2 1 529 109 109 LYS CG C 24.2 0.2 1 530 109 109 LYS N N 127.3 0.2 1 531 110 110 GLU H H 8.64 0.02 1 532 110 110 GLU C C 176.1 0.2 1 533 110 110 GLU CA C 56.3 0.2 1 534 110 110 GLU CB C 30.9 0.2 1 535 110 110 GLU CG C 36.8 0.2 1 536 110 110 GLU N N 121.6 0.2 1 537 111 111 LYS H H 8.96 0.02 1 538 111 111 LYS C C 174.4 0.2 1 539 111 111 LYS CA C 55.0 0.2 1 540 111 111 LYS CB C 35.1 0.2 1 541 111 111 LYS CD C 29.1 0.2 1 542 111 111 LYS CG C 24.2 0.2 1 543 111 111 LYS N N 124.4 0.2 1 544 112 112 ASN H H 8.58 0.02 1 545 112 112 ASN C C 175.3 0.2 1 546 112 112 ASN N N 120.8 0.2 1 547 113 113 MET H H 8.93 0.02 1 548 113 113 MET C C 175.4 0.3 1 549 113 113 MET CA C 54.6 0.2 1 550 113 113 MET CB C 33.7 0.2 1 551 113 113 MET CG C 31.6 0.2 1 552 113 113 MET N N 124.4 0.2 1 553 114 114 TYR H H 8.84 0.02 1 554 114 114 TYR C C 176.0 0.2 1 555 114 114 TYR CA C 58.0 0.2 1 556 114 114 TYR CB C 36.2 0.2 1 557 114 114 TYR N N 122.2 0.2 1 558 115 115 GLY H H 8.30 0.02 1 559 115 115 GLY C C 174.0 0.2 1 560 115 115 GLY CA C 45.5 0.2 1 561 115 115 GLY N N 105.9 0.2 1 562 116 116 LYS H H 7.78 0.02 1 563 116 116 LYS C C 175.0 0.2 1 564 116 116 LYS CA C 54.6 0.2 1 565 116 116 LYS CB C 34.5 0.2 1 566 116 116 LYS CD C 28.8 0.2 1 567 116 116 LYS CG C 24.5 0.2 1 568 116 116 LYS N N 120.5 0.2 1 569 117 117 GLN H H 8.52 0.02 1 570 117 117 GLN C C 175.9 0.2 1 571 117 117 GLN CA C 55.6 0.2 1 572 117 117 GLN CB C 29.4 0.2 1 573 117 117 GLN CG C 34.1 0.2 1 574 117 117 GLN N N 121.5 0.2 1 575 118 118 VAL H H 8.91 0.02 1 576 118 118 VAL C C 174.8 0.2 1 577 118 118 VAL CA C 60.8 0.2 1 578 118 118 VAL CB C 35.0 0.2 1 579 118 118 VAL CG1 C 21.2 0.2 2 580 118 118 VAL CG2 C 20.5 0.2 2 581 118 118 VAL N N 123.7 0.2 1 582 119 119 LEU H H 8.60 0.02 1 583 119 119 LEU C C 177.5 0.2 1 584 119 119 LEU CA C 54.0 0.2 1 585 119 119 LEU CB C 42.9 0.2 1 586 119 119 LEU CD1 C 25.0 0.2 2 587 119 119 LEU CD2 C 23.7 0.2 2 588 119 119 LEU N N 125.8 0.2 1 589 120 120 GLY H H 8.49 0.02 1 590 120 120 GLY C C 171.7 0.2 1 591 120 120 GLY CA C 44.7 0.2 1 592 120 120 GLY N N 109.5 0.2 1 593 121 121 ILE H H 8.23 0.02 1 594 121 121 ILE C C 175.6 0.2 1 595 121 121 ILE CA C 62.3 0.2 1 596 121 121 ILE CB C 39.9 0.2 1 597 121 121 ILE CG1 C 29.1 0.2 1 598 121 121 ILE N N 119.6 0.2 1 599 122 122 GLU H H 9.10 0.02 1 600 122 122 GLU C C 175.9 0.2 1 601 122 122 GLU CA C 55.0 0.2 1 602 122 122 GLU CB C 31.6 0.2 1 603 122 122 GLU N N 130.7 0.2 1 604 123 123 ARG H H 9.06 0.02 1 605 123 123 ARG C C 176.0 0.2 1 606 123 123 ARG CA C 59.2 0.2 1 607 123 123 ARG CB C 30.5 0.2 1 608 123 123 ARG N N 134.1 0.2 1 609 124 124 SER H H 7.93 0.02 1 610 124 124 SER C C 171.3 0.2 1 611 124 124 SER CA C 58.6 0.2 1 612 124 124 SER CB C 69.6 0.2 1 613 124 124 SER N N 124.3 0.2 1 614 125 125 THR H H 9.72 0.02 1 615 125 125 THR C C 171.3 0.2 1 616 125 125 THR CA C 61.2 0.2 1 617 125 125 THR CB C 71.1 0.2 1 618 125 125 THR N N 123.3 0.2 1 619 126 126 PHE H H 9.55 0.02 1 620 126 126 PHE C C 172.7 0.2 1 621 126 126 PHE CA C 57.1 0.2 1 622 126 126 PHE CB C 43.7 0.2 1 623 126 126 PHE N N 123.5 0.2 1 624 127 127 LEU H H 8.91 0.02 1 625 127 127 LEU C C 174.2 0.2 1 626 127 127 LEU CA C 53.6 0.2 1 627 127 127 LEU CB C 46.0 0.2 1 628 127 127 LEU N N 122.6 0.2 1 629 128 128 LEU H H 10.18 0.02 1 630 128 128 LEU C C 175.9 0.2 1 631 128 128 LEU CA C 54.5 0.2 1 632 128 128 LEU CB C 44.4 0.2 1 633 128 128 LEU N N 130.3 0.2 1 634 129 129 SER H H 9.30 0.02 1 635 129 129 SER C C 174.3 0.2 1 636 129 129 SER CA C 55.5 0.2 1 637 129 129 SER CB C 63.2 0.2 1 638 129 129 SER N N 117.0 0.2 1 639 130 130 PRO C C 177.2 0.2 1 640 130 130 PRO CA C 64.2 0.2 1 641 130 130 PRO CB C 31.9 0.2 1 642 131 131 GLU H H 7.21 0.02 1 643 131 131 GLU C C 176.3 0.2 1 644 131 131 GLU CA C 56.0 0.2 1 645 131 131 GLU CB C 29.4 0.2 1 646 131 131 GLU CG C 36.8 0.2 1 647 131 131 GLU N N 112.7 0.2 1 648 132 132 GLY H H 8.39 0.02 1 649 132 132 GLY C C 172.9 0.2 1 650 132 132 GLY CA C 45.9 0.2 1 651 132 132 GLY N N 109.5 0.2 1 652 133 133 GLN H H 7.20 0.02 1 653 133 133 GLN C C 176.1 0.2 1 654 133 133 GLN CA C 54.2 0.2 1 655 133 133 GLN CB C 30.1 0.2 1 656 133 133 GLN CG C 33.9 0.2 1 657 133 133 GLN N N 115.2 0.2 1 658 134 134 VAL H H 9.42 0.02 1 659 134 134 VAL C C 176.1 0.2 1 660 134 134 VAL CA C 63.1 0.2 1 661 134 134 VAL CB C 30.6 0.2 1 662 134 134 VAL N N 124.6 0.2 1 663 135 135 VAL H H 8.91 0.02 1 664 135 135 VAL C C 175.7 0.2 1 665 135 135 VAL CA C 62.1 0.2 1 666 135 135 VAL CB C 32.8 0.2 1 667 135 135 VAL CG1 C 21.4 0.2 . 668 135 135 VAL CG2 C 19.8 0.2 . 669 135 135 VAL N N 122.6 0.2 1 670 136 136 GLN H H 7.73 0.02 1 671 136 136 GLN C C 171.6 0.2 1 672 136 136 GLN CA C 57.2 0.2 1 673 136 136 GLN CB C 30.3 0.2 1 674 136 136 GLN CG C 32.5 0.2 1 675 136 136 GLN N N 119.3 0.2 1 676 137 137 ALA H H 8.34 0.02 1 677 137 137 ALA C C 175.5 0.2 1 678 137 137 ALA CA C 50.9 0.2 1 679 137 137 ALA CB C 24.0 0.2 1 680 137 137 ALA N N 125.9 0.2 1 681 138 138 TRP H H 9.42 0.02 1 682 138 138 TRP HE1 H 10.37 0.02 1 683 138 138 TRP C C 174.4 0.2 1 684 138 138 TRP CA C 58.4 0.2 1 685 138 138 TRP CB C 32.9 0.2 1 686 138 138 TRP N N 123.9 0.2 1 687 138 138 TRP NE1 N 129.8 0.2 1 688 139 139 ARG H H 8.70 0.02 1 689 139 139 ARG C C 176.1 0.2 1 690 139 139 ARG CA C 55.2 0.2 1 691 139 139 ARG N N 120.8 0.2 1 692 140 140 LYS H H 7.61 0.02 1 693 140 140 LYS C C 176.1 0.2 1 694 140 140 LYS CA C 57.8 0.2 1 695 140 140 LYS CB C 30.1 0.2 1 696 140 140 LYS CG C 25.7 0.2 1 697 140 140 LYS N N 121.1 0.2 1 698 141 141 VAL H H 7.65 0.02 1 699 141 141 VAL C C 176.5 0.2 1 700 141 141 VAL CA C 63.4 0.2 1 701 141 141 VAL CB C 33.3 0.2 1 702 141 141 VAL CG1 C 23.7 0.2 2 703 141 141 VAL CG2 C 23.7 0.2 2 704 141 141 VAL N N 118.6 0.2 1 705 142 142 LYS H H 8.32 0.02 1 706 142 142 LYS C C 176.1 0.2 1 707 142 142 LYS CA C 54.1 0.2 1 708 142 142 LYS CB C 32.5 0.2 1 709 142 142 LYS CD C 29.2 0.2 1 710 142 142 LYS CG C 24.7 0.2 1 711 142 142 LYS N N 128.0 0.2 1 712 143 143 VAL H H 8.48 0.02 1 713 143 143 VAL C C 177.0 0.2 1 714 143 143 VAL CA C 67.9 0.2 1 715 143 143 VAL CB C 32.0 0.2 1 716 143 143 VAL CG1 C 23.1 0.2 . 717 143 143 VAL CG2 C 21.3 0.2 . 718 143 143 VAL N N 124.5 0.2 1 719 144 144 ALA H H 8.26 0.02 1 720 144 144 ALA C C 179.2 0.2 1 721 144 144 ALA CA C 54.1 0.2 1 722 144 144 ALA CB C 17.3 0.2 1 723 144 144 ALA N N 122.0 0.2 1 724 145 145 GLY H H 9.26 0.02 1 725 145 145 GLY C C 175.9 0.2 1 726 145 145 GLY CA C 45.8 0.2 1 727 145 145 GLY N N 114.5 0.2 1 728 146 146 HIS H H 8.35 0.02 1 729 146 146 HIS C C 175.8 0.2 1 730 146 146 HIS CA C 59.7 0.2 1 731 146 146 HIS CB C 28.2 0.2 1 732 146 146 HIS N N 122.3 0.2 1 733 147 147 ALA H H 8.31 0.02 1 734 147 147 ALA C C 179.0 0.2 1 735 147 147 ALA CA C 56.1 0.2 1 736 147 147 ALA CB C 16.4 0.2 1 737 147 147 ALA N N 121.3 0.2 1 738 148 148 ASP H H 7.80 0.02 1 739 148 148 ASP C C 178.9 0.2 1 740 148 148 ASP CA C 57.1 0.2 1 741 148 148 ASP CB C 40.9 0.2 1 742 148 148 ASP N N 114.6 0.2 1 743 149 149 ALA H H 7.62 0.02 1 744 149 149 ALA C C 181.1 0.2 1 745 149 149 ALA CA C 54.9 0.2 1 746 149 149 ALA CB C 17.5 0.2 1 747 149 149 ALA N N 124.2 0.2 1 748 150 150 VAL H H 8.20 0.02 1 749 150 150 VAL C C 177.7 0.2 1 750 150 150 VAL CA C 65.6 0.2 1 751 150 150 VAL CG1 C 21.4 0.2 2 752 150 150 VAL CG2 C 21.4 0.2 2 753 150 150 VAL N N 122.7 0.2 1 754 151 151 LEU H H 8.13 0.02 1 755 151 151 LEU C C 177.9 0.2 1 756 151 151 LEU CA C 57.8 0.2 1 757 151 151 LEU CB C 40.1 0.2 1 758 151 151 LEU N N 120.7 0.2 1 759 152 152 ALA H H 7.88 0.02 1 760 152 152 ALA C C 180.8 0.2 1 761 152 152 ALA CA C 55.1 0.2 1 762 152 152 ALA CB C 17.6 0.2 1 763 152 152 ALA N N 119.2 0.2 1 764 153 153 ALA H H 8.04 0.02 1 765 153 153 ALA C C 179.5 0.2 1 766 153 153 ALA CA C 54.7 0.2 1 767 153 153 ALA CB C 18.4 0.2 1 768 153 153 ALA N N 121.9 0.2 1 769 154 154 LEU H H 8.70 0.02 1 770 154 154 LEU C C 177.7 0.2 1 771 154 154 LEU CA C 58.6 0.2 1 772 154 154 LEU CB C 41.0 0.2 1 773 154 154 LEU N N 120.8 0.2 1 774 155 155 LYS H H 8.24 0.02 1 775 155 155 LYS C C 178.8 0.2 1 776 155 155 LYS CA C 60.1 0.2 1 777 155 155 LYS CB C 32.1 0.2 1 778 155 155 LYS N N 116.4 0.2 1 779 156 156 ALA H H 7.51 0.02 1 780 156 156 ALA C C 180.4 0.2 1 781 156 156 ALA CA C 54.5 0.2 1 782 156 156 ALA CB C 18.0 0.2 1 783 156 156 ALA N N 119.8 0.2 1 784 157 157 HIS H H 8.21 0.02 1 785 157 157 HIS C C 177.0 0.2 1 786 157 157 HIS CA C 59.4 0.2 1 787 157 157 HIS CB C 31.1 0.2 1 788 157 157 HIS N N 117.2 0.2 1 789 158 158 ALA H H 8.31 0.02 1 790 158 158 ALA C C 177.4 0.2 1 791 158 158 ALA CA C 53.1 0.2 1 792 158 158 ALA CB C 18.1 0.2 1 793 158 158 ALA N N 120.3 0.2 1 794 159 159 LYS H H 7.55 0.02 1 795 159 159 LYS C C 175.7 0.2 1 796 159 159 LYS CA C 56.7 0.2 1 797 159 159 LYS CB C 31.9 0.2 1 798 159 159 LYS CD C 29.1 0.2 1 799 159 159 LYS CE C 42.3 0.2 1 800 159 159 LYS CG C 24.5 0.2 1 801 159 159 LYS N N 118.4 0.2 1 802 160 160 GLN H H 8.04 0.02 1 803 160 160 GLN C C 180.8 0.2 1 804 160 160 GLN CA C 57.2 0.2 1 805 160 160 GLN CB C 30.7 0.2 1 806 160 160 GLN N N 126.0 0.2 1 stop_ save_