data_50025 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB) ; _BMRB_accession_number 50025 _BMRB_flat_file_name bmr50025.str _Entry_type original _Submission_date 2019-09-25 _Accession_date 2019-09-25 _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 Bartkevihi Leonardo . . 2 Almeida Fabio . . 3 'Ano Bom' Cristiane . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "13C chemical shifts" 416 "15N chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-05-08 update BMRB 'update entry citation' 2020-03-27 original author 'original release' stop_ _Original_release_date 2019-09-25 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32030620 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bartkevihi Leonardo . . 2 Martins Bruna . . 3 'de Oliveira' 'Danielle Maria Perpetua' . . 4 Pires 'Jose Ricardo' . . 5 Anobom 'Cristiane Dinis' D. . 6 Almeida Fabio . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 14 _Journal_issue 1 _Journal_ISSN 1874-270X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 119 _Page_last 122 _Year 2020 _Details . loop_ _Keyword 'Mycobacterium tuberculosis' 'Ribose-5-phosphate isomerase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'MtRpiB dimer' _Enzyme_commission_number 5.3.1.6 loop_ _Mol_system_component_name _Mol_label 'Molecule 1, 1' $entity_1 'Molecule 1, 2' $entity_1 stop_ _System_molecular_weight 36625.3392 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Catalyzes the interconversion of ribulose-5-phosphate and ribose-5-phosphate' stop_ _Database_query_date . _Details 'The protein is a homodimer with two active sites in the interface of dimerization.' save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 18312.6696 _Mol_thiol_state 'all free' loop_ _Biological_function 'Catalyzes the interconversion of ribulose-5-phosphate and ribose-5-phosphate' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 170 _Mol_residue_sequence ; MAHHHHHHMSGMRVYLGADH AGYELKQRIIEHLKQTGHEP IDCGALRYDADDDYPAFCIA AATRTVADPGSLGIVLGGSG NGEQIAANKVPGARCALAWS VQTAALAREHNNAQLIGIGG RMHTVAEALAIVDAFVTTPW SKAQRHQRRIDILAEYERTH EAPPVPGAPA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 MET 10 SER 11 GLY 12 MET 13 ARG 14 VAL 15 TYR 16 LEU 17 GLY 18 ALA 19 ASP 20 HIS 21 ALA 22 GLY 23 TYR 24 GLU 25 LEU 26 LYS 27 GLN 28 ARG 29 ILE 30 ILE 31 GLU 32 HIS 33 LEU 34 LYS 35 GLN 36 THR 37 GLY 38 HIS 39 GLU 40 PRO 41 ILE 42 ASP 43 CYS 44 GLY 45 ALA 46 LEU 47 ARG 48 TYR 49 ASP 50 ALA 51 ASP 52 ASP 53 ASP 54 TYR 55 PRO 56 ALA 57 PHE 58 CYS 59 ILE 60 ALA 61 ALA 62 ALA 63 THR 64 ARG 65 THR 66 VAL 67 ALA 68 ASP 69 PRO 70 GLY 71 SER 72 LEU 73 GLY 74 ILE 75 VAL 76 LEU 77 GLY 78 GLY 79 SER 80 GLY 81 ASN 82 GLY 83 GLU 84 GLN 85 ILE 86 ALA 87 ALA 88 ASN 89 LYS 90 VAL 91 PRO 92 GLY 93 ALA 94 ARG 95 CYS 96 ALA 97 LEU 98 ALA 99 TRP 100 SER 101 VAL 102 GLN 103 THR 104 ALA 105 ALA 106 LEU 107 ALA 108 ARG 109 GLU 110 HIS 111 ASN 112 ASN 113 ALA 114 GLN 115 LEU 116 ILE 117 GLY 118 ILE 119 GLY 120 GLY 121 ARG 122 MET 123 HIS 124 THR 125 VAL 126 ALA 127 GLU 128 ALA 129 LEU 130 ALA 131 ILE 132 VAL 133 ASP 134 ALA 135 PHE 136 VAL 137 THR 138 THR 139 PRO 140 TRP 141 SER 142 LYS 143 ALA 144 GLN 145 ARG 146 HIS 147 GLN 148 ARG 149 ARG 150 ILE 151 ASP 152 ILE 153 LEU 154 ALA 155 GLU 156 TYR 157 GLU 158 ARG 159 THR 160 HIS 161 GLU 162 ALA 163 PRO 164 PRO 165 VAL 166 PRO 167 GLY 168 ALA 169 PRO 170 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $entity_1 'Mycobacterium tuberculosis' 1773 Bacteria . Mycobacterium tuberculosis 'ATCC 25618' Rv2465c stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) plasmid pCRT7/NT-TOPO 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 TRIS 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 5 mM 'natural abundance' 'sodium azide' 5 mM 'natural abundance' EDTA 5 mM 'natural abundance' PMSF 2 mM 'natural abundance' $entity_1 700 uM '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name 'CcpNmr Analysis' _Version 2.4 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'chemical shift assignments' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_software_2 _Saveframe_category software _Name DANGLE _Version 1.1 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Ascend _Field_strength 700 _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_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCACB_9 _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' 100 . mM pH 7.0 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 "'methyl protons" ppm 2.662318 internal indirect . . . 0.25144953 DSS H 1 "'methyl protons" ppm -0.034601993 internal indirect . . . 1 DSS N 15 "'methyl protons" ppm 0.000864778 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details 'TROSY offset.' loop_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' '3D HNCO' '3D HN(CA)CO' '3D HN(CO)CA' '3D HNCACB' '3D HN(CO)CACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'Molecule 1, 1' _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 10 10 SER H H 8.215 0.003 1 2 10 10 SER C C 174.360 0.02 1 3 10 10 SER N N 117.388 0.034 1 4 11 11 GLY H H 8.018 0.003 1 5 11 11 GLY N N 111.092 0.056 1 6 12 12 MET H H 8.035 0.003 1 7 12 12 MET C C 175.969 0.006 1 8 12 12 MET N N 120.233 0.06 1 9 13 13 ARG H H 8.445 0.004 1 10 13 13 ARG C C 174.981 0.03 1 11 13 13 ARG N N 125.271 0.029 1 12 14 14 VAL H H 7.593 0.003 1 13 14 14 VAL N N 123.131 0.08 1 14 15 15 TYR H H 9.542 0.004 1 15 15 15 TYR C C 175.910 0.012 1 16 15 15 TYR CA C 57.978 . 1 17 15 15 TYR CB C 38.746 . 1 18 15 15 TYR N N 128.488 0.027 1 19 16 16 LEU H H 8.767 0.005 1 20 16 16 LEU C C 175.956 . 1 21 16 16 LEU CA C 53.940 0.023 1 22 16 16 LEU CB C 45.416 0.031 1 23 16 16 LEU N N 121.070 0.022 1 24 17 17 GLY H H 8.096 0.006 1 25 17 17 GLY CA C 43.510 0.069 1 26 17 17 GLY N N 105.906 0.058 1 27 18 18 ALA H H 9.120 0.005 1 28 18 18 ALA C C 175.302 0.011 1 29 18 18 ALA CA C 51.829 0.037 1 30 18 18 ALA CB C 24.882 0.012 1 31 18 18 ALA N N 122.605 0.027 1 32 19 19 ASP H H 8.411 0.009 1 33 19 19 ASP C C 177.913 0.017 1 34 19 19 ASP CA C 51.356 0.06 1 35 19 19 ASP CB C 40.684 0.022 1 36 19 19 ASP N N 119.436 0.096 1 37 20 20 HIS H H 10.150 0.006 1 38 20 20 HIS C C 176.458 0.006 1 39 20 20 HIS CA C 58.600 0.006 1 40 20 20 HIS CB C 26.073 0.074 1 41 20 20 HIS N N 116.161 0.047 1 42 21 21 ALA H H 7.510 0.003 1 43 21 21 ALA C C 179.320 0.008 1 44 21 21 ALA CA C 53.386 0.052 1 45 21 21 ALA CB C 17.427 0.037 1 46 21 21 ALA N N 124.348 0.046 1 47 22 22 GLY H H 7.847 0.004 1 48 22 22 GLY C C 173.214 0.015 1 49 22 22 GLY CA C 44.009 0.0 1 50 22 22 GLY N N 104.789 0.04 1 51 23 23 TYR H H 7.522 0.003 1 52 23 23 TYR C C 176.018 0.003 1 53 23 23 TYR CA C 63.207 . 1 54 23 23 TYR CB C 38.842 0.031 1 55 23 23 TYR N N 123.368 0.057 1 56 24 24 GLU H H 8.913 0.004 1 57 24 24 GLU C C 179.398 0.008 1 58 24 24 GLU CA C 59.230 0.01 1 59 24 24 GLU CB C 28.152 0.018 1 60 24 24 GLU N N 120.329 0.036 1 61 25 25 LEU H H 8.330 0.003 1 62 25 25 LEU C C 178.323 0.009 1 63 25 25 LEU CA C 56.892 . 1 64 25 25 LEU CB C 39.346 . 1 65 25 25 LEU N N 121.532 0.032 1 66 26 26 LYS H H 8.509 0.004 1 67 26 26 LYS C C 177.133 0.012 1 68 26 26 LYS CA C 60.419 0.019 1 69 26 26 LYS CB C 28.788 0.005 1 70 26 26 LYS N N 120.782 0.062 1 71 27 27 GLN H H 7.541 0.004 1 72 27 27 GLN C C 179.260 0.002 1 73 27 27 GLN CA C 58.368 0.038 1 74 27 27 GLN CB C 27.510 0.004 1 75 27 27 GLN N N 117.214 0.066 1 76 28 28 ARG H H 7.447 0.003 1 77 28 28 ARG C C 179.827 . 1 78 28 28 ARG CA C 57.167 . 1 79 28 28 ARG CB C 28.669 . 1 80 28 28 ARG N N 118.600 0.037 1 81 29 29 ILE CA C 65.573 0.027 1 82 29 29 ILE CB C 36.469 0.021 1 83 30 30 ILE H H 8.594 0.003 1 84 30 30 ILE C C 177.405 0.044 1 85 30 30 ILE CA C 67.178 . 1 86 30 30 ILE CB C 37.129 . 1 87 30 30 ILE N N 122.605 0.025 1 88 31 31 GLU H H 7.235 0.003 1 89 31 31 GLU C C 178.598 0.075 1 90 31 31 GLU CA C 58.913 0.067 1 91 31 31 GLU CB C 28.594 0.027 1 92 31 31 GLU N N 117.390 0.061 1 93 32 32 HIS H H 8.019 0.003 1 94 32 32 HIS C C 178.571 0.056 1 95 32 32 HIS CA C 59.362 . 1 96 32 32 HIS CB C 31.352 . 1 97 32 32 HIS N N 119.230 0.065 1 98 33 33 LEU H H 9.054 0.003 1 99 33 33 LEU C C 178.640 0.008 1 100 33 33 LEU CA C 57.039 . 1 101 33 33 LEU CB C 40.632 . 1 102 33 33 LEU N N 119.666 0.034 1 103 34 34 LYS H H 8.037 0.007 1 104 34 34 LYS C C 180.788 0.013 1 105 34 34 LYS CA C 59.303 0.04 1 106 34 34 LYS CB C 31.360 0.012 1 107 34 34 LYS N N 119.133 0.047 1 108 35 35 GLN H H 7.985 0.004 1 109 35 35 GLN C C 177.599 0.001 1 110 35 35 GLN CA C 57.830 0.072 1 111 35 35 GLN CB C 27.692 0.022 1 112 35 35 GLN N N 118.848 0.05 1 113 36 36 THR H H 7.407 0.003 1 114 36 36 THR C C 174.261 0.003 1 115 36 36 THR CA C 60.704 0.01 1 116 36 36 THR CB C 68.767 0.002 1 117 36 36 THR N N 106.931 0.028 1 118 37 37 GLY H H 7.146 0.002 1 119 37 37 GLY C C 173.643 . 1 120 37 37 GLY CA C 45.531 0.026 1 121 37 37 GLY N N 106.700 0.055 1 122 38 38 HIS H H 7.963 0.004 1 123 38 38 HIS C C 173.329 0.017 1 124 38 38 HIS CA C 55.339 0.044 1 125 38 38 HIS CB C 31.782 0.004 1 126 38 38 HIS N N 120.212 0.043 1 127 39 39 GLU H H 8.705 0.005 1 128 39 39 GLU C C 172.449 . 1 129 39 39 GLU CA C 52.422 . 1 130 39 39 GLU CB C 30.232 . 1 131 39 39 GLU N N 120.766 0.033 1 132 40 40 PRO CA C 60.750 . 1 133 40 40 PRO CB C 32.041 0.021 1 134 41 41 ILE H H 9.307 0.004 1 135 41 41 ILE C C 174.230 0.03 1 136 41 41 ILE CA C 60.666 . 1 137 41 41 ILE CB C 38.004 . 1 138 41 41 ILE N N 126.955 0.062 1 139 42 42 ASP H H 8.640 0.004 1 140 42 42 ASP C C 177.276 0.008 1 141 42 42 ASP CA C 53.786 0.029 1 142 42 42 ASP CB C 40.537 0.005 1 143 42 42 ASP N N 127.559 0.03 1 144 43 43 CYS H H 9.534 0.005 1 145 43 43 CYS C C 174.223 0.021 1 146 43 43 CYS CA C 60.031 0.075 1 147 43 43 CYS CB C 27.482 0.027 1 148 43 43 CYS N N 125.439 0.036 1 149 44 44 GLY H H 8.505 0.004 1 150 44 44 GLY C C 174.017 0.167 1 151 44 44 GLY CA C 41.635 0.028 1 152 44 44 GLY N N 108.353 0.048 1 153 45 45 ALA H H 8.006 0.004 1 154 45 45 ALA C C 178.620 0.009 1 155 45 45 ALA CA C 52.587 0.046 1 156 45 45 ALA CB C 20.673 0.046 1 157 45 45 ALA N N 122.805 0.029 1 158 46 46 LEU H H 9.259 0.005 1 159 46 46 LEU C C 176.457 0.01 1 160 46 46 LEU CA C 55.260 0.06 1 161 46 46 LEU CB C 40.974 0.029 1 162 46 46 LEU N N 123.941 0.039 1 163 47 47 ARG H H 7.509 0.003 1 164 47 47 ARG C C 173.641 0.004 1 165 47 47 ARG CA C 53.007 0.02 1 166 47 47 ARG CB C 31.549 0.023 1 167 47 47 ARG N N 116.468 0.039 1 168 48 48 TYR H H 8.300 0.004 1 169 48 48 TYR C C 174.340 0.015 1 170 48 48 TYR CA C 58.722 0.061 1 171 48 48 TYR CB C 36.793 0.008 1 172 48 48 TYR N N 123.003 0.053 1 173 49 49 ASP H H 8.691 0.014 1 174 49 49 ASP C C 174.917 0.001 1 175 49 49 ASP CA C 52.452 0.0 1 176 49 49 ASP CB C 41.318 0.005 1 177 49 49 ASP N N 132.459 0.176 1 178 50 50 ALA H H 8.129 0.004 1 179 50 50 ALA C C 176.463 0.011 1 180 50 50 ALA CA C 53.150 0.026 1 181 50 50 ALA CB C 17.765 0.004 1 182 50 50 ALA N N 125.219 0.05 1 183 51 51 ASP H H 7.627 0.002 1 184 51 51 ASP C C 176.112 0.013 1 185 51 51 ASP CA C 53.734 0.059 1 186 51 51 ASP CB C 41.589 0.001 1 187 51 51 ASP N N 114.739 0.042 1 188 52 52 ASP H H 7.614 0.003 1 189 52 52 ASP C C 175.287 0.02 1 190 52 52 ASP CA C 53.913 0.097 1 191 52 52 ASP CB C 40.681 0.039 1 192 52 52 ASP N N 120.467 0.05 1 193 53 53 ASP H H 8.189 0.005 1 194 53 53 ASP C C 177.479 0.005 1 195 53 53 ASP CA C 53.716 0.203 1 196 53 53 ASP CB C 44.203 0.007 1 197 53 53 ASP N N 115.562 0.031 1 198 54 54 TYR H H 9.227 0.005 1 199 54 54 TYR C C 174.812 . 1 200 54 54 TYR CA C 61.827 . 1 201 54 54 TYR CB C 37.581 . 1 202 54 54 TYR N N 123.335 0.045 1 203 56 56 ALA H H 9.418 0.005 1 204 56 56 ALA C C 179.970 0.009 1 205 56 56 ALA CA C 55.257 0.04 1 206 56 56 ALA CB C 17.963 0.01 1 207 56 56 ALA N N 116.394 0.035 1 208 57 57 PHE H H 6.563 0.006 1 209 57 57 PHE C C 177.300 0.065 1 210 57 57 PHE CA C 59.601 0.021 1 211 57 57 PHE CB C 38.586 0.001 1 212 57 57 PHE N N 114.802 0.058 1 213 58 58 CYS H H 7.440 0.005 1 214 58 58 CYS C C 176.411 0.03 1 215 58 58 CYS CA C 62.095 0.038 1 216 58 58 CYS CB C 27.163 0.039 1 217 58 58 CYS N N 117.590 0.061 1 218 59 59 ILE H H 8.473 0.005 1 219 59 59 ILE C C 179.294 0.016 1 220 59 59 ILE CA C 64.126 0.053 1 221 59 59 ILE CB C 37.203 0.045 1 222 59 59 ILE N N 120.424 0.134 1 223 60 60 ALA H H 7.631 0.004 1 224 60 60 ALA C C 178.605 0.01 1 225 60 60 ALA CA C 55.443 0.037 1 226 60 60 ALA CB C 17.372 0.031 1 227 60 60 ALA N N 125.059 0.03 1 228 61 61 ALA H H 7.563 0.003 1 229 61 61 ALA C C 180.416 0.032 1 230 61 61 ALA CA C 55.141 . 1 231 61 61 ALA CB C 15.906 0.075 1 232 61 61 ALA N N 118.267 0.042 1 233 62 62 ALA H H 8.109 0.003 1 234 62 62 ALA C C 178.250 0.027 1 235 62 62 ALA CA C 55.628 . 1 236 62 62 ALA CB C 17.882 0.079 1 237 62 62 ALA N N 120.478 0.04 1 238 63 63 THR H H 8.467 0.005 1 239 63 63 THR CA C 66.364 0.114 1 240 63 63 THR CB C 68.535 0.022 1 241 63 63 THR N N 114.156 0.078 1 242 64 64 ARG H H 7.753 0.004 1 243 64 64 ARG C C 177.555 0.141 1 244 64 64 ARG CA C 58.527 0.021 1 245 64 64 ARG CB C 27.983 0.096 1 246 64 64 ARG N N 120.558 0.049 1 247 65 65 THR H H 7.256 0.006 1 248 65 65 THR CA C 65.438 0.069 1 249 65 65 THR CB C 68.386 0.102 1 250 65 65 THR N N 115.558 0.048 1 251 66 66 VAL H H 7.762 0.002 1 252 66 66 VAL C C 177.485 0.022 1 253 66 66 VAL CA C 65.608 . 1 254 66 66 VAL CB C 30.710 . 1 255 66 66 VAL N N 120.613 0.092 1 256 67 67 ALA H H 7.103 0.002 1 257 67 67 ALA C C 175.292 0.016 1 258 67 67 ALA CA C 52.132 0.055 1 259 67 67 ALA CB C 18.068 0.027 1 260 67 67 ALA N N 118.815 0.044 1 261 68 68 ASP H H 7.205 0.003 1 262 68 68 ASP C C 172.404 . 1 263 68 68 ASP CA C 50.004 . 1 264 68 68 ASP CB C 39.921 . 1 265 68 68 ASP N N 120.025 0.027 1 266 69 69 PRO C C 177.600 0.007 1 267 69 69 PRO CA C 63.984 . 1 268 69 69 PRO CB C 30.794 . 1 269 70 70 GLY H H 8.330 0.003 1 270 70 70 GLY C C 174.686 0.012 1 271 70 70 GLY CA C 44.607 0.017 1 272 70 70 GLY N N 113.474 0.049 1 273 71 71 SER H H 8.281 0.004 1 274 71 71 SER C C 173.760 0.088 1 275 71 71 SER CA C 58.298 0.178 1 276 71 71 SER CB C 65.559 0.021 1 277 71 71 SER N N 118.785 0.035 1 278 72 72 LEU H H 8.475 0.005 1 279 72 72 LEU CA C 53.117 0.079 1 280 72 72 LEU CB C 45.967 0.011 1 281 72 72 LEU N N 120.132 0.012 1 282 73 73 GLY H H 9.450 0.003 1 283 73 73 GLY C C 172.120 . 1 284 73 73 GLY CA C 45.138 0.08 1 285 73 73 GLY N N 106.229 0.089 1 286 74 74 ILE H H 8.954 0.004 1 287 74 74 ILE C C 174.910 . 1 288 74 74 ILE CA C 59.651 0.056 1 289 74 74 ILE CB C 41.198 0.054 1 290 74 74 ILE N N 119.238 0.037 1 291 75 75 VAL H H 8.956 0.005 1 292 75 75 VAL C C 174.784 . 1 293 75 75 VAL CA C 57.208 0.071 1 294 75 75 VAL CB C 32.638 0.044 1 295 75 75 VAL N N 118.293 0.068 1 296 76 76 LEU H H 8.303 0.005 1 297 76 76 LEU CA C 52.668 0.108 1 298 76 76 LEU CB C 44.303 0.033 1 299 76 76 LEU N N 120.924 0.054 1 300 77 77 GLY H H 7.340 0.003 1 301 77 77 GLY CA C 43.890 . 1 302 77 77 GLY N N 106.957 0.048 1 303 78 78 GLY H H 9.204 0.008 1 304 78 78 GLY CA C 47.789 . 1 305 78 78 GLY N N 113.823 0.07 1 306 80 80 GLY H H 7.126 0.005 1 307 80 80 GLY C C 173.788 0.016 1 308 80 80 GLY CA C 46.134 0.014 1 309 80 80 GLY N N 111.287 0.078 1 310 81 81 ASN H H 7.759 0.004 1 311 81 81 ASN C C 177.188 . 1 312 81 81 ASN CA C 55.320 0.009 1 313 81 81 ASN CB C 38.672 . 1 314 81 81 ASN N N 118.002 0.027 1 315 82 82 GLY H H 7.818 0.004 1 316 82 82 GLY C C 174.085 0.024 1 317 82 82 GLY CA C 47.488 0.035 1 318 82 82 GLY N N 107.087 0.032 1 319 83 83 GLU H H 8.303 0.003 1 320 83 83 GLU C C 177.737 0.026 1 321 83 83 GLU CA C 60.662 0.064 1 322 83 83 GLU CB C 26.407 0.019 1 323 83 83 GLU N N 120.129 0.051 1 324 84 84 GLN H H 7.797 0.004 1 325 84 84 GLN C C 177.450 0.001 1 326 84 84 GLN CA C 57.398 0.071 1 327 84 84 GLN CB C 25.638 0.101 1 328 84 84 GLN N N 117.331 0.047 1 329 85 85 ILE H H 7.540 0.006 1 330 85 85 ILE C C 177.139 0.0 1 331 85 85 ILE CA C 66.181 0.091 1 332 85 85 ILE CB C 36.930 0.118 1 333 85 85 ILE N N 123.135 0.004 1 334 86 86 ALA H H 7.638 0.005 1 335 86 86 ALA C C 178.792 0.028 1 336 86 86 ALA CA C 54.515 0.056 1 337 86 86 ALA CB C 17.318 0.061 1 338 86 86 ALA N N 116.474 0.069 1 339 87 87 ALA H H 7.797 0.004 1 340 87 87 ALA C C 178.042 . 1 341 87 87 ALA CA C 55.015 0.044 1 342 87 87 ALA CB C 18.418 0.028 1 343 87 87 ALA N N 117.104 0.05 1 344 88 88 ASN H H 8.281 0.003 1 345 88 88 ASN CA C 55.328 0.037 1 346 88 88 ASN CB C 39.826 0.044 1 347 88 88 ASN N N 111.519 0.052 1 348 89 89 LYS H H 7.703 0.003 1 349 89 89 LYS C C 177.984 0.028 1 350 89 89 LYS CA C 54.812 0.079 1 351 89 89 LYS CB C 29.942 0.094 1 352 89 89 LYS N N 118.453 0.042 1 353 90 90 VAL H H 7.613 0.006 1 354 90 90 VAL CA C 60.257 . 1 355 90 90 VAL CB C 30.675 . 1 356 90 90 VAL N N 125.148 0.031 1 357 91 91 PRO C C 177.987 0.011 1 358 91 91 PRO CA C 62.613 0.066 1 359 91 91 PRO CB C 30.530 0.029 1 360 92 92 GLY H H 9.405 0.005 1 361 92 92 GLY C C 174.324 0.046 1 362 92 92 GLY CA C 44.597 0.054 1 363 92 92 GLY N N 113.510 0.039 1 364 93 93 ALA H H 8.029 0.003 1 365 93 93 ALA C C 177.549 0.009 1 366 93 93 ALA CA C 51.949 0.049 1 367 93 93 ALA CB C 19.912 0.006 1 368 93 93 ALA N N 123.047 0.05 1 369 94 94 ARG H H 9.057 0.005 1 370 94 94 ARG C C 172.763 . 1 371 94 94 ARG CA C 55.449 0.067 1 372 94 94 ARG CB C 31.864 0.044 1 373 94 94 ARG N N 122.163 0.05 1 374 95 95 CYS H H 9.946 0.003 1 375 95 95 CYS C C 173.771 . 1 376 95 95 CYS CA C 55.136 0.061 1 377 95 95 CYS CB C 27.920 0.017 1 378 95 95 CYS N N 124.701 0.03 1 379 96 96 ALA H H 7.877 0.003 1 380 96 96 ALA C C 175.241 0.008 1 381 96 96 ALA CA C 50.043 0.051 1 382 96 96 ALA CB C 20.070 0.043 1 383 96 96 ALA N N 129.473 0.023 1 384 97 97 LEU H H 8.902 0.004 1 385 97 97 LEU C C 175.081 0.044 1 386 97 97 LEU CA C 54.037 0.034 1 387 97 97 LEU CB C 41.266 0.059 1 388 97 97 LEU N N 123.494 0.097 1 389 98 98 ALA H H 8.620 0.005 1 390 98 98 ALA C C 174.030 0.001 1 391 98 98 ALA CA C 49.853 0.091 1 392 98 98 ALA CB C 19.596 0.052 1 393 98 98 ALA N N 129.775 0.074 1 394 99 99 TRP H H 7.060 0.004 1 395 99 99 TRP C C 172.817 . 1 396 99 99 TRP CA C 52.905 0.014 1 397 99 99 TRP CB C 26.935 0.004 1 398 99 99 TRP N N 118.992 0.032 1 399 100 100 SER H H 6.980 0.002 1 400 100 100 SER CA C 54.518 0.001 1 401 100 100 SER CB C 65.096 0.009 1 402 100 100 SER N N 110.971 0.038 1 403 101 101 VAL H H 8.871 0.004 1 404 101 101 VAL C C 177.188 0.003 1 405 101 101 VAL CA C 66.682 0.129 1 406 101 101 VAL CB C 30.245 0.055 1 407 101 101 VAL N N 122.673 0.042 1 408 102 102 GLN H H 8.030 0.004 1 409 102 102 GLN C C 178.562 0.01 1 410 102 102 GLN CA C 58.675 0.0 1 411 102 102 GLN CB C 27.514 0.04 1 412 102 102 GLN N N 117.023 0.028 1 413 103 103 THR H H 7.405 0.002 1 414 103 103 THR C C 178.703 0.106 1 415 103 103 THR CA C 64.027 0.014 1 416 103 103 THR CB C 69.556 0.06 1 417 103 103 THR N N 107.467 0.033 1 418 104 104 ALA H H 7.594 0.003 1 419 104 104 ALA C C 177.569 0.029 1 420 104 104 ALA CA C 55.286 0.084 1 421 104 104 ALA CB C 19.068 0.173 1 422 104 104 ALA N N 126.000 0.037 1 423 105 105 ALA H H 7.796 0.003 1 424 105 105 ALA C C 180.822 0.013 1 425 105 105 ALA CA C 54.831 . 1 426 105 105 ALA CB C 17.837 0.061 1 427 105 105 ALA N N 118.080 0.053 1 428 106 106 LEU H H 8.303 0.003 1 429 106 106 LEU C C 178.916 0.011 1 430 106 106 LEU CA C 57.202 0.04 1 431 106 106 LEU CB C 41.400 0.027 1 432 106 106 LEU N N 117.451 0.051 1 433 107 107 ALA H H 7.446 0.003 1 434 107 107 ALA C C 181.255 0.003 1 435 107 107 ALA CA C 53.838 0.023 1 436 107 107 ALA CB C 16.743 0.043 1 437 107 107 ALA N N 120.139 0.109 1 438 108 108 ARG H H 6.997 0.002 1 439 108 108 ARG C C 177.938 0.023 1 440 108 108 ARG CA C 56.885 0.011 1 441 108 108 ARG CB C 27.849 0.025 1 442 108 108 ARG N N 116.297 0.056 1 443 109 109 GLU H H 8.554 0.004 1 444 109 109 GLU C C 177.782 0.123 1 445 109 109 GLU CA C 60.308 0.015 1 446 109 109 GLU CB C 30.535 0.039 1 447 109 109 GLU N N 117.823 0.031 1 448 110 110 HIS H H 9.042 0.004 1 449 110 110 HIS C C 176.353 0.017 1 450 110 110 HIS CA C 55.268 0.058 1 451 110 110 HIS CB C 32.171 0.035 1 452 110 110 HIS N N 112.328 0.057 1 453 111 111 ASN H H 6.686 0.003 1 454 111 111 ASN C C 173.355 0.016 1 455 111 111 ASN CA C 53.175 0.016 1 456 111 111 ASN CB C 39.032 0.015 1 457 111 111 ASN N N 111.093 0.037 1 458 112 112 ASN H H 7.454 0.005 1 459 112 112 ASN C C 175.361 0.019 1 460 112 112 ASN CA C 51.845 0.08 1 461 112 112 ASN CB C 34.375 0.023 1 462 112 112 ASN N N 117.324 0.034 1 463 113 113 ALA H H 8.248 0.005 1 464 113 113 ALA C C 177.927 0.012 1 465 113 113 ALA CA C 53.195 0.028 1 466 113 113 ALA CB C 17.280 0.014 1 467 113 113 ALA N N 122.402 0.05 1 468 114 114 GLN H H 9.065 0.006 1 469 114 114 GLN C C 175.306 . 1 470 114 114 GLN CA C 54.924 0.018 1 471 114 114 GLN CB C 27.683 0.011 1 472 114 114 GLN N N 123.606 0.046 1 473 115 115 LEU H H 7.989 0.005 1 474 115 115 LEU CA C 54.049 0.033 1 475 115 115 LEU CB C 47.366 0.006 1 476 115 115 LEU N N 113.324 0.063 1 477 116 116 ILE H H 7.089 0.006 1 478 116 116 ILE CA C 58.195 0.076 1 479 116 116 ILE CB C 40.356 0.062 1 480 116 116 ILE N N 110.175 0.036 1 481 117 117 GLY H H 8.508 0.002 1 482 117 117 GLY CA C 43.089 0.025 1 483 117 117 GLY N N 106.039 0.004 1 484 118 118 ILE H H 7.888 0.004 1 485 118 118 ILE C C 174.683 0.033 1 486 118 118 ILE CA C 59.872 0.079 1 487 118 118 ILE CB C 41.529 0.25 1 488 118 118 ILE N N 118.554 0.011 1 489 119 119 GLY H H 9.505 0.003 1 490 119 119 GLY C C 174.677 0.028 1 491 119 119 GLY CA C 45.727 0.071 1 492 119 119 GLY N N 114.093 0.062 1 493 120 120 GLY H H 9.309 0.004 1 494 120 120 GLY C C 175.519 0.012 1 495 120 120 GLY CA C 46.825 0.015 1 496 120 120 GLY N N 113.750 0.03 1 497 121 121 ARG H H 8.547 0.004 1 498 121 121 ARG C C 177.313 0.001 1 499 121 121 ARG CA C 56.232 0.021 1 500 121 121 ARG CB C 28.981 0.026 1 501 121 121 ARG N N 115.501 0.031 1 502 122 122 MET H H 7.752 0.003 1 503 122 122 MET C C 174.671 0.008 1 504 122 122 MET CA C 53.836 0.018 1 505 122 122 MET CB C 31.434 0.022 1 506 122 122 MET N N 114.816 0.03 1 507 123 123 HIS H H 6.783 0.003 1 508 123 123 HIS C C 176.071 0.013 1 509 123 123 HIS CA C 53.104 0.073 1 510 123 123 HIS CB C 33.084 0.004 1 511 123 123 HIS N N 113.489 0.046 1 512 124 124 THR H H 8.728 0.01 1 513 124 124 THR C C 175.709 0.009 1 514 124 124 THR CA C 60.956 0.002 1 515 124 124 THR CB C 70.209 0.022 1 516 124 124 THR N N 112.980 0.108 1 517 125 125 VAL H H 8.636 0.004 1 518 125 125 VAL C C 177.310 . 1 519 125 125 VAL CA C 67.019 . 1 520 125 125 VAL CB C 30.230 . 1 521 125 125 VAL N N 122.129 0.032 1 522 126 126 ALA H H 8.218 0.004 1 523 126 126 ALA C C 181.456 0.0 1 524 126 126 ALA CA C 54.959 0.026 1 525 126 126 ALA CB C 17.290 0.008 1 526 126 126 ALA N N 119.542 0.047 1 527 127 127 GLU H H 7.684 0.003 1 528 127 127 GLU C C 178.843 0.0 1 529 127 127 GLU CA C 58.323 0.011 1 530 127 127 GLU CB C 29.594 0.027 1 531 127 127 GLU N N 118.934 0.036 1 532 128 128 ALA H H 8.255 0.005 1 533 128 128 ALA C C 179.212 0.023 1 534 128 128 ALA CA C 54.851 0.009 1 535 128 128 ALA CB C 17.394 0.003 1 536 128 128 ALA N N 121.691 0.05 1 537 129 129 LEU H H 8.362 0.004 1 538 129 129 LEU C C 177.871 0.01 1 539 129 129 LEU CA C 57.384 0.009 1 540 129 129 LEU CB C 38.670 0.03 1 541 129 129 LEU N N 116.082 0.026 1 542 130 130 ALA H H 7.223 0.003 1 543 130 130 ALA C C 181.192 0.049 1 544 130 130 ALA CA C 54.504 0.071 1 545 130 130 ALA CB C 16.590 0.015 1 546 130 130 ALA N N 120.944 0.028 1 547 131 131 ILE H H 7.542 0.006 1 548 131 131 ILE CA C 66.241 0.02 1 549 131 131 ILE CB C 36.510 0.056 1 550 131 131 ILE N N 121.953 0.054 1 551 132 132 VAL H H 7.835 0.005 1 552 132 132 VAL C C 177.402 . 1 553 132 132 VAL CA C 67.184 0.015 1 554 132 132 VAL CB C 30.185 0.019 1 555 132 132 VAL N N 119.949 0.039 1 556 133 133 ASP H H 8.377 0.003 1 557 133 133 ASP C C 179.129 0.02 1 558 133 133 ASP CA C 57.196 0.036 1 559 133 133 ASP CB C 39.180 0.006 1 560 133 133 ASP N N 119.172 0.033 1 561 134 134 ALA H H 7.659 0.003 1 562 134 134 ALA C C 179.512 0.037 1 563 134 134 ALA CA C 54.540 0.036 1 564 134 134 ALA CB C 18.600 0.023 1 565 134 134 ALA N N 123.087 0.023 1 566 135 135 PHE H H 8.083 0.002 1 567 135 135 PHE C C 175.752 0.033 1 568 135 135 PHE CA C 60.068 0.084 1 569 135 135 PHE CB C 39.849 0.038 1 570 135 135 PHE N N 120.946 0.04 1 571 136 136 VAL H H 8.238 0.004 1 572 136 136 VAL C C 176.979 0.016 1 573 136 136 VAL CA C 63.162 0.096 1 574 136 136 VAL CB C 30.648 0.084 1 575 136 136 VAL N N 108.928 0.102 1 576 137 137 THR H H 7.243 0.003 1 577 137 137 THR C C 175.670 0.004 1 578 137 137 THR CA C 62.184 0.022 1 579 137 137 THR CB C 70.516 0.015 1 580 137 137 THR N N 106.876 0.065 1 581 138 138 THR H H 7.012 0.003 1 582 138 138 THR C C 172.578 . 1 583 138 138 THR CA C 62.041 . 1 584 138 138 THR CB C 69.693 . 1 585 138 138 THR N N 121.606 0.069 1 586 140 140 TRP H H 7.861 0.003 1 587 140 140 TRP C C 177.745 0.016 1 588 140 140 TRP CA C 55.294 0.061 1 589 140 140 TRP CB C 30.276 0.13 1 590 140 140 TRP N N 123.106 0.028 1 591 141 141 SER H H 7.460 0.006 1 592 141 141 SER C C 174.936 . 1 593 141 141 SER CA C 60.017 . 1 594 141 141 SER CB C 64.004 . 1 595 141 141 SER N N 123.530 0.061 1 596 146 146 HIS H H 6.377 0.003 1 597 146 146 HIS C C 179.327 0.019 1 598 146 146 HIS CA C 57.967 0.205 1 599 146 146 HIS CB C 30.765 0.027 1 600 146 146 HIS N N 116.164 0.041 1 601 147 147 GLN H H 8.878 0.006 1 602 147 147 GLN C C 177.279 0.028 1 603 147 147 GLN CA C 57.944 0.06 1 604 147 147 GLN CB C 27.930 0.019 1 605 147 147 GLN N N 122.652 0.027 1 606 148 148 ARG H H 8.453 0.004 1 607 148 148 ARG C C 178.815 0.001 1 608 148 148 ARG CA C 58.971 0.052 1 609 148 148 ARG CB C 28.777 0.001 1 610 148 148 ARG N N 118.779 0.174 1 611 149 149 ARG H H 7.000 0.003 1 612 149 149 ARG C C 177.646 . 1 613 149 149 ARG CA C 60.408 0.075 1 614 149 149 ARG CB C 28.436 0.304 1 615 149 149 ARG N N 116.619 0.047 1 616 150 150 ILE H H 7.509 0.003 1 617 150 150 ILE C C 178.727 0.011 1 618 150 150 ILE CA C 65.045 0.008 1 619 150 150 ILE CB C 36.919 0.009 1 620 150 150 ILE N N 119.914 0.04 1 621 151 151 ASP H H 8.708 0.004 1 622 151 151 ASP C C 179.830 0.014 1 623 151 151 ASP CA C 57.307 0.027 1 624 151 151 ASP CB C 39.152 0.022 1 625 151 151 ASP N N 122.714 0.053 1 626 152 152 ILE H H 7.889 0.007 1 627 152 152 ILE C C 179.245 0.012 1 628 152 152 ILE CA C 64.844 0.024 1 629 152 152 ILE CB C 38.093 0.013 1 630 152 152 ILE N N 122.829 0.138 1 631 153 153 LEU H H 7.548 0.003 1 632 153 153 LEU C C 178.104 0.02 1 633 153 153 LEU CA C 57.456 0.04 1 634 153 153 LEU CB C 41.113 0.001 1 635 153 153 LEU N N 121.059 0.032 1 636 154 154 ALA H H 8.584 0.005 1 637 154 154 ALA C C 180.905 0.012 1 638 154 154 ALA CA C 54.675 0.001 1 639 154 154 ALA CB C 17.604 0.027 1 640 154 154 ALA N N 122.189 0.033 1 641 155 155 GLU H H 7.927 0.003 1 642 155 155 GLU C C 178.750 0.003 1 643 155 155 GLU CA C 58.204 0.007 1 644 155 155 GLU CB C 27.913 0.022 1 645 155 155 GLU N N 119.823 0.021 1 646 156 156 TYR H H 7.887 0.004 1 647 156 156 TYR C C 177.977 0.025 1 648 156 156 TYR CA C 61.486 0.012 1 649 156 156 TYR CB C 36.874 0.035 1 650 156 156 TYR N N 121.386 0.053 1 651 157 157 GLU H H 8.468 0.006 1 652 157 157 GLU C C 176.785 0.01 1 653 157 157 GLU CA C 59.450 0.013 1 654 157 157 GLU CB C 29.661 0.003 1 655 157 157 GLU N N 119.136 0.046 1 656 158 158 ARG H H 7.334 0.003 1 657 158 158 ARG C C 178.160 0.016 1 658 158 158 ARG CA C 58.482 0.015 1 659 158 158 ARG CB C 30.579 0.035 1 660 158 158 ARG N N 115.897 0.043 1 661 159 159 THR H H 7.723 0.003 1 662 159 159 THR C C 175.614 0.01 1 663 159 159 THR CA C 61.886 0.053 1 664 159 159 THR CB C 70.881 0.033 1 665 159 159 THR N N 107.010 0.053 1 666 160 160 HIS H H 8.917 0.004 1 667 160 160 HIS C C 172.863 0.021 1 668 160 160 HIS CA C 57.250 0.008 1 669 160 160 HIS CB C 25.514 0.006 1 670 160 160 HIS N N 117.872 0.049 1 671 161 161 GLU H H 7.859 0.004 1 672 161 161 GLU C C 175.473 0.018 1 673 161 161 GLU CA C 54.288 0.004 1 674 161 161 GLU CB C 28.479 0.02 1 675 161 161 GLU N N 119.303 0.034 1 676 162 162 ALA H H 8.770 0.003 1 677 162 162 ALA C C 175.340 . 1 678 162 162 ALA CA C 50.549 . 1 679 162 162 ALA CB C 16.362 . 1 680 162 162 ALA N N 131.035 0.035 1 681 164 164 PRO C C 176.467 0.006 1 682 164 164 PRO CA C 62.217 0.014 1 683 164 164 PRO CB C 31.082 0.02 1 684 165 165 VAL H H 8.175 0.004 1 685 165 165 VAL C C 174.762 . 1 686 165 165 VAL CA C 59.156 . 1 687 165 165 VAL CB C 31.447 . 1 688 165 165 VAL N N 121.376 0.042 1 689 166 166 PRO C C 177.453 0.005 1 690 166 166 PRO CA C 63.245 0.036 1 691 166 166 PRO CB C 31.328 0.007 1 692 167 167 GLY H H 8.512 0.003 1 693 167 167 GLY C C 173.655 0.044 1 694 167 167 GLY CA C 44.668 0.017 1 695 167 167 GLY N N 111.041 0.041 1 696 168 168 ALA H H 7.897 0.004 1 697 168 168 ALA C C 184.457 . 1 698 168 168 ALA CA C 50.168 . 1 699 168 168 ALA CB C 17.426 . 1 700 168 168 ALA N N 124.630 0.055 1 701 169 169 PRO C C 175.778 0.007 1 702 169 169 PRO CA C 62.804 0.017 1 703 169 169 PRO CB C 30.987 0.014 1 704 170 170 ALA H H 7.877 0.003 1 705 170 170 ALA C C 182.650 . 1 706 170 170 ALA CA C 53.417 . 1 707 170 170 ALA CB C 19.290 . 1 708 170 170 ALA N N 130.264 0.033 1 stop_ save_