data_19243 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shifts of isolated Domain 1 from E. coli HisJ ; _BMRB_accession_number 19243 _BMRB_flat_file_name bmr19243.str _Entry_type original _Submission_date 2013-05-15 _Accession_date 2013-05-15 _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 Chu Byron 'C. H.' . 2 Vogel Hans J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 139 "13C chemical shifts" 425 "15N chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-12-09 update BMRB 'update entry citation' 2013-09-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19242 'E. coli apo-HisJ' 19244 'Backbone chemical shifts of isolated Domain 2 from E. coli HisJ' 19245 'Backbone chemical shifts from E. coli HisJ complexed with Histidine' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24036119 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chu Byron C.H. . 2 Dewolf Timothy . . 3 Vogel Hans J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31409 _Page_last 31422 _Year 2013 _Details . loop_ _Keyword 'E. coli' HisJ histidine 'Periplasmic binding protein' 'structural domain' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Domain 1 from E. coli HisJ' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Domain 1 from E. coli HisJ' $D1 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_D1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common D1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; GGMAIPQNIRIGTDPTYAPF ESKNSQGELVGFDIDLAKEL CKRINTQCTFVENPLDALIP SLKAKKIDAIMSSLSITEKR QQEIAFTDKLYAAGGGGSGL FGVGTGMGLRKEDNELREAL NKAFAEMRADGTYEKLAKKY FDFDVYGG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLY 3 MET 4 ALA 5 ILE 6 PRO 7 GLN 8 ASN 9 ILE 10 ARG 11 ILE 12 GLY 13 THR 14 ASP 15 PRO 16 THR 17 TYR 18 ALA 19 PRO 20 PHE 21 GLU 22 SER 23 LYS 24 ASN 25 SER 26 GLN 27 GLY 28 GLU 29 LEU 30 VAL 31 GLY 32 PHE 33 ASP 34 ILE 35 ASP 36 LEU 37 ALA 38 LYS 39 GLU 40 LEU 41 CYS 42 LYS 43 ARG 44 ILE 45 ASN 46 THR 47 GLN 48 CYS 49 THR 50 PHE 51 VAL 52 GLU 53 ASN 54 PRO 55 LEU 56 ASP 57 ALA 58 LEU 59 ILE 60 PRO 61 SER 62 LEU 63 LYS 64 ALA 65 LYS 66 LYS 67 ILE 68 ASP 69 ALA 70 ILE 71 MET 72 SER 73 SER 74 LEU 75 SER 76 ILE 77 THR 78 GLU 79 LYS 80 ARG 81 GLN 82 GLN 83 GLU 84 ILE 85 ALA 86 PHE 87 THR 88 ASP 89 LYS 90 LEU 91 TYR 92 ALA 93 ALA 94 GLY 95 GLY 96 GLY 97 GLY 98 SER 99 GLY 100 LEU 101 PHE 102 GLY 103 VAL 104 GLY 105 THR 106 GLY 107 MET 108 GLY 109 LEU 110 ARG 111 LYS 112 GLU 113 ASP 114 ASN 115 GLU 116 LEU 117 ARG 118 GLU 119 ALA 120 LEU 121 ASN 122 LYS 123 ALA 124 PHE 125 ALA 126 GLU 127 MET 128 ARG 129 ALA 130 ASP 131 GLY 132 THR 133 TYR 134 GLU 135 LYS 136 LEU 137 ALA 138 LYS 139 LYS 140 TYR 141 PHE 142 ASP 143 PHE 144 ASP 145 VAL 146 TYR 147 GLY 148 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value EMBL CAJ55342 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 60.81 164 97.78 98.89 9.44e-56 EMBL CAJ55343 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 60.81 164 97.78 98.89 9.14e-56 EMBL CAJ55344 "periplasmic histidine-binding protein, partial [Salmonella enterica subsp. enterica serovar Heidelberg]" 60.81 164 97.78 98.89 9.44e-56 GB AEW46917 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Abortusequi]" 60.81 154 97.78 98.89 1.38e-55 GB AEW46918 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Abortusequi]" 60.81 144 97.78 98.89 1.43e-55 GB AEW46919 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Abortusequi]" 60.81 147 97.78 98.89 1.49e-55 GB AHA92022 "histidine transport protein, partial [Salmonella enterica]" 60.81 160 97.78 98.89 1.32e-55 GB AHS49988 "histidine ABC transporter substrate-binding protein HisJ, partial [Salmonella enterica subsp. enterica serovar Enteritidis str." 60.81 220 97.78 98.89 1.01e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $D1 'E. coli' 562 Bacteria . Escherichia coli K12 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 $D1 'recombinant technology' . Escherichia coli BL21 pET-15 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 $D1 1 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' DSS 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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 . M pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '1H chemical shifts were referenced to the methyl signal of DSS, and 15N and 13C chemical shifts were indirectly referenced to DSS (0 ppm for 1H).' 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_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '2D 1H-15N HSQC' 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 'Domain 1 from E. coli HisJ' _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 GLY C C 174.1000 . 1 2 2 2 GLY CA C 44.7100 . 1 3 3 3 MET H H 8.4430 . 1 4 3 3 MET C C 176.0000 . 1 5 3 3 MET CA C 55.0800 . 1 6 3 3 MET CB C 32.4300 . 1 7 3 3 MET N N 121.2000 . 1 8 4 4 ALA H H 8.3810 . 1 9 4 4 ALA C C 177.3000 . 1 10 4 4 ALA CA C 52.1500 . 1 11 4 4 ALA CB C 18.3300 . 1 12 4 4 ALA N N 125.7000 . 1 13 5 5 ILE H H 7.8680 . 1 14 5 5 ILE C C 174.3000 . 1 15 5 5 ILE CA C 57.7100 . 1 16 5 5 ILE CB C 37.2700 . 1 17 5 5 ILE N N 121.3000 . 1 18 6 6 PRO C C 176.1000 . 1 19 6 6 PRO CA C 62.2100 . 1 20 6 6 PRO CB C 31.6600 . 1 21 7 7 GLN H H 8.3780 . 1 22 7 7 GLN C C 175.6000 . 1 23 7 7 GLN CA C 57.2200 . 1 24 7 7 GLN CB C 28.4800 . 1 25 7 7 GLN N N 119.2000 . 1 26 8 8 ASN H H 7.4740 . 1 27 8 8 ASN C C 173.6000 . 1 28 8 8 ASN CA C 51.7500 . 1 29 8 8 ASN CB C 40.5800 . 1 30 8 8 ASN N N 116.3000 . 1 31 9 9 ILE H H 8.4210 . 1 32 9 9 ILE C C 174.7000 . 1 33 9 9 ILE CA C 59.5200 . 1 34 9 9 ILE CB C 39.8000 . 1 35 9 9 ILE N N 121.0000 . 1 36 10 10 ARG H H 9.1000 . 1 37 10 10 ARG C C 175.9000 . 1 38 10 10 ARG CA C 53.9400 . 1 39 10 10 ARG CB C 30.7000 . 1 40 10 10 ARG N N 126.5000 . 1 41 11 11 ILE H H 9.2850 . 1 42 11 11 ILE C C 175.6000 . 1 43 11 11 ILE CA C 59.5000 . 1 44 11 11 ILE CB C 37.4700 . 1 45 11 11 ILE N N 127.4000 . 1 46 12 12 GLY H H 9.3560 . 1 47 12 12 GLY C C 171.8000 . 1 48 12 12 GLY CA C 44.5000 . 1 49 12 12 GLY N N 114.6000 . 1 50 13 13 THR H H 8.6040 . 1 51 13 13 THR C C 181.6000 . 1 52 13 13 THR CA C 61.5300 . 1 53 13 13 THR CB C 70.0400 . 1 54 13 13 THR N N 120.5000 . 1 55 14 14 ASP H H 8.1940 . 1 56 14 14 ASP C C 177.4000 . 1 57 14 14 ASP CA C 49.7500 . 1 58 14 14 ASP CB C 40.6100 . 1 59 14 14 ASP N N 126.9000 . 1 60 15 15 PRO C C 175.4000 . 1 61 15 15 PRO CA C 61.8400 . 1 62 15 15 PRO CB C 27.8600 . 1 63 16 16 THR H H 8.6990 . 1 64 16 16 THR C C 174.0000 . 1 65 16 16 THR CA C 59.6100 . 1 66 16 16 THR CB C 68.6400 . 1 67 16 16 THR N N 116.2000 . 1 68 17 17 TYR H H 8.9380 . 1 69 17 17 TYR C C 175.2000 . 1 70 17 17 TYR CA C 53.6500 . 1 71 17 17 TYR CB C 38.7100 . 1 72 17 17 TYR N N 125.8000 . 1 73 18 18 ALA H H 9.0470 . 1 74 18 18 ALA C C 176.4000 . 1 75 18 18 ALA CA C 51.5900 . 1 76 18 18 ALA CB C 16.1500 . 1 77 18 18 ALA N N 131.4000 . 1 78 19 19 PRO C C 173.2000 . 1 79 19 19 PRO CA C 63.2400 . 1 80 19 19 PRO CB C 31.6700 . 1 81 20 20 PHE H H 8.2120 . 1 82 20 20 PHE C C 176.6000 . 1 83 20 20 PHE CA C 62.6300 . 1 84 20 20 PHE CB C 37.7100 . 1 85 20 20 PHE N N 125.7000 . 1 86 21 21 GLU H H 7.6350 . 1 87 21 21 GLU C C 173.8000 . 1 88 21 21 GLU CA C 54.6000 . 1 89 21 21 GLU CB C 29.0500 . 1 90 21 21 GLU N N 111.2000 . 1 91 22 22 SER H H 8.7530 . 1 92 22 22 SER C C 171.4000 . 1 93 22 22 SER CA C 57.4000 . 1 94 22 22 SER CB C 62.9100 . 1 95 22 22 SER N N 116.9000 . 1 96 23 23 LYS H H 8.2310 . 1 97 23 23 LYS C C 177.6000 . 1 98 23 23 LYS CA C 53.7700 . 1 99 23 23 LYS CB C 33.4800 . 1 100 23 23 LYS N N 117.4000 . 1 101 24 24 ASN H H 8.6120 . 1 102 24 24 ASN C C 178.0000 . 1 103 24 24 ASN CA C 50.6100 . 1 104 24 24 ASN CB C 38.2000 . 1 105 24 24 ASN N N 122.5000 . 1 106 25 25 SER C C 175.4000 . 1 107 25 25 SER CA C 60.9500 . 1 108 25 25 SER CB C 62.3700 . 1 109 26 26 GLN H H 7.5250 . 1 110 26 26 GLN C C 176.2000 . 1 111 26 26 GLN CA C 55.2500 . 1 112 26 26 GLN CB C 28.2800 . 1 113 26 26 GLN N N 119.3000 . 1 114 27 27 GLY H H 8.1620 . 1 115 27 27 GLY C C 173.7000 . 1 116 27 27 GLY CA C 45.0800 . 1 117 27 27 GLY N N 108.8000 . 1 118 28 28 GLU H H 7.8390 . 1 119 28 28 GLU C C 175.8000 . 1 120 28 28 GLU CA C 54.4700 . 1 121 28 28 GLU CB C 29.7500 . 1 122 28 28 GLU N N 121.2000 . 1 123 29 29 LEU H H 8.3010 . 1 124 29 29 LEU C C 176.4000 . 1 125 29 29 LEU CA C 54.3700 . 1 126 29 29 LEU CB C 41.1000 . 1 127 29 29 LEU N N 123.5000 . 1 128 30 30 VAL H H 8.8740 . 1 129 30 30 VAL C C 175.3000 . 1 130 30 30 VAL CA C 58.3500 . 1 131 30 30 VAL CB C 36.1700 . 1 132 30 30 VAL N N 118.0000 . 1 133 31 31 GLY H H 8.5890 . 1 134 31 31 GLY C C 174.1000 . 1 135 31 31 GLY CA C 43.7900 . 1 136 31 31 GLY N N 109.7000 . 1 137 32 32 PHE H H 8.2420 . 1 138 32 32 PHE C C 177.7000 . 1 139 32 32 PHE CA C 59.5400 . 1 140 32 32 PHE CB C 39.2000 . 1 141 32 32 PHE N N 120.0000 . 1 142 33 33 ASP H H 9.0510 . 1 143 33 33 ASP C C 179.0000 . 1 144 33 33 ASP CA C 56.1000 . 1 145 33 33 ASP CB C 38.5400 . 1 146 33 33 ASP N N 116.4000 . 1 147 34 34 ILE H H 6.5170 . 1 148 34 34 ILE C C 177.9000 . 1 149 34 34 ILE CA C 60.9500 . 1 150 34 34 ILE CB C 33.7000 . 1 151 34 34 ILE N N 118.7000 . 1 152 35 35 ASP H H 8.5180 . 1 153 35 35 ASP C C 180.3000 . 1 154 35 35 ASP CA C 57.1100 . 1 155 35 35 ASP CB C 40.3900 . 1 156 35 35 ASP N N 121.1000 . 1 157 36 36 LEU H H 8.5480 . 1 158 36 36 LEU C C 178.4000 . 1 159 36 36 LEU CA C 57.7300 . 1 160 36 36 LEU CB C 42.2200 . 1 161 36 36 LEU N N 120.6000 . 1 162 37 37 ALA H H 8.3250 . 1 163 37 37 ALA C C 178.5000 . 1 164 37 37 ALA CA C 55.2200 . 1 165 37 37 ALA CB C 17.3800 . 1 166 37 37 ALA N N 120.2000 . 1 167 38 38 LYS H H 8.7740 . 1 168 38 38 LYS C C 180.1000 . 1 169 38 38 LYS CA C 60.5500 . 1 170 38 38 LYS CB C 31.8600 . 1 171 38 38 LYS N N 116.4000 . 1 172 39 39 GLU H H 7.7190 . 1 173 39 39 GLU C C 178.3000 . 1 174 39 39 GLU CA C 58.4400 . 1 175 39 39 GLU CB C 28.0500 . 1 176 39 39 GLU N N 121.5000 . 1 177 40 40 LEU H H 8.5400 . 1 178 40 40 LEU C C 178.6000 . 1 179 40 40 LEU CA C 58.4700 . 1 180 40 40 LEU CB C 40.3000 . 1 181 40 40 LEU N N 121.4000 . 1 182 41 41 CYS H H 8.6070 . 1 183 41 41 CYS C C 175.8000 . 1 184 41 41 CYS CA C 62.3800 . 1 185 41 41 CYS CB C 46.9500 . 1 186 41 41 CYS N N 115.7000 . 1 187 42 42 LYS H H 7.5090 . 1 188 42 42 LYS C C 180.8000 . 1 189 42 42 LYS CA C 58.8700 . 1 190 42 42 LYS CB C 31.4300 . 1 191 42 42 LYS N N 119.3000 . 1 192 43 43 ARG H H 8.0500 . 1 193 43 43 ARG C C 178.7000 . 1 194 43 43 ARG CA C 58.7100 . 1 195 43 43 ARG CB C 29.9300 . 1 196 43 43 ARG N N 119.5000 . 1 197 44 44 ILE H H 7.7560 . 1 198 44 44 ILE C C 175.0000 . 1 199 44 44 ILE CA C 60.9700 . 1 200 44 44 ILE CB C 36.6300 . 1 201 44 44 ILE N N 111.8000 . 1 202 45 45 ASN H H 7.7540 . 1 203 45 45 ASN C C 173.6000 . 1 204 45 45 ASN CA C 53.6700 . 1 205 45 45 ASN CB C 36.6400 . 1 206 45 45 ASN N N 118.8000 . 1 207 46 46 THR H H 7.9250 . 1 208 46 46 THR C C 173.0000 . 1 209 46 46 THR CA C 60.0400 . 1 210 46 46 THR CB C 70.5200 . 1 211 46 46 THR N N 112.8000 . 1 212 47 47 GLN H H 8.0370 . 1 213 47 47 GLN C C 175.4000 . 1 214 47 47 GLN CA C 54.5800 . 1 215 47 47 GLN CB C 28.6800 . 1 216 47 47 GLN N N 123.6000 . 1 217 48 48 CYS H H 8.8810 . 1 218 48 48 CYS C C 173.8000 . 1 219 48 48 CYS CA C 53.2000 . 1 220 48 48 CYS CB C 47.4400 . 1 221 48 48 CYS N N 123.8000 . 1 222 49 49 THR H H 8.3270 . 1 223 49 49 THR C C 172.7000 . 1 224 49 49 THR CA C 60.2100 . 1 225 49 49 THR CB C 70.9900 . 1 226 49 49 THR N N 118.6000 . 1 227 50 50 PHE H H 8.9770 . 1 228 50 50 PHE C C 175.8000 . 1 229 50 50 PHE CA C 57.3600 . 1 230 50 50 PHE CB C 40.8600 . 1 231 50 50 PHE N N 123.6000 . 1 232 51 51 VAL H H 9.2560 . 1 233 51 51 VAL C C 174.7000 . 1 234 51 51 VAL CA C 60.6300 . 1 235 51 51 VAL CB C 33.7700 . 1 236 51 51 VAL N N 126.0000 . 1 237 52 52 GLU H H 8.6170 . 1 238 52 52 GLU C C 176.8000 . 1 239 52 52 GLU CA C 54.4500 . 1 240 52 52 GLU CB C 29.4700 . 1 241 52 52 GLU N N 126.8000 . 1 242 53 53 ASN H H 8.9070 . 1 243 53 53 ASN C C 170.7000 . 1 244 53 53 ASN CA C 51.2600 . 1 245 53 53 ASN CB C 44.0000 . 1 246 53 53 ASN N N 127.0000 . 1 247 54 54 PRO C C 178.6000 . 1 248 54 54 PRO CA C 61.6400 . 1 249 54 54 PRO CB C 31.4900 . 1 250 55 55 LEU H H 9.0570 . 1 251 55 55 LEU C C 179.6000 . 1 252 55 55 LEU CA C 58.1500 . 1 253 55 55 LEU CB C 41.4200 . 1 254 55 55 LEU N N 124.1000 . 1 255 56 56 ASP H H 8.6460 . 1 256 56 56 ASP C C 176.5000 . 1 257 56 56 ASP CA C 56.1300 . 1 258 56 56 ASP CB C 39.6500 . 1 259 56 56 ASP N N 115.4000 . 1 260 57 57 ALA H H 8.0710 . 1 261 57 57 ALA C C 179.9000 . 1 262 57 57 ALA CA C 51.4700 . 1 263 57 57 ALA CB C 19.1900 . 1 264 57 57 ALA N N 120.4000 . 1 265 58 58 LEU H H 7.7620 . 1 266 58 58 LEU C C 177.8000 . 1 267 58 58 LEU CA C 58.9400 . 1 268 58 58 LEU CB C 40.1700 . 1 269 58 58 LEU N N 122.2000 . 1 270 59 59 ILE H H 9.0870 . 1 271 59 59 ILE C C 176.3000 . 1 272 59 59 ILE CA C 68.1300 . 1 273 59 59 ILE CB C 33.9500 . 1 274 59 59 ILE N N 119.6000 . 1 275 60 60 PRO C C 180.1000 . 1 276 60 60 PRO CA C 65.9100 . 1 277 60 60 PRO CB C 30.0000 . 1 278 61 61 SER H H 7.8510 . 1 279 61 61 SER C C 175.5000 . 1 280 61 61 SER CA C 62.1700 . 1 281 61 61 SER CB C 63.1300 . 1 282 61 61 SER N N 114.8000 . 1 283 62 62 LEU H H 8.2860 . 1 284 62 62 LEU C C 181.0000 . 1 285 62 62 LEU CA C 57.4000 . 1 286 62 62 LEU CB C 41.8200 . 1 287 62 62 LEU N N 126.2000 . 1 288 63 63 LYS H H 8.4700 . 1 289 63 63 LYS C C 178.0000 . 1 290 63 63 LYS CA C 59.5000 . 1 291 63 63 LYS CB C 30.7700 . 1 292 63 63 LYS N N 121.0000 . 1 293 64 64 ALA H H 7.6810 . 1 294 64 64 ALA C C 176.2000 . 1 295 64 64 ALA CA C 51.6900 . 1 296 64 64 ALA CB C 18.1600 . 1 297 64 64 ALA N N 118.7000 . 1 298 65 65 LYS H H 7.7500 . 1 299 65 65 LYS C C 176.0000 . 1 300 65 65 LYS CA C 57.8000 . 1 301 65 65 LYS CB C 27.7400 . 1 302 65 65 LYS N N 112.2000 . 1 303 66 66 LYS H H 8.4160 . 1 304 66 66 LYS C C 176.6000 . 1 305 66 66 LYS CA C 57.2400 . 1 306 66 66 LYS CB C 32.1800 . 1 307 66 66 LYS N N 118.3000 . 1 308 67 67 ILE H H 7.0330 . 1 309 67 67 ILE C C 174.0000 . 1 310 67 67 ILE CA C 59.0600 . 1 311 67 67 ILE CB C 40.4700 . 1 312 67 67 ILE N N 107.5000 . 1 313 68 68 ASP H H 9.7340 . 1 314 68 68 ASP C C 172.2000 . 1 315 68 68 ASP CA C 55.5500 . 1 316 68 68 ASP CB C 44.2300 . 1 317 68 68 ASP N N 119.0000 . 1 318 69 69 ALA H H 7.6610 . 1 319 69 69 ALA C C 175.9000 . 1 320 69 69 ALA CA C 50.1400 . 1 321 69 69 ALA CB C 22.0200 . 1 322 69 69 ALA N N 117.4000 . 1 323 70 70 ILE H H 9.3900 . 1 324 70 70 ILE C C 174.6000 . 1 325 70 70 ILE CA C 60.0500 . 1 326 70 70 ILE CB C 41.1600 . 1 327 70 70 ILE N N 120.4000 . 1 328 71 71 MET H H 8.4510 . 1 329 71 71 MET C C 172.5000 . 1 330 71 71 MET CA C 53.0500 . 1 331 71 71 MET CB C 33.9800 . 1 332 71 71 MET N N 128.4000 . 1 333 72 72 SER H H 8.6800 . 1 334 72 72 SER C C 173.0000 . 1 335 72 72 SER CA C 57.4700 . 1 336 72 72 SER CB C 64.7000 . 1 337 72 72 SER N N 122.3000 . 1 338 73 73 SER H H 8.5030 . 1 339 73 73 SER C C 174.9000 . 1 340 73 73 SER CA C 58.7700 . 1 341 73 73 SER CB C 62.9900 . 1 342 73 73 SER N N 120.1000 . 1 343 74 74 LEU H H 8.7160 . 1 344 74 74 LEU C C 175.4000 . 1 345 74 74 LEU CA C 54.4300 . 1 346 74 74 LEU CB C 42.2900 . 1 347 74 74 LEU N N 121.0000 . 1 348 75 75 SER H H 8.1060 . 1 349 75 75 SER C C 174.2000 . 1 350 75 75 SER CA C 58.8600 . 1 351 75 75 SER CB C 63.0600 . 1 352 75 75 SER N N 122.0000 . 1 353 76 76 ILE H H 8.2260 . 1 354 76 76 ILE C C 175.3000 . 1 355 76 76 ILE CA C 61.4200 . 1 356 76 76 ILE CB C 35.4900 . 1 357 76 76 ILE N N 125.3000 . 1 358 77 77 THR H H 6.4800 . 1 359 77 77 THR C C 174.6000 . 1 360 77 77 THR CA C 57.7600 . 1 361 77 77 THR CB C 71.2800 . 1 362 77 77 THR N N 116.1000 . 1 363 78 78 GLU C C 179.5000 . 1 364 78 78 GLU CA C 58.9400 . 1 365 78 78 GLU CB C 28.6000 . 1 366 79 79 LYS H H 8.3890 . 1 367 79 79 LYS C C 180.5000 . 1 368 79 79 LYS CA C 58.8000 . 1 369 79 79 LYS CB C 31.5500 . 1 370 79 79 LYS N N 118.5000 . 1 371 80 80 ARG H H 7.6410 . 1 372 80 80 ARG C C 179.0000 . 1 373 80 80 ARG CA C 59.5300 . 1 374 80 80 ARG CB C 30.2800 . 1 375 80 80 ARG N N 118.4000 . 1 376 81 81 GLN H H 8.3810 . 1 377 81 81 GLN C C 176.6000 . 1 378 81 81 GLN CA C 57.5600 . 1 379 81 81 GLN CB C 28.7600 . 1 380 81 81 GLN N N 118.9000 . 1 381 82 82 GLN H H 7.3000 . 1 382 82 82 GLN C C 177.3000 . 1 383 82 82 GLN CA C 57.2700 . 1 384 82 82 GLN CB C 27.9700 . 1 385 82 82 GLN N N 115.3000 . 1 386 83 83 GLU H H 7.6090 . 1 387 83 83 GLU C C 176.4000 . 1 388 83 83 GLU CA C 57.0100 . 1 389 83 83 GLU CB C 33.0400 . 1 390 83 83 GLU N N 115.8000 . 1 391 84 84 ILE H H 8.2900 . 1 392 84 84 ILE C C 172.6000 . 1 393 84 84 ILE CA C 59.3600 . 1 394 84 84 ILE CB C 40.7800 . 1 395 84 84 ILE N N 115.2000 . 1 396 85 85 ALA H H 8.6780 . 1 397 85 85 ALA C C 175.0000 . 1 398 85 85 ALA CA C 49.1600 . 1 399 85 85 ALA CB C 22.2900 . 1 400 85 85 ALA N N 120.6000 . 1 401 86 86 PHE H H 8.2920 . 1 402 86 86 PHE C C 178.8000 . 1 403 86 86 PHE CA C 55.8800 . 1 404 86 86 PHE CB C 44.1800 . 1 405 86 86 PHE N N 115.5000 . 1 406 87 87 THR H H 7.8910 . 1 407 87 87 THR C C 174.7000 . 1 408 87 87 THR CA C 61.9700 . 1 409 87 87 THR CB C 72.8300 . 1 410 87 87 THR N N 108.2000 . 1 411 88 88 ASP H H 8.8400 . 1 412 88 88 ASP C C 174.3000 . 1 413 88 88 ASP CA C 55.0600 . 1 414 88 88 ASP CB C 40.8100 . 1 415 88 88 ASP N N 118.6000 . 1 416 89 89 LYS H H 7.7590 . 1 417 89 89 LYS C C 176.2000 . 1 418 89 89 LYS CA C 55.8400 . 1 419 89 89 LYS CB C 31.5500 . 1 420 89 89 LYS N N 118.2000 . 1 421 90 90 LEU H H 8.7130 . 1 422 90 90 LEU C C 177.9000 . 1 423 90 90 LEU CA C 54.4100 . 1 424 90 90 LEU CB C 41.7200 . 1 425 90 90 LEU N N 123.7000 . 1 426 91 91 TYR H H 6.8570 . 1 427 91 91 TYR C C 173.0000 . 1 428 91 91 TYR CA C 56.1800 . 1 429 91 91 TYR CB C 37.3600 . 1 430 91 91 TYR N N 110.1000 . 1 431 92 92 ALA H H 8.4030 . 1 432 92 92 ALA C C 176.2000 . 1 433 92 92 ALA CA C 51.8900 . 1 434 92 92 ALA CB C 19.0200 . 1 435 92 92 ALA N N 123.7000 . 1 436 93 93 ALA H H 8.3080 . 1 437 93 93 ALA C C 177.7000 . 1 438 93 93 ALA CA C 51.9600 . 1 439 93 93 ALA CB C 18.8600 . 1 440 93 93 ALA N N 124.0000 . 1 441 94 94 GLY H H 8.4980 . 1 442 94 94 GLY C C 175.1000 . 1 443 94 94 GLY CA C 45.2200 . 1 444 94 94 GLY N N 108.7000 . 1 445 95 95 GLY H H 8.3960 . 1 446 95 95 GLY C C 174.9000 . 1 447 95 95 GLY CA C 45.1900 . 1 448 95 95 GLY N N 109.3000 . 1 449 96 96 GLY H H 8.2160 . 1 450 96 96 GLY C C 174.9000 . 1 451 96 96 GLY CA C 45.0500 . 1 452 96 96 GLY N N 108.9000 . 1 453 97 97 GLY H H 8.1800 . 1 454 97 97 GLY C C 174.5000 . 1 455 97 97 GLY CA C 44.8600 . 1 456 97 97 GLY N N 109.5000 . 1 457 98 98 SER H H 8.2080 . 1 458 98 98 SER C C 175.3000 . 1 459 98 98 SER CA C 58.3800 . 1 460 98 98 SER CB C 63.6600 . 1 461 98 98 SER N N 116.1000 . 1 462 99 99 GLY H H 8.3360 . 1 463 99 99 GLY C C 174.2000 . 1 464 99 99 GLY CA C 45.0400 . 1 465 99 99 GLY N N 111.3000 . 1 466 100 100 LEU H H 7.8470 . 1 467 100 100 LEU C C 177.0000 . 1 468 100 100 LEU CA C 54.5100 . 1 469 100 100 LEU CB C 41.1800 . 1 470 100 100 LEU N N 121.9000 . 1 471 101 101 PHE H H 8.0870 . 1 472 101 101 PHE C C 176.5000 . 1 473 101 101 PHE CA C 57.5100 . 1 474 101 101 PHE CB C 38.7000 . 1 475 101 101 PHE N N 120.4000 . 1 476 102 102 GLY H H 8.1740 . 1 477 102 102 GLY C C 173.9000 . 1 478 102 102 GLY CA C 44.9900 . 1 479 102 102 GLY N N 111.0000 . 1 480 103 103 VAL H H 7.8460 . 1 481 103 103 VAL C C 176.0000 . 1 482 103 103 VAL CA C 61.5300 . 1 483 103 103 VAL CB C 31.8900 . 1 484 103 103 VAL N N 120.4000 . 1 485 104 104 GLY H H 8.4280 . 1 486 104 104 GLY C C 172.0000 . 1 487 104 104 GLY CA C 44.0400 . 1 488 104 104 GLY N N 112.7000 . 1 489 105 105 THR H H 7.7900 . 1 490 105 105 THR C C 173.0000 . 1 491 105 105 THR CA C 59.3600 . 1 492 105 105 THR CB C 70.9600 . 1 493 105 105 THR N N 110.6000 . 1 494 106 106 GLY H H 7.8670 . 1 495 106 106 GLY C C 171.7000 . 1 496 106 106 GLY CA C 43.8400 . 1 497 106 106 GLY N N 104.9000 . 1 498 107 107 MET H H 7.9240 . 1 499 107 107 MET C C 176.1000 . 1 500 107 107 MET CA C 55.2500 . 1 501 107 107 MET CB C 33.5900 . 1 502 107 107 MET N N 121.6000 . 1 503 108 108 GLY H H 8.8110 . 1 504 108 108 GLY C C 171.9000 . 1 505 108 108 GLY CA C 44.5300 . 1 506 108 108 GLY N N 112.3000 . 1 507 109 109 LEU H H 8.7670 . 1 508 109 109 LEU C C 175.9000 . 1 509 109 109 LEU CA C 53.7400 . 1 510 109 109 LEU CB C 46.0100 . 1 511 109 109 LEU N N 124.7000 . 1 512 110 110 ARG H H 10.2800 . 1 513 110 110 ARG C C 180.4000 . 1 514 110 110 ARG CA C 57.1600 . 1 515 110 110 ARG CB C 29.6300 . 1 516 110 110 ARG N N 121.7000 . 1 517 111 111 LYS H H 9.2270 . 1 518 111 111 LYS C C 178.2000 . 1 519 111 111 LYS CA C 59.5700 . 1 520 111 111 LYS CB C 31.8300 . 1 521 111 111 LYS N N 123.2000 . 1 522 112 112 GLU H H 9.0280 . 1 523 112 112 GLU C C 177.7000 . 1 524 112 112 GLU CA C 57.2500 . 1 525 112 112 GLU CB C 27.7600 . 1 526 112 112 GLU N N 113.9000 . 1 527 113 113 ASP H H 7.2540 . 1 528 113 113 ASP C C 177.3000 . 1 529 113 113 ASP CA C 53.7100 . 1 530 113 113 ASP CB C 37.5300 . 1 531 113 113 ASP N N 126.0000 . 1 532 114 114 ASN H H 7.8390 . 1 533 114 114 ASN C C 176.9000 . 1 534 114 114 ASN CA C 56.9800 . 1 535 114 114 ASN CB C 38.8500 . 1 536 114 114 ASN N N 120.1000 . 1 537 115 115 GLU H H 8.7770 . 1 538 115 115 GLU C C 179.9000 . 1 539 115 115 GLU CA C 59.9100 . 1 540 115 115 GLU CB C 27.6200 . 1 541 115 115 GLU N N 120.5000 . 1 542 116 116 LEU H H 8.3690 . 1 543 116 116 LEU C C 177.1000 . 1 544 116 116 LEU CA C 57.4300 . 1 545 116 116 LEU CB C 40.6800 . 1 546 116 116 LEU N N 122.9000 . 1 547 117 117 ARG H H 7.5780 . 1 548 117 117 ARG C C 177.4000 . 1 549 117 117 ARG CA C 59.9700 . 1 550 117 117 ARG CB C 30.0700 . 1 551 117 117 ARG N N 119.1000 . 1 552 118 118 GLU H H 8.4020 . 1 553 118 118 GLU C C 179.8000 . 1 554 118 118 GLU CA C 59.1600 . 1 555 118 118 GLU CB C 28.5800 . 1 556 118 118 GLU N N 116.1000 . 1 557 119 119 ALA H H 8.1320 . 1 558 119 119 ALA C C 181.3000 . 1 559 119 119 ALA CA C 54.7500 . 1 560 119 119 ALA CB C 17.1600 . 1 561 119 119 ALA N N 123.5000 . 1 562 120 120 LEU H H 8.3660 . 1 563 120 120 LEU C C 178.4000 . 1 564 120 120 LEU CA C 57.7200 . 1 565 120 120 LEU CB C 41.4800 . 1 566 120 120 LEU N N 121.2000 . 1 567 121 121 ASN H H 8.4250 . 1 568 121 121 ASN C C 179.7000 . 1 569 121 121 ASN CA C 55.3000 . 1 570 121 121 ASN CB C 37.1200 . 1 571 121 121 ASN N N 119.2000 . 1 572 122 122 LYS H H 8.0660 . 1 573 122 122 LYS C C 178.4000 . 1 574 122 122 LYS CA C 59.1100 . 1 575 122 122 LYS CB C 31.7600 . 1 576 122 122 LYS N N 123.8000 . 1 577 123 123 ALA H H 7.9400 . 1 578 123 123 ALA C C 179.5000 . 1 579 123 123 ALA CA C 54.1400 . 1 580 123 123 ALA CB C 18.6900 . 1 581 123 123 ALA N N 122.2000 . 1 582 124 124 PHE H H 8.9040 . 1 583 124 124 PHE C C 177.2000 . 1 584 124 124 PHE CA C 61.2400 . 1 585 124 124 PHE CB C 37.9600 . 1 586 124 124 PHE N N 119.4000 . 1 587 125 125 ALA H H 7.9280 . 1 588 125 125 ALA C C 182.1000 . 1 589 125 125 ALA CA C 54.8700 . 1 590 125 125 ALA CB C 16.6600 . 1 591 125 125 ALA N N 121.3000 . 1 592 126 126 GLU H H 7.9290 . 1 593 126 126 GLU C C 178.6000 . 1 594 126 126 GLU CA C 59.0600 . 1 595 126 126 GLU CB C 28.3400 . 1 596 126 126 GLU N N 120.0000 . 1 597 127 127 MET H H 8.1770 . 1 598 127 127 MET C C 179.0000 . 1 599 127 127 MET CA C 57.4200 . 1 600 127 127 MET CB C 32.6700 . 1 601 127 127 MET N N 120.9000 . 1 602 128 128 ARG H H 7.7690 . 1 603 128 128 ARG C C 179.3000 . 1 604 128 128 ARG CA C 58.7000 . 1 605 128 128 ARG CB C 27.6300 . 1 606 128 128 ARG N N 119.2000 . 1 607 129 129 ALA H H 7.8120 . 1 608 129 129 ALA C C 179.3000 . 1 609 129 129 ALA CA C 54.1700 . 1 610 129 129 ALA CB C 18.0600 . 1 611 129 129 ALA N N 122.4000 . 1 612 130 130 ASP H H 8.0680 . 1 613 130 130 ASP C C 177.8000 . 1 614 130 130 ASP CA C 53.0500 . 1 615 130 130 ASP CB C 39.6000 . 1 616 130 130 ASP N N 115.1000 . 1 617 131 131 GLY H H 7.2050 . 1 618 131 131 GLY C C 176.0000 . 1 619 131 131 GLY CA C 45.0800 . 1 620 131 131 GLY N N 106.7000 . 1 621 132 132 THR H H 9.0950 . 1 622 132 132 THR C C 175.7000 . 1 623 132 132 THR CA C 67.6200 . 1 624 132 132 THR CB C 66.9300 . 1 625 132 132 THR N N 122.3000 . 1 626 133 133 TYR H H 8.0200 . 1 627 133 133 TYR C C 175.9000 . 1 628 133 133 TYR CA C 62.4900 . 1 629 133 133 TYR CB C 38.4200 . 1 630 133 133 TYR N N 121.3000 . 1 631 134 134 GLU H H 8.1430 . 1 632 134 134 GLU C C 178.2000 . 1 633 134 134 GLU CA C 58.9300 . 1 634 134 134 GLU CB C 28.8300 . 1 635 134 134 GLU N N 118.2000 . 1 636 135 135 LYS H H 7.5230 . 1 637 135 135 LYS C C 179.5000 . 1 638 135 135 LYS CA C 59.2100 . 1 639 135 135 LYS CB C 31.5200 . 1 640 135 135 LYS N N 119.0000 . 1 641 136 136 LEU H H 8.0320 . 1 642 136 136 LEU C C 179.2000 . 1 643 136 136 LEU CA C 57.0000 . 1 644 136 136 LEU CB C 41.4900 . 1 645 136 136 LEU N N 119.1000 . 1 646 137 137 ALA H H 8.8080 . 1 647 137 137 ALA C C 180.5000 . 1 648 137 137 ALA CA C 54.9400 . 1 649 137 137 ALA CB C 17.5100 . 1 650 137 137 ALA N N 121.1000 . 1 651 138 138 LYS H H 8.0240 . 1 652 138 138 LYS C C 177.7000 . 1 653 138 138 LYS CA C 57.3000 . 1 654 138 138 LYS CB C 31.4000 . 1 655 138 138 LYS N N 117.0000 . 1 656 139 139 LYS H H 7.0550 . 1 657 139 139 LYS C C 176.9000 . 1 658 139 139 LYS CA C 57.8800 . 1 659 139 139 LYS CB C 31.2000 . 1 660 139 139 LYS N N 117.5000 . 1 661 140 140 TYR H H 6.9880 . 1 662 140 140 TYR C C 175.0000 . 1 663 140 140 TYR CA C 57.9200 . 1 664 140 140 TYR CB C 39.9500 . 1 665 140 140 TYR N N 113.7000 . 1 666 141 141 PHE H H 8.0510 . 1 667 141 141 PHE C C 175.5000 . 1 668 141 141 PHE CA C 55.2400 . 1 669 141 141 PHE CB C 41.3300 . 1 670 141 141 PHE N N 116.8000 . 1 671 142 142 ASP H H 8.6220 . 1 672 142 142 ASP C C 174.4000 . 1 673 142 142 ASP CA C 52.5600 . 1 674 142 142 ASP CB C 39.6700 . 1 675 142 142 ASP N N 122.5000 . 1 676 143 143 PHE H H 6.7260 . 1 677 143 143 PHE C C 173.9000 . 1 678 143 143 PHE CA C 53.9500 . 1 679 143 143 PHE CB C 39.9200 . 1 680 143 143 PHE N N 115.2000 . 1 681 144 144 ASP H H 8.6950 . 1 682 144 144 ASP C C 176.0000 . 1 683 144 144 ASP CA C 53.4300 . 1 684 144 144 ASP CB C 39.5700 . 1 685 144 144 ASP N N 119.3000 . 1 686 145 145 VAL H H 7.5280 . 1 687 145 145 VAL C C 175.1000 . 1 688 145 145 VAL CA C 61.6900 . 1 689 145 145 VAL CB C 32.3600 . 1 690 145 145 VAL N N 128.7000 . 1 691 146 146 TYR H H 8.3440 . 1 692 146 146 TYR C C 176.8000 . 1 693 146 146 TYR CA C 61.9500 . 1 694 146 146 TYR CB C 38.1600 . 1 695 146 146 TYR N N 124.0000 . 1 696 147 147 GLY H H 7.6800 . 1 697 147 147 GLY C C 174.3000 . 1 698 147 147 GLY CA C 45.4700 . 1 699 147 147 GLY N N 104.8000 . 1 700 148 148 GLY H H 7.8020 . 1 701 148 148 GLY C C 178.9000 . 1 702 148 148 GLY CA C 45.6700 . 1 703 148 148 GLY N N 115.4000 . 1 stop_ save_