data_27620 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; human CYPA/PPIA ; _BMRB_accession_number 27620 _BMRB_flat_file_name bmr27620.str _Entry_type original _Submission_date 2018-09-24 _Accession_date 2018-09-24 _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 Jewginski Michal . . 2 Mackereth Cameron D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 158 "13C chemical shifts" 472 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-04-24 update BMRB 'update entry citation' 2018-09-25 original author 'original release' stop_ _Original_release_date 2018-09-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Assessing interactions between helical aromatic oligoamide foldamers and protein surfaces: a tethering approach ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30395443 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vallade Maelle . . 2 Jewginski Michal . . 3 Fischer Lucile . . 4 Buratto Jeremie . . 5 Bathany Katell . . 6 Schmitter Jean-Marie . . 7 Stupfel Marine . . 8 Godde Frederic . . 9 Mackereth Cameron D. . 10 Huc Ivan . . stop_ _Journal_abbreviation 'Bioconjug. Chem.' _Journal_volume 30 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 54 _Page_last 62 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CYPA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CYPA $CYPA 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_CYPA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CYPA _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 167 _Mol_residue_sequence ; GAMVNPTVFFDIAVDGEPLG RVSFELFADKVPKTAENFRA LSTGEKGFGYKGSCFHRIIP GFMCQGGDFTRHNGTGGKSI YGEKFEDENFILKHTGPGIL SMANAGPNTNGSQFFICTAK TEWLDGKHVVFGKVKEGMNI VEAMERFGSRNGKTSKKITI ADCGQLE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 ALA 3 1 MET 4 2 VAL 5 3 ASN 6 4 PRO 7 5 THR 8 6 VAL 9 7 PHE 10 8 PHE 11 9 ASP 12 10 ILE 13 11 ALA 14 12 VAL 15 13 ASP 16 14 GLY 17 15 GLU 18 16 PRO 19 17 LEU 20 18 GLY 21 19 ARG 22 20 VAL 23 21 SER 24 22 PHE 25 23 GLU 26 24 LEU 27 25 PHE 28 26 ALA 29 27 ASP 30 28 LYS 31 29 VAL 32 30 PRO 33 31 LYS 34 32 THR 35 33 ALA 36 34 GLU 37 35 ASN 38 36 PHE 39 37 ARG 40 38 ALA 41 39 LEU 42 40 SER 43 41 THR 44 42 GLY 45 43 GLU 46 44 LYS 47 45 GLY 48 46 PHE 49 47 GLY 50 48 TYR 51 49 LYS 52 50 GLY 53 51 SER 54 52 CYS 55 53 PHE 56 54 HIS 57 55 ARG 58 56 ILE 59 57 ILE 60 58 PRO 61 59 GLY 62 60 PHE 63 61 MET 64 62 CYS 65 63 GLN 66 64 GLY 67 65 GLY 68 66 ASP 69 67 PHE 70 68 THR 71 69 ARG 72 70 HIS 73 71 ASN 74 72 GLY 75 73 THR 76 74 GLY 77 75 GLY 78 76 LYS 79 77 SER 80 78 ILE 81 79 TYR 82 80 GLY 83 81 GLU 84 82 LYS 85 83 PHE 86 84 GLU 87 85 ASP 88 86 GLU 89 87 ASN 90 88 PHE 91 89 ILE 92 90 LEU 93 91 LYS 94 92 HIS 95 93 THR 96 94 GLY 97 95 PRO 98 96 GLY 99 97 ILE 100 98 LEU 101 99 SER 102 100 MET 103 101 ALA 104 102 ASN 105 103 ALA 106 104 GLY 107 105 PRO 108 106 ASN 109 107 THR 110 108 ASN 111 109 GLY 112 110 SER 113 111 GLN 114 112 PHE 115 113 PHE 116 114 ILE 117 115 CYS 118 116 THR 119 117 ALA 120 118 LYS 121 119 THR 122 120 GLU 123 121 TRP 124 122 LEU 125 123 ASP 126 124 GLY 127 125 LYS 128 126 HIS 129 127 VAL 130 128 VAL 131 129 PHE 132 130 GLY 133 131 LYS 134 132 VAL 135 133 LYS 136 134 GLU 137 135 GLY 138 136 MET 139 137 ASN 140 138 ILE 141 139 VAL 142 140 GLU 143 141 ALA 144 142 MET 145 143 GLU 146 144 ARG 147 145 PHE 148 146 GLY 149 147 SER 150 148 ARG 151 149 ASN 152 150 GLY 153 151 LYS 154 152 THR 155 153 SER 156 154 LYS 157 155 LYS 158 156 ILE 159 157 THR 160 158 ILE 161 159 ALA 162 160 ASP 163 161 CYS 164 162 GLY 165 163 GLN 166 164 LEU 167 165 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 SP P62937 PPIA . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CYPA Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $CYPA 'recombinant technology' . Escherichia coli BL21(DE3) pLysY pET-His1a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '13C,15N-labelled native sequence full-length human cyclophilin A' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CYPA 600 uM '[U-99% 13C; U-99% 15N]' TRIS 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' D2O 10 % '[U-100% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 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 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details '5 mm CPTCI 1H-13C/15N/D Z-GRD' 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_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 60 . mM pH 7.5 . pH pressure 1 . atm temperature 293 . 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 external indirect . . . 0.251449530 water H 1 protons ppm 4.82 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCA' '3D HNCACB' '3D CBCA(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 CYPA _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 3 MET H H 8.52 0.02 1 2 1 3 MET C C 175.80 0.2 1 3 1 3 MET CA C 55.34 0.2 1 4 1 3 MET CB C 32.88 0.2 1 5 1 3 MET N N 120.54 0.2 1 6 2 4 VAL H H 8.18 0.02 1 7 2 4 VAL C C 175.84 0.2 1 8 2 4 VAL CA C 61.38 0.2 1 9 2 4 VAL CB C 33.33 0.2 1 10 2 4 VAL N N 122.16 0.2 1 11 3 5 ASN H H 8.67 0.02 1 12 3 5 ASN C C 173.99 0.2 1 13 3 5 ASN CA C 51.05 0.2 1 14 3 5 ASN CB C 37.72 0.2 1 15 3 5 ASN N N 126.75 0.2 1 16 4 6 PRO C C 175.08 0.2 1 17 4 6 PRO CA C 62.81 0.2 1 18 4 6 PRO CB C 33.11 0.2 1 19 5 7 THR H H 8.81 0.02 1 20 5 7 THR C C 175.22 0.2 1 21 5 7 THR CA C 60.77 0.2 1 22 5 7 THR CB C 71.05 0.2 1 23 5 7 THR N N 115.12 0.2 1 24 6 8 VAL H H 8.74 0.02 1 25 6 8 VAL C C 173.77 0.2 1 26 6 8 VAL CA C 58.61 0.2 1 27 6 8 VAL CB C 35.99 0.2 1 28 6 8 VAL N N 120.19 0.2 1 29 7 9 PHE H H 8.98 0.02 1 30 7 9 PHE C C 172.63 0.2 1 31 7 9 PHE CA C 55.74 0.2 1 32 7 9 PHE CB C 42.92 0.2 1 33 7 9 PHE N N 119.23 0.2 1 34 8 10 PHE H H 9.58 0.02 1 35 8 10 PHE C C 175.00 0.2 1 36 8 10 PHE CA C 53.35 0.2 1 37 8 10 PHE CB C 42.90 0.2 1 38 8 10 PHE N N 117.07 0.2 1 39 9 11 ASP H H 9.30 0.02 1 40 9 11 ASP C C 175.26 0.2 1 41 9 11 ASP CA C 54.68 0.2 1 42 9 11 ASP CB C 41.29 0.2 1 43 9 11 ASP N N 124.38 0.2 1 44 10 12 ILE H H 9.07 0.02 1 45 10 12 ILE C C 176.06 0.2 1 46 10 12 ILE CA C 58.12 0.2 1 47 10 12 ILE CB C 37.59 0.2 1 48 10 12 ILE N N 124.33 0.2 1 49 11 13 ALA H H 9.64 0.02 1 50 11 13 ALA C C 174.88 0.2 1 51 11 13 ALA CA C 50.73 0.2 1 52 11 13 ALA CB C 22.48 0.2 1 53 11 13 ALA N N 132.59 0.2 1 54 12 14 VAL H H 8.95 0.02 1 55 12 14 VAL C C 176.47 0.2 1 56 12 14 VAL CA C 60.49 0.2 1 57 12 14 VAL CB C 33.09 0.2 1 58 12 14 VAL N N 118.60 0.2 1 59 13 15 ASP H H 9.88 0.02 1 60 13 15 ASP C C 176.13 0.2 1 61 13 15 ASP CA C 55.76 0.2 1 62 13 15 ASP CB C 39.76 0.2 1 63 13 15 ASP N N 131.11 0.2 1 64 14 16 GLY H H 8.59 0.02 1 65 14 16 GLY C C 173.67 0.2 1 66 14 16 GLY CA C 45.31 0.2 1 67 14 16 GLY N N 101.80 0.2 1 68 15 17 GLU H H 8.07 0.02 1 69 15 17 GLU C C 174.47 0.2 1 70 15 17 GLU CA C 52.93 0.2 1 71 15 17 GLU CB C 30.34 0.2 1 72 15 17 GLU N N 123.42 0.2 1 73 16 18 PRO C C 176.08 0.2 1 74 16 18 PRO CA C 64.82 0.2 1 75 16 18 PRO CB C 32.42 0.2 1 76 17 19 LEU H H 9.21 0.02 1 77 17 19 LEU C C 175.95 0.2 1 78 17 19 LEU CA C 55.48 0.2 1 79 17 19 LEU CB C 44.02 0.2 1 80 17 19 LEU N N 126.18 0.2 1 81 18 20 GLY H H 7.26 0.02 1 82 18 20 GLY C C 170.00 0.2 1 83 18 20 GLY CA C 45.24 0.2 1 84 18 20 GLY N N 102.65 0.2 1 85 19 21 ARG H H 8.39 0.02 1 86 19 21 ARG C C 174.99 0.2 1 87 19 21 ARG CA C 55.01 0.2 1 88 19 21 ARG CB C 33.33 0.2 1 89 19 21 ARG N N 121.32 0.2 1 90 20 22 VAL H H 9.40 0.02 1 91 20 22 VAL C C 173.84 0.2 1 92 20 22 VAL CA C 60.02 0.2 1 93 20 22 VAL CB C 34.78 0.2 1 94 20 22 VAL N N 127.01 0.2 1 95 21 23 SER H H 8.80 0.02 1 96 21 23 SER C C 173.74 0.2 1 97 21 23 SER CA C 55.37 0.2 1 98 21 23 SER CB C 66.61 0.2 1 99 21 23 SER N N 120.44 0.2 1 100 22 24 PHE H H 9.53 0.02 1 101 22 24 PHE C C 175.20 0.2 1 102 22 24 PHE CA C 55.80 0.2 1 103 22 24 PHE CB C 42.53 0.2 1 104 22 24 PHE N N 119.01 0.2 1 105 23 25 GLU H H 8.74 0.02 1 106 23 25 GLU C C 174.74 0.2 1 107 23 25 GLU CA C 55.23 0.2 1 108 23 25 GLU CB C 31.62 0.2 1 109 23 25 GLU N N 123.28 0.2 1 110 24 26 LEU H H 8.20 0.02 1 111 24 26 LEU C C 177.18 0.2 1 112 24 26 LEU CA C 51.75 0.2 1 113 24 26 LEU CB C 43.03 0.2 1 114 24 26 LEU N N 122.68 0.2 1 115 25 27 PHE H H 8.86 0.02 1 116 25 27 PHE C C 176.46 0.2 1 117 25 27 PHE CA C 54.36 0.2 1 118 25 27 PHE CB C 35.93 0.2 1 119 25 27 PHE N N 124.89 0.2 1 120 26 28 ALA H H 8.47 0.02 1 121 26 28 ALA C C 176.31 0.2 1 122 26 28 ALA CA C 54.40 0.2 1 123 26 28 ALA CB C 18.65 0.2 1 124 26 28 ALA N N 129.21 0.2 1 125 27 29 ASP H H 9.07 0.02 1 126 27 29 ASP C C 176.94 0.2 1 127 27 29 ASP CA C 55.38 0.2 1 128 27 29 ASP CB C 38.80 0.2 1 129 27 29 ASP N N 114.48 0.2 1 130 28 30 LYS H H 7.55 0.02 1 131 28 30 LYS C C 176.85 0.2 1 132 28 30 LYS CA C 56.23 0.2 1 133 28 30 LYS CB C 35.79 0.2 1 134 28 30 LYS N N 118.50 0.2 1 135 29 31 VAL H H 8.40 0.02 1 136 29 31 VAL HA H 4.48 0.02 1 137 29 31 VAL C C 172.22 0.2 1 138 29 31 VAL CA C 58.18 0.2 1 139 29 31 VAL CB C 31.69 0.2 1 140 29 31 VAL N N 114.84 0.2 1 141 30 32 PRO C C 180.91 0.2 1 142 30 32 PRO CA C 66.31 0.2 1 143 30 32 PRO CB C 31.72 0.2 1 144 31 33 LYS H H 10.69 0.02 1 145 31 33 LYS C C 181.82 0.2 1 146 31 33 LYS CA C 60.48 0.2 1 147 31 33 LYS CB C 32.30 0.2 1 148 31 33 LYS N N 123.97 0.2 1 149 32 34 THR H H 10.31 0.02 1 150 32 34 THR C C 177.65 0.2 1 151 32 34 THR CA C 67.52 0.2 1 152 32 34 THR CB C 68.86 0.2 1 153 32 34 THR N N 124.21 0.2 1 154 33 35 ALA H H 9.31 0.02 1 155 33 35 ALA C C 178.15 0.2 1 156 33 35 ALA CA C 55.92 0.2 1 157 33 35 ALA CB C 18.13 0.2 1 158 33 35 ALA N N 125.82 0.2 1 159 34 36 GLU H H 8.04 0.02 1 160 34 36 GLU C C 177.38 0.2 1 161 34 36 GLU CA C 57.90 0.2 1 162 34 36 GLU CB C 27.91 0.2 1 163 34 36 GLU N N 117.35 0.2 1 164 35 37 ASN H H 7.14 0.02 1 165 35 37 ASN C C 174.56 0.2 1 166 35 37 ASN CA C 56.75 0.2 1 167 35 37 ASN CB C 39.50 0.2 1 168 35 37 ASN N N 115.70 0.2 1 169 36 38 PHE H H 7.03 0.02 1 170 36 38 PHE C C 178.71 0.2 1 171 36 38 PHE CA C 61.46 0.2 1 172 36 38 PHE CB C 40.02 0.2 1 173 36 38 PHE N N 118.06 0.2 1 174 37 39 ARG H H 8.96 0.02 1 175 37 39 ARG C C 177.94 0.2 1 176 37 39 ARG CA C 60.47 0.2 1 177 37 39 ARG CB C 29.87 0.2 1 178 37 39 ARG N N 121.22 0.2 1 179 38 40 ALA H H 8.70 0.02 1 180 38 40 ALA C C 182.37 0.2 1 181 38 40 ALA CA C 54.39 0.2 1 182 38 40 ALA CB C 18.21 0.2 1 183 38 40 ALA N N 119.20 0.2 1 184 39 41 LEU H H 8.21 0.02 1 185 39 41 LEU C C 179.50 0.2 1 186 39 41 LEU CA C 57.25 0.2 1 187 39 41 LEU CB C 41.02 0.2 1 188 39 41 LEU N N 120.87 0.2 1 189 40 42 SER H H 7.90 0.02 1 190 40 42 SER C C 174.40 0.2 1 191 40 42 SER CA C 63.37 0.2 1 192 40 42 SER CB C 62.92 0.2 1 193 40 42 SER N N 119.45 0.2 1 194 41 43 THR H H 7.99 0.02 1 195 41 43 THR C C 178.13 0.2 1 196 41 43 THR CA C 62.85 0.2 1 197 41 43 THR CB C 69.56 0.2 1 198 41 43 THR N N 108.56 0.2 1 199 42 44 GLY H H 7.59 0.02 1 200 42 44 GLY C C 177.69 0.2 1 201 42 44 GLY CA C 45.78 0.2 1 202 42 44 GLY N N 108.42 0.2 1 203 43 45 GLU H H 8.03 0.02 1 204 43 45 GLU C C 176.50 0.2 1 205 43 45 GLU CA C 58.55 0.2 1 206 43 45 GLU CB C 30.01 0.2 1 207 43 45 GLU N N 118.75 0.2 1 208 44 46 LYS H H 9.14 0.02 1 209 44 46 LYS C C 176.59 0.2 1 210 44 46 LYS CA C 54.28 0.2 1 211 44 46 LYS CB C 30.26 0.2 1 212 44 46 LYS N N 118.61 0.2 1 213 45 47 GLY H H 7.96 0.02 1 214 45 47 GLY C C 172.52 0.2 1 215 45 47 GLY CA C 44.63 0.2 1 216 45 47 GLY N N 105.70 0.2 1 217 46 48 PHE H H 6.43 0.02 1 218 46 48 PHE C C 172.69 0.2 1 219 46 48 PHE CA C 54.03 0.2 1 220 46 48 PHE CB C 39.55 0.2 1 221 46 48 PHE N N 113.82 0.2 1 222 47 49 GLY H H 7.77 0.02 1 223 47 49 GLY C C 171.45 0.2 1 224 47 49 GLY CA C 45.53 0.2 1 225 47 49 GLY N N 104.79 0.2 1 226 48 50 TYR H H 6.91 0.02 1 227 48 50 TYR C C 178.00 0.2 1 228 48 50 TYR CA C 57.16 0.2 1 229 48 50 TYR CB C 38.41 0.2 1 230 48 50 TYR N N 113.86 0.2 1 231 49 51 LYS H H 8.50 0.02 1 232 49 51 LYS C C 177.46 0.2 1 233 49 51 LYS CA C 61.12 0.2 1 234 49 51 LYS CB C 31.22 0.2 1 235 49 51 LYS N N 125.10 0.2 1 236 50 52 GLY H H 9.51 0.02 1 237 50 52 GLY C C 174.30 0.2 1 238 50 52 GLY CA C 45.27 0.2 1 239 50 52 GLY N N 118.09 0.2 1 240 51 53 SER H H 8.40 0.02 1 241 51 53 SER C C 171.72 0.2 1 242 51 53 SER CA C 58.91 0.2 1 243 51 53 SER CB C 64.73 0.2 1 244 51 53 SER N N 116.55 0.2 1 245 52 54 CYS H H 10.08 0.02 1 246 52 54 CYS C C 176.44 0.2 1 247 52 54 CYS CA C 56.07 0.2 1 248 52 54 CYS CB C 32.04 0.2 1 249 52 54 CYS N N 115.36 0.2 1 250 53 55 PHE H H 8.73 0.02 1 251 53 55 PHE C C 174.88 0.2 1 252 53 55 PHE CA C 58.10 0.2 1 253 53 55 PHE CB C 38.80 0.2 1 254 53 55 PHE N N 123.18 0.2 1 255 54 56 HIS H H 7.60 0.02 1 256 54 56 HIS C C 175.45 0.2 1 257 54 56 HIS CA C 57.14 0.2 1 258 54 56 HIS CB C 31.52 0.2 1 259 54 56 HIS N N 120.47 0.2 1 260 55 57 ARG H H 7.05 0.02 1 261 55 57 ARG C C 173.44 0.2 1 262 55 57 ARG CA C 54.80 0.2 1 263 55 57 ARG CB C 33.49 0.2 1 264 55 57 ARG N N 123.36 0.2 1 265 56 58 ILE H H 9.21 0.02 1 266 56 58 ILE C C 173.58 0.2 1 267 56 58 ILE CA C 61.61 0.2 1 268 56 58 ILE CB C 41.48 0.2 1 269 56 58 ILE N N 126.57 0.2 1 270 57 59 ILE H H 8.73 0.02 1 271 57 59 ILE C C 173.70 0.2 1 272 57 59 ILE CA C 57.70 0.2 1 273 57 59 ILE CB C 40.54 0.2 1 274 57 59 ILE N N 128.07 0.2 1 275 58 60 PRO C C 177.71 0.2 1 276 58 60 PRO CA C 62.99 0.2 1 277 58 60 PRO CB C 31.97 0.2 1 278 59 61 GLY H H 9.77 0.02 1 279 59 61 GLY C C 172.29 0.2 1 280 59 61 GLY CA C 45.03 0.2 1 281 59 61 GLY N N 114.41 0.2 1 282 60 62 PHE H H 8.19 0.02 1 283 60 62 PHE C C 173.42 0.2 1 284 60 62 PHE CA C 56.93 0.2 1 285 60 62 PHE CB C 39.77 0.2 1 286 60 62 PHE N N 119.48 0.2 1 287 61 63 MET H H 8.09 0.02 1 288 61 63 MET C C 174.17 0.2 1 289 61 63 MET CA C 55.05 0.2 1 290 61 63 MET CB C 34.63 0.2 1 291 61 63 MET N N 111.25 0.2 1 292 62 64 CYS H H 8.49 0.02 1 293 62 64 CYS C C 173.08 0.2 1 294 62 64 CYS CA C 57.55 0.2 1 295 62 64 CYS CB C 30.20 0.2 1 296 62 64 CYS N N 114.88 0.2 1 297 63 65 GLN H H 9.66 0.02 1 298 63 65 GLN C C 174.00 0.2 1 299 63 65 GLN CA C 54.60 0.2 1 300 63 65 GLN CB C 30.43 0.2 1 301 63 65 GLN N N 126.80 0.2 1 302 64 66 GLY H H 7.36 0.02 1 303 64 66 GLY C C 173.33 0.2 1 304 64 66 GLY CA C 44.62 0.2 1 305 64 66 GLY N N 110.94 0.2 1 306 65 67 GLY H H 9.41 0.02 1 307 65 67 GLY C C 175.24 0.2 1 308 65 67 GLY CA C 46.65 0.2 1 309 65 67 GLY N N 106.22 0.2 1 310 66 68 ASP H H 9.99 0.02 1 311 66 68 ASP C C 176.16 0.2 1 312 66 68 ASP CA C 51.61 0.2 1 313 66 68 ASP CB C 38.61 0.2 1 314 66 68 ASP N N 124.15 0.2 1 315 67 69 PHE H H 6.64 0.02 1 316 67 69 PHE C C 174.08 0.2 1 317 67 69 PHE CA C 56.09 0.2 1 318 67 69 PHE CB C 39.23 0.2 1 319 67 69 PHE N N 116.06 0.2 1 320 68 70 THR H H 7.28 0.02 1 321 68 70 THR C C 175.62 0.2 1 322 68 70 THR CA C 61.88 0.2 1 323 68 70 THR CB C 68.94 0.2 1 324 68 70 THR N N 108.95 0.2 1 325 69 71 ARG H H 8.67 0.02 1 326 69 71 ARG C C 176.22 0.2 1 327 69 71 ARG CA C 55.11 0.2 1 328 69 71 ARG CB C 31.69 0.2 1 329 69 71 ARG N N 122.13 0.2 1 330 70 72 HIS C C 174.39 0.2 1 331 70 72 HIS CA C 56.93 0.2 1 332 70 72 HIS CB C 28.68 0.2 1 333 71 73 ASN H H 7.50 0.02 1 334 71 73 ASN C C 175.86 0.2 1 335 71 73 ASN CA C 52.34 0.2 1 336 71 73 ASN CB C 38.81 0.2 1 337 71 73 ASN N N 112.49 0.2 1 338 72 74 GLY H H 9.71 0.02 1 339 72 74 GLY C C 175.74 0.2 1 340 72 74 GLY CA C 44.86 0.2 1 341 72 74 GLY N N 110.81 0.2 1 342 73 75 THR H H 7.94 0.02 1 343 73 75 THR C C 175.91 0.2 1 344 73 75 THR CA C 62.30 0.2 1 345 73 75 THR CB C 70.63 0.2 1 346 73 75 THR N N 112.25 0.2 1 347 74 76 GLY H H 8.73 0.02 1 348 74 76 GLY C C 175.22 0.2 1 349 74 76 GLY CA C 45.07 0.2 1 350 74 76 GLY N N 114.16 0.2 1 351 75 77 GLY H H 8.13 0.02 1 352 75 77 GLY C C 172.07 0.2 1 353 75 77 GLY CA C 43.08 0.2 1 354 75 77 GLY N N 109.11 0.2 1 355 76 78 LYS H H 7.00 0.02 1 356 76 78 LYS C C 172.43 0.2 1 357 76 78 LYS CA C 55.88 0.2 1 358 76 78 LYS CB C 34.42 0.2 1 359 76 78 LYS N N 115.47 0.2 1 360 77 79 SER H H 7.72 0.02 1 361 77 79 SER C C 175.73 0.2 1 362 77 79 SER CA C 57.01 0.2 1 363 77 79 SER CB C 69.60 0.2 1 364 77 79 SER N N 114.39 0.2 1 365 78 80 ILE H H 8.58 0.02 1 366 78 80 ILE C C 175.95 0.2 1 367 78 80 ILE CA C 63.77 0.2 1 368 78 80 ILE CB C 37.18 0.2 1 369 78 80 ILE N N 111.38 0.2 1 370 79 81 TYR H H 8.07 0.02 1 371 79 81 TYR C C 175.39 0.2 1 372 79 81 TYR CA C 56.18 0.2 1 373 79 81 TYR CB C 38.64 0.2 1 374 79 81 TYR N N 121.03 0.2 1 375 80 82 GLY H H 7.08 0.02 1 376 80 82 GLY C C 174.15 0.2 1 377 80 82 GLY CA C 43.80 0.2 1 378 80 82 GLY N N 106.56 0.2 1 379 81 83 GLU C C 175.77 0.2 1 380 81 83 GLU CA C 60.83 0.2 1 381 81 83 GLU CB C 30.21 0.2 1 382 82 84 LYS H H 7.84 0.02 1 383 82 84 LYS C C 175.48 0.2 1 384 82 84 LYS CA C 53.67 0.2 1 385 82 84 LYS CB C 36.81 0.2 1 386 82 84 LYS N N 112.05 0.2 1 387 83 85 PHE H H 9.18 0.02 1 388 83 85 PHE C C 173.47 0.2 1 389 83 85 PHE CA C 55.99 0.2 1 390 83 85 PHE CB C 41.19 0.2 1 391 83 85 PHE N N 116.59 0.2 1 392 84 86 GLU H H 9.26 0.02 1 393 84 86 GLU C C 176.27 0.2 1 394 84 86 GLU CA C 56.26 0.2 1 395 84 86 GLU CB C 29.11 0.2 1 396 84 86 GLU N N 119.59 0.2 1 397 85 87 ASP H H 8.63 0.02 1 398 85 87 ASP C C 176.21 0.2 1 399 85 87 ASP CA C 54.38 0.2 1 400 85 87 ASP CB C 40.76 0.2 1 401 85 87 ASP N N 118.93 0.2 1 402 86 88 GLU H H 9.50 0.02 1 403 86 88 GLU C C 176.26 0.2 1 404 86 88 GLU CA C 60.29 0.2 1 405 86 88 GLU CB C 31.82 0.2 1 406 86 88 GLU N N 132.02 0.2 1 407 87 89 ASN H H 7.06 0.02 1 408 87 89 ASN C C 170.71 0.2 1 409 87 89 ASN CA C 52.79 0.2 1 410 87 89 ASN CB C 39.43 0.2 1 411 87 89 ASN N N 106.84 0.2 1 412 88 90 PHE H H 8.36 0.02 1 413 88 90 PHE C C 177.91 0.2 1 414 88 90 PHE CA C 55.85 0.2 1 415 88 90 PHE CB C 38.86 0.2 1 416 88 90 PHE N N 113.01 0.2 1 417 89 91 ILE H H 8.33 0.02 1 418 89 91 ILE C C 177.74 0.2 1 419 89 91 ILE CA C 65.00 0.2 1 420 89 91 ILE CB C 38.89 0.2 1 421 89 91 ILE N N 119.99 0.2 1 422 90 92 LEU H H 7.77 0.02 1 423 90 92 LEU C C 176.32 0.2 1 424 90 92 LEU CA C 54.10 0.2 1 425 90 92 LEU CB C 41.80 0.2 1 426 90 92 LEU N N 117.31 0.2 1 427 91 93 LYS H H 8.09 0.02 1 428 91 93 LYS C C 176.30 0.2 1 429 91 93 LYS CA C 54.46 0.2 1 430 91 93 LYS CB C 34.58 0.2 1 431 91 93 LYS N N 119.01 0.2 1 432 92 94 HIS H H 10.73 0.02 1 433 92 94 HIS C C 177.81 0.2 1 434 92 94 HIS CA C 56.99 0.2 1 435 92 94 HIS CB C 25.86 0.2 1 436 92 94 HIS N N 122.63 0.2 1 437 93 95 THR H H 7.27 0.02 1 438 93 95 THR C C 175.50 0.2 1 439 93 95 THR CA C 63.24 0.2 1 440 93 95 THR CB C 69.70 0.2 1 441 93 95 THR N N 110.53 0.2 1 442 94 96 GLY H H 7.51 0.02 1 443 94 96 GLY C C 168.71 0.2 1 444 94 96 GLY CA C 45.62 0.2 1 445 94 96 GLY N N 107.45 0.2 1 446 95 97 PRO C C 177.13 0.2 1 447 95 97 PRO CA C 62.77 0.2 1 448 95 97 PRO CB C 31.97 0.2 1 449 96 98 GLY H H 9.29 0.02 1 450 96 98 GLY C C 173.03 0.2 1 451 96 98 GLY CA C 44.99 0.2 1 452 96 98 GLY N N 110.47 0.2 1 453 97 99 ILE H H 6.77 0.02 1 454 97 99 ILE C C 173.21 0.2 1 455 97 99 ILE CA C 59.41 0.2 1 456 97 99 ILE CB C 37.54 0.2 1 457 97 99 ILE N N 121.51 0.2 1 458 98 100 LEU H H 7.89 0.02 1 459 98 100 LEU C C 174.15 0.2 1 460 98 100 LEU CA C 53.25 0.2 1 461 98 100 LEU CB C 43.65 0.2 1 462 98 100 LEU N N 129.00 0.2 1 463 99 101 SER H H 8.29 0.02 1 464 99 101 SER C C 174.75 0.2 1 465 99 101 SER CA C 55.01 0.2 1 466 99 101 SER CB C 65.33 0.2 1 467 99 101 SER N N 118.84 0.2 1 468 100 102 MET H H 8.56 0.02 1 469 100 102 MET C C 177.84 0.2 1 470 100 102 MET CA C 53.83 0.2 1 471 100 102 MET CB C 31.03 0.2 1 472 100 102 MET N N 123.11 0.2 1 473 101 103 ALA H H 8.01 0.02 1 474 101 103 ALA C C 175.62 0.2 1 475 101 103 ALA CA C 51.60 0.2 1 476 101 103 ALA CB C 19.46 0.2 1 477 101 103 ALA N N 126.00 0.2 1 478 102 104 ASN H H 8.15 0.02 1 479 102 104 ASN C C 173.85 0.2 1 480 102 104 ASN CA C 54.18 0.2 1 481 102 104 ASN CB C 40.45 0.2 1 482 102 104 ASN N N 113.47 0.2 1 483 103 105 ALA H H 8.79 0.02 1 484 103 105 ALA C C 176.93 0.2 1 485 103 105 ALA CA C 50.36 0.2 1 486 103 105 ALA CB C 18.98 0.2 1 487 103 105 ALA N N 123.46 0.2 1 488 104 106 GLY H H 8.21 0.02 1 489 104 106 GLY C C 172.13 0.2 1 490 104 106 GLY CA C 43.51 0.2 1 491 104 106 GLY N N 109.50 0.2 1 492 105 107 PRO C C 176.16 0.2 1 493 105 107 PRO CA C 64.01 0.2 1 494 105 107 PRO CB C 31.84 0.2 1 495 106 108 ASN H H 8.87 0.02 1 496 106 108 ASN C C 175.02 0.2 1 497 106 108 ASN CA C 54.29 0.2 1 498 106 108 ASN CB C 37.06 0.2 1 499 106 108 ASN N N 119.18 0.2 1 500 107 109 THR H H 10.25 0.02 1 501 107 109 THR C C 173.73 0.2 1 502 107 109 THR CA C 60.29 0.2 1 503 107 109 THR CB C 69.00 0.2 1 504 107 109 THR N N 110.54 0.2 1 505 108 110 ASN H H 7.38 0.02 1 506 108 110 ASN C C 174.12 0.2 1 507 108 110 ASN CA C 55.70 0.2 1 508 108 110 ASN CB C 39.72 0.2 1 509 108 110 ASN N N 120.75 0.2 1 510 109 111 GLY H H 9.20 0.02 1 511 109 111 GLY C C 171.08 0.2 1 512 109 111 GLY CA C 45.78 0.2 1 513 109 111 GLY N N 110.85 0.2 1 514 110 112 SER H H 8.78 0.02 1 515 110 112 SER C C 176.02 0.2 1 516 110 112 SER CA C 57.56 0.2 1 517 110 112 SER CB C 66.27 0.2 1 518 110 112 SER N N 117.20 0.2 1 519 111 113 GLN H H 8.39 0.02 1 520 111 113 GLN C C 175.10 0.2 1 521 111 113 GLN CA C 57.66 0.2 1 522 111 113 GLN CB C 31.76 0.2 1 523 111 113 GLN N N 124.57 0.2 1 524 112 114 PHE H H 8.07 0.02 1 525 112 114 PHE C C 171.83 0.2 1 526 112 114 PHE CA C 55.41 0.2 1 527 112 114 PHE CB C 43.08 0.2 1 528 112 114 PHE N N 117.99 0.2 1 529 113 115 PHE H H 9.82 0.02 1 530 113 115 PHE C C 174.38 0.2 1 531 113 115 PHE CA C 54.57 0.2 1 532 113 115 PHE CB C 42.76 0.2 1 533 113 115 PHE N N 116.57 0.2 1 534 114 116 ILE H H 9.12 0.02 1 535 114 116 ILE C C 177.46 0.2 1 536 114 116 ILE CA C 59.94 0.2 1 537 114 116 ILE CB C 40.22 0.2 1 538 114 116 ILE N N 118.61 0.2 1 539 115 117 CYS H H 9.62 0.02 1 540 115 117 CYS C C 176.66 0.2 1 541 115 117 CYS CA C 60.85 0.2 1 542 115 117 CYS CB C 28.64 0.2 1 543 115 117 CYS N N 125.61 0.2 1 544 116 118 THR H H 8.97 0.02 1 545 116 118 THR C C 172.39 0.2 1 546 116 118 THR CA C 60.75 0.2 1 547 116 118 THR CB C 66.88 0.2 1 548 116 118 THR N N 115.80 0.2 1 549 117 119 ALA H H 7.63 0.02 1 550 117 119 ALA C C 175.25 0.2 1 551 117 119 ALA CA C 50.56 0.2 1 552 117 119 ALA CB C 22.60 0.2 1 553 117 119 ALA N N 122.41 0.2 1 554 118 120 LYS H H 8.74 0.02 1 555 118 120 LYS C C 176.23 0.2 1 556 118 120 LYS CA C 57.97 0.2 1 557 118 120 LYS CB C 32.67 0.2 1 558 118 120 LYS N N 120.24 0.2 1 559 119 121 THR H H 7.35 0.02 1 560 119 121 THR C C 177.04 0.2 1 561 119 121 THR CA C 57.31 0.2 1 562 119 121 THR CB C 68.76 0.2 1 563 119 121 THR N N 119.19 0.2 1 564 120 122 GLU H H 9.12 0.02 1 565 120 122 GLU C C 177.11 0.2 1 566 120 122 GLU CA C 59.30 0.2 1 567 120 122 GLU CB C 28.90 0.2 1 568 120 122 GLU N N 124.71 0.2 1 569 121 123 TRP H H 7.27 0.02 1 570 121 123 TRP HE1 H 9.73 0.02 1 571 121 123 TRP C C 176.32 0.2 1 572 121 123 TRP CA C 59.71 0.2 1 573 121 123 TRP CB C 26.71 0.2 1 574 121 123 TRP N N 118.02 0.2 1 575 121 123 TRP NE1 N 130.19 0.2 1 576 122 124 LEU H H 7.04 0.02 1 577 122 124 LEU C C 177.45 0.2 1 578 122 124 LEU CA C 54.60 0.2 1 579 122 124 LEU CB C 38.67 0.2 1 580 122 124 LEU N N 120.19 0.2 1 581 123 125 ASP H H 7.62 0.02 1 582 123 125 ASP C C 178.35 0.2 1 583 123 125 ASP CA C 55.82 0.2 1 584 123 125 ASP CB C 39.36 0.2 1 585 123 125 ASP N N 122.35 0.2 1 586 124 126 GLY H H 9.56 0.02 1 587 124 126 GLY C C 172.06 0.2 1 588 124 126 GLY CA C 45.02 0.2 1 589 124 126 GLY N N 111.44 0.2 1 590 125 127 LYS H H 7.75 0.02 1 591 125 127 LYS C C 175.31 0.2 1 592 125 127 LYS CA C 56.31 0.2 1 593 125 127 LYS CB C 35.40 0.2 1 594 125 127 LYS N N 115.74 0.2 1 595 126 128 HIS H H 7.58 0.02 1 596 126 128 HIS C C 173.95 0.2 1 597 126 128 HIS CA C 54.84 0.2 1 598 126 128 HIS CB C 31.54 0.2 1 599 126 128 HIS N N 119.99 0.2 1 600 127 129 VAL H H 8.49 0.02 1 601 127 129 VAL C C 175.30 0.2 1 602 127 129 VAL CA C 63.84 0.2 1 603 127 129 VAL CB C 33.41 0.2 1 604 127 129 VAL N N 124.90 0.2 1 605 128 130 VAL H H 9.51 0.02 1 606 128 130 VAL C C 177.03 0.2 1 607 128 130 VAL CA C 63.08 0.2 1 608 128 130 VAL CB C 31.73 0.2 1 609 128 130 VAL N N 133.04 0.2 1 610 129 131 PHE H H 8.12 0.02 1 611 129 131 PHE C C 172.72 0.2 1 612 129 131 PHE CA C 55.91 0.2 1 613 129 131 PHE CB C 42.53 0.2 1 614 129 131 PHE N N 117.97 0.2 1 615 130 132 GLY H H 7.32 0.02 1 616 130 132 GLY C C 170.64 0.2 1 617 130 132 GLY CA C 46.45 0.2 1 618 130 132 GLY N N 110.89 0.2 1 619 131 133 LYS H H 8.37 0.02 1 620 131 133 LYS C C 175.08 0.2 1 621 131 133 LYS CA C 54.81 0.2 1 622 131 133 LYS CB C 35.94 0.2 1 623 131 133 LYS N N 115.30 0.2 1 624 132 134 VAL H H 9.04 0.02 1 625 132 134 VAL C C 175.38 0.2 1 626 132 134 VAL CA C 64.07 0.2 1 627 132 134 VAL CB C 32.60 0.2 1 628 132 134 VAL N N 124.12 0.2 1 629 133 135 LYS H H 9.49 0.02 1 630 133 135 LYS C C 175.33 0.2 1 631 133 135 LYS CA C 56.61 0.2 1 632 133 135 LYS CB C 33.91 0.2 1 633 133 135 LYS N N 131.94 0.2 1 634 134 136 GLU H H 7.56 0.02 1 635 134 136 GLU C C 174.88 0.2 1 636 134 136 GLU CA C 55.29 0.2 1 637 134 136 GLU CB C 32.75 0.2 1 638 134 136 GLU N N 118.59 0.2 1 639 135 137 GLY H H 8.70 0.02 1 640 135 137 GLY C C 177.13 0.2 1 641 135 137 GLY CA C 46.04 0.2 1 642 135 137 GLY N N 108.09 0.2 1 643 136 138 MET H H 8.88 0.02 1 644 136 138 MET C C 177.65 0.2 1 645 136 138 MET CA C 56.84 0.2 1 646 136 138 MET CB C 30.09 0.2 1 647 136 138 MET N N 122.71 0.2 1 648 137 139 ASN H H 8.93 0.02 1 649 137 139 ASN C C 177.52 0.2 1 650 137 139 ASN CA C 56.07 0.2 1 651 137 139 ASN CB C 35.89 0.2 1 652 137 139 ASN N N 114.65 0.2 1 653 138 140 ILE H H 7.65 0.02 1 654 138 140 ILE C C 177.62 0.2 1 655 138 140 ILE CA C 61.54 0.2 1 656 138 140 ILE CB C 34.12 0.2 1 657 138 140 ILE N N 124.42 0.2 1 658 139 141 VAL H H 7.26 0.02 1 659 139 141 VAL C C 178.03 0.2 1 660 139 141 VAL CA C 66.11 0.2 1 661 139 141 VAL CB C 31.08 0.2 1 662 139 141 VAL N N 122.12 0.2 1 663 140 142 GLU H H 8.32 0.02 1 664 140 142 GLU C C 179.46 0.2 1 665 140 142 GLU CA C 59.20 0.2 1 666 140 142 GLU CB C 29.58 0.2 1 667 140 142 GLU N N 117.53 0.2 1 668 141 143 ALA H H 7.51 0.02 1 669 141 143 ALA C C 180.63 0.2 1 670 141 143 ALA CA C 54.90 0.2 1 671 141 143 ALA CB C 17.99 0.2 1 672 141 143 ALA N N 121.17 0.2 1 673 142 144 MET H H 8.30 0.02 1 674 142 144 MET C C 177.88 0.2 1 675 142 144 MET CA C 59.66 0.2 1 676 142 144 MET CB C 33.46 0.2 1 677 142 144 MET N N 117.90 0.2 1 678 143 145 GLU H H 7.87 0.02 1 679 143 145 GLU C C 177.99 0.2 1 680 143 145 GLU CA C 59.34 0.2 1 681 143 145 GLU CB C 30.33 0.2 1 682 143 145 GLU N N 116.55 0.2 1 683 144 146 ARG H H 7.04 0.02 1 684 144 146 ARG C C 177.28 0.2 1 685 144 146 ARG CA C 57.70 0.2 1 686 144 146 ARG CB C 29.53 0.2 1 687 144 146 ARG N N 114.64 0.2 1 688 145 147 PHE H H 7.64 0.02 1 689 145 147 PHE C C 175.79 0.2 1 690 145 147 PHE CA C 57.81 0.2 1 691 145 147 PHE CB C 38.72 0.2 1 692 145 147 PHE N N 115.52 0.2 1 693 146 148 GLY H H 7.54 0.02 1 694 146 148 GLY C C 171.99 0.2 1 695 146 148 GLY CA C 44.03 0.2 1 696 146 148 GLY N N 104.80 0.2 1 697 147 149 SER H H 8.23 0.02 1 698 147 149 SER C C 175.47 0.2 1 699 147 149 SER CA C 58.31 0.2 1 700 147 149 SER CB C 65.81 0.2 1 701 147 149 SER N N 110.09 0.2 1 702 148 150 ARG C C 176.83 0.2 1 703 148 150 ARG CA C 59.74 0.2 1 704 148 150 ARG CB C 29.85 0.2 1 705 149 151 ASN H H 7.89 0.02 1 706 149 151 ASN C C 176.79 0.2 1 707 149 151 ASN CA C 52.39 0.2 1 708 149 151 ASN CB C 38.40 0.2 1 709 149 151 ASN N N 111.87 0.2 1 710 150 152 GLY H H 8.05 0.02 1 711 150 152 GLY C C 173.34 0.2 1 712 150 152 GLY CA C 44.94 0.2 1 713 150 152 GLY N N 110.39 0.2 1 714 151 153 LYS H H 7.55 0.02 1 715 151 153 LYS C C 178.65 0.2 1 716 151 153 LYS CA C 57.30 0.2 1 717 151 153 LYS CB C 32.34 0.2 1 718 151 153 LYS N N 120.07 0.2 1 719 152 154 THR H H 8.89 0.02 1 720 152 154 THR C C 176.01 0.2 1 721 152 154 THR CA C 60.10 0.2 1 722 152 154 THR CB C 71.44 0.2 1 723 152 154 THR N N 117.08 0.2 1 724 153 155 SER H H 9.45 0.02 1 725 153 155 SER C C 174.00 0.2 1 726 153 155 SER CA C 59.01 0.2 1 727 153 155 SER CB C 63.67 0.2 1 728 153 155 SER N N 117.13 0.2 1 729 154 156 LYS H H 7.55 0.02 1 730 154 156 LYS C C 174.31 0.2 1 731 154 156 LYS CA C 54.73 0.2 1 732 154 156 LYS CB C 38.34 0.2 1 733 154 156 LYS N N 119.86 0.2 1 734 155 157 LYS H H 8.81 0.02 1 735 155 157 LYS C C 175.99 0.2 1 736 155 157 LYS CA C 56.45 0.2 1 737 155 157 LYS CB C 32.13 0.2 1 738 155 157 LYS N N 121.88 0.2 1 739 156 158 ILE H H 9.63 0.02 1 740 156 158 ILE C C 176.31 0.2 1 741 156 158 ILE CA C 59.36 0.2 1 742 156 158 ILE CB C 36.60 0.2 1 743 156 158 ILE N N 134.57 0.2 1 744 157 159 THR H H 9.27 0.02 1 745 157 159 THR C C 173.53 0.2 1 746 157 159 THR CA C 59.66 0.2 1 747 157 159 THR CB C 72.66 0.2 1 748 157 159 THR N N 117.10 0.2 1 749 158 160 ILE H H 8.60 0.02 1 750 158 160 ILE C C 174.68 0.2 1 751 158 160 ILE CA C 60.55 0.2 1 752 158 160 ILE CB C 36.86 0.2 1 753 158 160 ILE N N 121.66 0.2 1 754 159 161 ALA H H 8.90 0.02 1 755 159 161 ALA C C 178.61 0.2 1 756 159 161 ALA CA C 54.15 0.2 1 757 159 161 ALA CB C 18.72 0.2 1 758 159 161 ALA N N 132.56 0.2 1 759 160 162 ASP H H 8.08 0.02 1 760 160 162 ASP C C 172.88 0.2 1 761 160 162 ASP CA C 52.69 0.2 1 762 160 162 ASP CB C 43.58 0.2 1 763 160 162 ASP N N 111.67 0.2 1 764 161 163 CYS H H 8.60 0.02 1 765 161 163 CYS C C 172.47 0.2 1 766 161 163 CYS CA C 55.36 0.2 1 767 161 163 CYS CB C 31.36 0.2 1 768 161 163 CYS N N 116.23 0.2 1 769 162 164 GLY H H 6.86 0.02 1 770 162 164 GLY C C 170.06 0.2 1 771 162 164 GLY CA C 45.37 0.2 1 772 162 164 GLY N N 104.29 0.2 1 773 163 165 GLN H H 9.10 0.02 1 774 163 165 GLN C C 175.49 0.2 1 775 163 165 GLN CA C 54.99 0.2 1 776 163 165 GLN CB C 30.63 0.2 1 777 163 165 GLN N N 121.14 0.2 1 778 164 166 LEU H H 8.60 0.02 1 779 164 166 LEU C C 176.06 0.2 1 780 164 166 LEU CA C 54.80 0.2 1 781 164 166 LEU CB C 43.27 0.2 1 782 164 166 LEU N N 126.17 0.2 1 783 165 167 GLU H H 8.18 0.02 1 784 165 167 GLU C C 180.72 0.2 1 785 165 167 GLU CA C 58.16 0.2 1 786 165 167 GLU CB C 31.52 0.2 1 787 165 167 GLU N N 126.38 0.2 1 stop_ save_