data_27266 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for TNF alpha ; _BMRB_accession_number 27266 _BMRB_flat_file_name bmr27266.str _Entry_type original _Submission_date 2017-09-28 _Accession_date 2017-09-28 _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 Hofmann Daniela . . 2 Salmon Loic . . 3 Wider Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 123 "13C chemical shifts" 348 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-01-18 update BMRB 'update entry citation' 2017-12-14 original author 'original release' stop_ _Original_release_date 2017-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The activity of tumor necrosis factor alpha is modulated by dynamic conformational rearrangements ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29192773 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hofmann Daniela . . 2 Salmon Loic . . 3 Wider Gerhard . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 140 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 167 _Page_last 175 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TNF alpha homotrimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TNF alpha homotrimer, subunit 1' $TNF_alpha_homotrimer 'TNF alpha homotrimer, subunit 2' $TNF_alpha_homotrimer 'TNF alpha homotrimer, subunit 3' $TNF_alpha_homotrimer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details homotrimer save_ ######################## # Monomeric polymers # ######################## save_TNF_alpha_homotrimer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TNF_alpha_homotrimer _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details none ############################## # Polymer residue sequence # ############################## _Residue_count 161 _Mol_residue_sequence ; MGSHHHHHHRTPSDKPVAHV VANPQAEGQLQWLNRRANAL LANGVELRDNQLVVPSEGLY LIYSQVLFKGQGCPSTHVLL THTISRIAVSYQTKVNLLSA IKSPCQRETPEGAEAKPWYE PIYLGGVFQLEKGDRLSAEI NRPDYLDFAESGQVYFGIIA L ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 MET 2 -2 GLY 3 -1 SER 4 0 HIS 5 1 HIS 6 2 HIS 7 3 HIS 8 4 HIS 9 5 HIS 10 6 ARG 11 7 THR 12 8 PRO 13 9 SER 14 10 ASP 15 11 LYS 16 12 PRO 17 13 VAL 18 14 ALA 19 15 HIS 20 16 VAL 21 17 VAL 22 18 ALA 23 19 ASN 24 20 PRO 25 21 GLN 26 22 ALA 27 23 GLU 28 24 GLY 29 25 GLN 30 26 LEU 31 27 GLN 32 28 TRP 33 29 LEU 34 30 ASN 35 31 ARG 36 32 ARG 37 33 ALA 38 34 ASN 39 35 ALA 40 36 LEU 41 37 LEU 42 38 ALA 43 39 ASN 44 40 GLY 45 41 VAL 46 42 GLU 47 43 LEU 48 44 ARG 49 45 ASP 50 46 ASN 51 47 GLN 52 48 LEU 53 49 VAL 54 50 VAL 55 51 PRO 56 52 SER 57 53 GLU 58 54 GLY 59 55 LEU 60 56 TYR 61 57 LEU 62 58 ILE 63 59 TYR 64 60 SER 65 61 GLN 66 62 VAL 67 63 LEU 68 64 PHE 69 65 LYS 70 66 GLY 71 67 GLN 72 68 GLY 73 69 CYS 74 70 PRO 75 71 SER 76 72 THR 77 73 HIS 78 74 VAL 79 75 LEU 80 76 LEU 81 77 THR 82 78 HIS 83 79 THR 84 80 ILE 85 81 SER 86 82 ARG 87 83 ILE 88 84 ALA 89 85 VAL 90 86 SER 91 87 TYR 92 88 GLN 93 89 THR 94 90 LYS 95 91 VAL 96 92 ASN 97 93 LEU 98 94 LEU 99 95 SER 100 96 ALA 101 97 ILE 102 98 LYS 103 99 SER 104 100 PRO 105 101 CYS 106 102 GLN 107 103 ARG 108 104 GLU 109 105 THR 110 106 PRO 111 107 GLU 112 108 GLY 113 109 ALA 114 110 GLU 115 111 ALA 116 112 LYS 117 113 PRO 118 114 TRP 119 115 TYR 120 116 GLU 121 117 PRO 122 118 ILE 123 119 TYR 124 120 LEU 125 121 GLY 126 122 GLY 127 123 VAL 128 124 PHE 129 125 GLN 130 126 LEU 131 127 GLU 132 128 LYS 133 129 GLY 134 130 ASP 135 131 ARG 136 132 LEU 137 133 SER 138 134 ALA 139 135 GLU 140 136 ILE 141 137 ASN 142 138 ARG 143 139 PRO 144 140 ASP 145 141 TYR 146 142 LEU 147 143 ASP 148 144 PHE 149 145 ALA 150 146 GLU 151 147 SER 152 148 GLY 153 149 GLN 154 150 VAL 155 151 TYR 156 152 PHE 157 153 GLY 158 154 ILE 159 155 ILE 160 156 ALA 161 157 LEU 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 PDB P01375 1TNF . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TNF_alpha_homotrimer 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 _Vector_name _Details $TNF_alpha_homotrimer 'recombinant technology' . Escherichia coli DE3-RIL pET-23a 'expressed in BL21-codonPlus (DE3)-RIL competent cells' 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 $TNF_alpha_homotrimer 1 mM '[U-13C; U-15N; U-2H]' 'PBS buffer' 100 mM 'natural abundance' NaCl 137 mM 'natural abundance' KCl 2.7 mM 'natural abundance' Na2HPO4 10 mM 'natural abundance' KH2PO4 1.8 mM 'natural abundance' stop_ save_ save_sample_2-7 _Saveframe_category sample _Sample_type solution _Details ; Different mutations of the TNF alpha homotrimer were used to confirm the assignment, these are G121A, Y119S, T89A, T72A, I97A, I155A. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TNF_alpha_homotrimer 0.75 mM 0.5 1.0 '[U-13C; U-15N]' 'PBS buffer' 100 mM . . 'natural abundance' NaCl 137 mM . . 'natural abundance' KCl 2.7 mM . . 'natural abundance' Na2HPO4 10 mM . . 'natural abundance' KH2PO4 1.8 mM . . 'natural abundance' stop_ save_ save_sample_8-11 _Saveframe_category sample _Sample_type solution _Details ; Unlabeling" of the specific amino acids Arg, Lys, Cys and Asn was used to confirm the assignment. In a U-13C; U-15N background [12C,14N]- Arg, Lys, Cys and Asn amino acids were added. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TNF_alpha_homotrimer 0.75 mM 0.5 1.0 '[U-13C; U-15N]' 'PBS buffer' 100 mM . . 'natural abundance' NaCl 137 mM . . 'natural abundance' KCl 2.7 mM . . 'natural abundance' Na2HPO4 10 mM . . 'natural abundance' KH2PO4 1.8 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details ; cara.nmr.ch Switzerland ; save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AVIII HD' _Field_strength 600 _Details 'Cryo Probe head' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVIII _Field_strength 700 _Details 'Cryo Probe head' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AVIII HD' _Field_strength 900 _Details 'Cryo Probe head' save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVIII _Field_strength 500 _Details 'Cryo Probe head' save_ save_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVIII _Field_strength 750 _Details 'PATXI (ATM) probe head' 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_2D_1H-13C_HSQC_aliphatic_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_1 save_ save_2D_TROSY_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_/_TROSY_version_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC / TROSY version' _Sample_label $sample_8-11 save_ save_3D_HNCO_(planes_only)_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO (planes only)' _Sample_label $sample_8-11 save_ save_2D_1H-15N_HSQC_/_TROSY_version_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC / TROSY version' _Sample_label $sample_2-7 save_ save_3D_TROSY_HN(CO)CA_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CA' _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 7.4 . pH pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'DSS in the sample buffer was used as a standard' 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 . 'separate tube (no insert) similar to the experimental sample tube' . 0.2514495 DSS H 1 'methyl protons' ppm 0 external direct . 'separate tube (no insert) similar to the experimental sample tube' . 1 DSS N 15 'methyl protons' ppm 0 external indirect . 'separate tube (no insert) similar to the experimental sample tube' . 0.101329 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 'The abiguity index 6 applies to all assignments as homotrimer, and 5 applies to Tyr 7.' loop_ _Software_label $CARA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC aliphatic' '2D 1H-13C HSQC aromatic' '2D TROSY 1H-15N HSQC' '3D TROSY HNCO' '3D TROSY HN(CA)CO' '3D TROSY HNCACB' '3D TROSY HN(CO)CACB' '3D 1H-15N NOESY' '2D 1H-15N HSQC / TROSY version' '3D HNCO (planes only)' '3D TROSY HN(CO)CA' stop_ loop_ _Sample_label $sample_1 $sample_8-11 $sample_2-7 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'TNF alpha homotrimer, subunit 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 7 11 THR H H 7.965 0.02 . 2 7 11 THR C C 175.136 0.3 . 3 7 11 THR CA C 58.129 0.3 . 4 7 11 THR CB C 69.919 0.3 . 5 7 11 THR N N 117.128 0.3 . 6 9 13 SER H H 8.057 0.02 . 7 9 13 SER C C 174.327 0.3 . 8 9 13 SER CA C 57.613 0.3 . 9 9 13 SER CB C 63.423 0.3 . 10 9 13 SER N N 115.119 0.3 . 11 10 14 ASP H H 8.3 0.02 . 12 10 14 ASP C C 176.178 0.3 . 13 10 14 ASP CA C 53.072 0.3 . 14 10 14 ASP CB C 40.096 0.3 . 15 10 14 ASP N N 124.084 0.3 . 16 11 15 LYS H H 7.847 0.02 . 17 11 15 LYS C C 174.879 0.3 . 18 11 15 LYS CA C 54.197 0.3 . 19 11 15 LYS CB C 31.829 0.3 . 20 11 15 LYS N N 121.852 0.3 . 21 13 17 VAL H H 7.654 0.02 . 22 13 17 VAL C C 171.257 0.3 . 23 13 17 VAL CA C 59.406 0.3 . 24 13 17 VAL CB C 32.932 0.3 . 25 13 17 VAL N N 121.728 0.3 . 26 14 18 ALA H H 9.145 0.02 . 27 14 18 ALA C C 174.655 0.3 . 28 14 18 ALA CA C 50.71 0.3 . 29 14 18 ALA CB C 24.486 0.3 . 30 14 18 ALA N N 126.81 0.3 . 31 15 19 HIS H H 9.109 0.02 . 32 15 19 HIS C C 174.663 0.3 . 33 15 19 HIS CA C 57.892 0.3 . 34 15 19 HIS CB C 31.531 0.3 . 35 15 19 HIS N N 121.71 0.3 . 36 16 20 VAL H H 9.297 0.02 . 37 16 20 VAL C C 174.845 0.3 . 38 16 20 VAL CA C 58.335 0.3 . 39 16 20 VAL CB C 33.539 0.3 . 40 16 20 VAL N N 119.749 0.3 . 41 17 21 VAL H H 8.328 0.02 . 42 17 21 VAL C C 176.178 0.3 . 43 17 21 VAL CA C 58.455 0.3 . 44 17 21 VAL CB C 34.827 0.3 . 45 17 21 VAL N N 110.837 0.3 . 46 18 22 ALA H H 7.203 0.02 . 47 18 22 ALA C C 177.341 0.3 . 48 18 22 ALA CA C 51.802 0.3 . 49 18 22 ALA CB C 18.407 0.3 . 50 18 22 ALA N N 123.708 0.3 . 51 19 23 ASN H H 8.608 0.02 . 52 19 23 ASN C C 175.227 0.3 . 53 19 23 ASN CA C 49.567 0.3 . 54 19 23 ASN CB C 38.487 0.3 . 55 19 23 ASN N N 118.954 0.3 . 56 21 25 GLN H H 7.484 0.02 . 57 21 25 GLN C C 175.766 0.3 . 58 21 25 GLN CA C 54.846 0.3 . 59 21 25 GLN CB C 28.318 0.3 . 60 21 25 GLN N N 115.81 0.3 . 61 22 26 ALA H H 6.972 0.02 . 62 22 26 ALA C C 175.276 0.3 . 63 22 26 ALA CA C 50.511 0.3 . 64 22 26 ALA CB C 17.646 0.3 . 65 22 26 ALA N N 125.128 0.3 . 66 23 27 GLU H H 7.9 0.02 . 67 23 27 GLU C C 177.95 0.3 . 68 23 27 GLU CA C 56.321 0.3 . 69 23 27 GLU CB C 28.935 0.3 . 70 23 27 GLU N N 120.402 0.3 . 71 24 28 GLY H H 8.732 0.02 . 72 24 28 GLY C C 173.016 0.3 . 73 24 28 GLY CA C 45.318 0.3 . 74 24 28 GLY N N 112.418 0.3 . 75 25 29 GLN H H 7.518 0.02 . 76 25 29 GLN C C 172.898 0.3 . 77 25 29 GLN CA C 53.314 0.3 . 78 25 29 GLN CB C 31.994 0.3 . 79 25 29 GLN N N 115.475 0.3 . 80 26 30 LEU H H 8.501 0.02 . 81 26 30 LEU C C 173.828 0.3 . 82 26 30 LEU CA C 52.777 0.3 . 83 26 30 LEU CB C 40.085 0.3 . 84 26 30 LEU N N 123.186 0.3 . 85 27 31 GLN H H 8.669 0.02 . 86 27 31 GLN C C 174.011 0.3 . 87 27 31 GLN CA C 52.923 0.3 . 88 27 31 GLN CB C 30.612 0.3 . 89 27 31 GLN N N 129.876 0.3 . 90 28 32 TRP H H 8.844 0.02 . 91 28 32 TRP C C 176.502 0.3 . 92 28 32 TRP CA C 55.538 0.3 . 93 28 32 TRP CB C 30.687 0.3 . 94 28 32 TRP N N 127.693 0.3 . 95 29 33 LEU H H 9.775 0.02 . 96 29 33 LEU C C 175.707 0.3 . 97 29 33 LEU CA C 54.182 0.3 . 98 29 33 LEU CB C 44.792 0.3 . 99 29 33 LEU N N 121.895 0.3 . 100 30 34 ASN H H 8.455 0.02 . 101 30 34 ASN C C 174.385 0.3 . 102 30 34 ASN CA C 52.093 0.3 . 103 30 34 ASN CB C 39.275 0.3 . 104 30 34 ASN N N 116.685 0.3 . 105 35 39 ALA H H 7.746 0.02 . 106 35 39 ALA C C 176.897 0.3 . 107 35 39 ALA CA C 51.181 0.3 . 108 35 39 ALA CB C 20.918 0.3 . 109 35 39 ALA N N 121.588 0.3 . 110 36 40 LEU H H 9.37 0.02 . 111 36 40 LEU C C 176.113 0.3 . 112 36 40 LEU CA C 54.195 0.3 . 113 36 40 LEU CB C 46.865 0.3 . 114 36 40 LEU N N 122.509 0.3 . 115 37 41 LEU H H 8.221 0.02 . 116 37 41 LEU C C 174.925 0.3 . 117 37 41 LEU CA C 55.774 0.3 . 118 37 41 LEU CB C 42.087 0.3 . 119 37 41 LEU N N 122.544 0.3 . 120 38 42 ALA H H 9.085 0.02 . 121 38 42 ALA C C 177.229 0.3 . 122 38 42 ALA CA C 51.22 0.3 . 123 38 42 ALA CB C 22.367 0.3 . 124 38 42 ALA N N 128.003 0.3 . 125 39 43 ASN H H 8.875 0.02 . 126 39 43 ASN C C 175.065 0.3 . 127 39 43 ASN CA C 53.611 0.3 . 128 39 43 ASN CB C 35.802 0.3 . 129 39 43 ASN N N 114.263 0.3 . 130 40 44 GLY H H 8.348 0.02 . 131 40 44 GLY C C 175.328 0.3 . 132 40 44 GLY CA C 44.472 0.3 . 133 40 44 GLY N N 103.956 0.3 . 134 41 45 VAL H H 6.859 0.02 . 135 41 45 VAL C C 174.5 0.3 . 136 41 45 VAL CA C 63.131 0.3 . 137 41 45 VAL CB C 30.248 0.3 . 138 41 45 VAL N N 120.564 0.3 . 139 42 46 GLU H H 7.451 0.02 . 140 42 46 GLU C C 173.809 0.3 . 141 42 46 GLU CA C 53.804 0.3 . 142 42 46 GLU CB C 32.938 0.3 . 143 42 46 GLU N N 124.734 0.3 . 144 43 47 LEU H H 8.39 0.02 . 145 43 47 LEU C C 175.828 0.3 . 146 43 47 LEU CA C 53.054 0.3 . 147 43 47 LEU CB C 43.102 0.3 . 148 43 47 LEU N N 125.344 0.3 . 149 44 48 ARG H H 9.12 0.02 . 150 44 48 ARG C C 175.742 0.3 . 151 44 48 ARG CA C 54.059 0.3 . 152 44 48 ARG CB C 32.548 0.3 . 153 44 48 ARG N N 126.998 0.3 . 154 45 49 ASP H H 9.384 0.02 . 155 45 49 ASP CA C 55.052 0.3 . 156 45 49 ASP CB C 38.84 0.3 . 157 45 49 ASP N N 126.899 0.3 . 158 46 50 ASN H H 9.227 0.02 . 159 46 50 ASN C C 173.482 0.3 . 160 46 50 ASN CA C 53.757 0.3 . 161 46 50 ASN CB C 40.801 0.3 . 162 46 50 ASN N N 114.094 0.3 . 163 47 51 GLN H H 7.913 0.02 . 164 47 51 GLN C C 175.31 0.3 . 165 47 51 GLN CA C 53.358 0.3 . 166 47 51 GLN CB C 30.458 0.3 . 167 47 51 GLN N N 118.071 0.3 . 168 48 52 LEU H H 8.359 0.02 . 169 48 52 LEU C C 176.466 0.3 . 170 48 52 LEU CA C 52.669 0.3 . 171 48 52 LEU CB C 42.254 0.3 . 172 48 52 LEU N N 120.024 0.3 . 173 49 53 VAL H H 8.805 0.02 . 174 49 53 VAL C C 177.001 0.3 . 175 49 53 VAL CA C 60.444 0.3 . 176 49 53 VAL CB C 32.196 0.3 . 177 49 53 VAL N N 122.591 0.3 . 178 52 56 SER H H 6.685 0.02 . 179 52 56 SER C C 172.895 0.3 . 180 52 56 SER CA C 56.017 0.3 . 181 52 56 SER CB C 64.245 0.3 . 182 52 56 SER N N 111.177 0.3 . 183 53 57 GLU H H 9.243 0.02 . 184 53 57 GLU C C 176.311 0.3 . 185 53 57 GLU CA C 55.065 0.3 . 186 53 57 GLU CB C 28.742 0.3 . 187 53 57 GLU N N 125.976 0.3 . 188 54 58 GLY H H 8.413 0.02 . 189 54 58 GLY C C 171.188 0.3 . 190 54 58 GLY CA C 44.65 0.3 . 191 54 58 GLY N N 110.301 0.3 . 192 55 59 LEU H H 8.301 0.02 . 193 55 59 LEU C C 176.331 0.3 . 194 55 59 LEU CA C 53.282 0.3 . 195 55 59 LEU CB C 41.876 0.3 . 196 55 59 LEU N N 120.904 0.3 . 197 56 60 TYR H H 9.156 0.02 . 198 56 60 TYR C C 175.074 0.3 . 199 56 60 TYR CA C 55.839 0.3 . 200 56 60 TYR CB C 40.525 0.3 . 201 56 60 TYR N N 121.839 0.3 . 202 57 61 LEU H H 8.706 0.02 . 203 57 61 LEU CA C 54.065 0.3 . 204 57 61 LEU CB C 42.002 0.3 . 205 57 61 LEU N N 124.732 0.3 . 206 63 67 LEU H H 5.67 0.02 . 207 63 67 LEU CA C 53.531 0.3 . 208 63 67 LEU CB C 44.097 0.3 . 209 63 67 LEU N N 122.131 0.3 . 210 64 68 PHE H H 8.662 0.02 . 211 64 68 PHE CA C 55.961 0.3 . 212 64 68 PHE CB C 41.482 0.3 . 213 64 68 PHE N N 125.313 0.3 . 214 65 69 LYS H H 9.445 0.02 . 215 65 69 LYS C C 173.896 0.3 . 216 65 69 LYS CA C 53.69 0.3 . 217 65 69 LYS CB C 35.66 0.3 . 218 65 69 LYS N N 124.189 0.3 . 219 66 70 GLY H H 6.095 0.02 . 220 66 70 GLY C C 171.188 0.3 . 221 66 70 GLY CA C 42.759 0.3 . 222 66 70 GLY N N 109.811 0.3 . 223 67 71 GLN H H 8.167 0.02 . 224 67 71 GLN C C 175.362 0.3 . 225 67 71 GLN CA C 54.566 0.3 . 226 67 71 GLN CB C 27.74 0.3 . 227 67 71 GLN N N 119.751 0.3 . 228 68 72 GLY H H 7.78 0.02 . 229 68 72 GLY C C 173.171 0.3 . 230 68 72 GLY CA C 43.938 0.3 . 231 68 72 GLY N N 111.127 0.3 . 232 74 78 VAL H H 7.57 0.02 . 233 74 78 VAL C C 173.85 0.3 . 234 74 78 VAL CA C 61.6 0.3 . 235 74 78 VAL CB C 32.413 0.3 . 236 74 78 VAL N N 126.614 0.3 . 237 75 79 LEU H H 7.739 0.02 . 238 75 79 LEU C C 175.762 0.3 . 239 75 79 LEU CA C 52.81 0.3 . 240 75 79 LEU CB C 42.747 0.3 . 241 75 79 LEU N N 126.459 0.3 . 242 76 80 LEU H H 8.546 0.02 . 243 76 80 LEU C C 174.985 0.3 . 244 76 80 LEU CA C 52.048 0.3 . 245 76 80 LEU CB C 41.17 0.3 . 246 76 80 LEU N N 125.497 0.3 . 247 77 81 THR H H 8.485 0.02 . 248 77 81 THR C C 171.999 0.3 . 249 77 81 THR CA C 59.314 0.3 . 250 77 81 THR CB C 70.495 0.3 . 251 77 81 THR N N 113.314 0.3 . 252 78 82 HIS H H 7.943 0.02 . 253 78 82 HIS C C 174.508 0.3 . 254 78 82 HIS CA C 53.072 0.3 . 255 78 82 HIS CB C 35.627 0.3 . 256 78 82 HIS N N 123.174 0.3 . 257 79 83 THR H H 8.518 0.02 . 258 79 83 THR C C 173.669 0.3 . 259 79 83 THR CA C 60.42 0.3 . 260 79 83 THR CB C 72.675 0.3 . 261 79 83 THR N N 121.314 0.3 . 262 80 84 ILE H H 9.057 0.02 . 263 80 84 ILE CA C 58.812 0.3 . 264 80 84 ILE CB C 37.832 0.3 . 265 80 84 ILE N N 126.693 0.3 . 266 81 85 SER H H 8.992 0.02 . 267 81 85 SER C C 171.256 0.3 . 268 81 85 SER CA C 56.274 0.3 . 269 81 85 SER CB C 65.424 0.3 . 270 81 85 SER N N 123.579 0.3 . 271 82 86 ARG H H 8.867 0.02 . 272 82 86 ARG C C 175.02 0.3 . 273 82 86 ARG CA C 53.142 0.3 . 274 82 86 ARG CB C 33.34 0.3 . 275 82 86 ARG N N 122.185 0.3 . 276 83 87 ILE H H 9.371 0.02 . 277 83 87 ILE C C 175.504 0.3 . 278 83 87 ILE CA C 60.471 0.3 . 279 83 87 ILE CB C 38.032 0.3 . 280 83 87 ILE N N 129.965 0.3 . 281 84 88 ALA H H 8.318 0.02 . 282 84 88 ALA C C 178.329 0.3 . 283 84 88 ALA CA C 50.676 0.3 . 284 84 88 ALA CB C 18.514 0.3 . 285 84 88 ALA N N 132.63 0.3 . 286 85 89 VAL H H 8.613 0.02 . 287 85 89 VAL C C 177.639 0.3 . 288 85 89 VAL CA C 64.52 0.3 . 289 85 89 VAL CB C 30.587 0.3 . 290 85 89 VAL N N 123.557 0.3 . 291 86 90 SER H H 8.351 0.02 . 292 86 90 SER C C 174.614 0.3 . 293 86 90 SER CA C 59.376 0.3 . 294 86 90 SER CB C 62.278 0.3 . 295 86 90 SER N N 115.26 0.3 . 296 87 91 TYR H H 7.405 0.02 . 297 87 91 TYR C C 175.213 0.3 . 298 87 91 TYR CA C 57.282 0.3 . 299 87 91 TYR CB C 38.305 0.3 . 300 87 91 TYR N N 120.016 0.3 . 301 88 92 GLN H H 8.367 0.02 . 302 88 92 GLN C C 175.302 0.3 . 303 88 92 GLN CA C 56.333 0.3 . 304 88 92 GLN CB C 26.204 0.3 . 305 88 92 GLN N N 118.973 0.3 . 306 89 93 THR H H 7.332 0.02 . 307 89 93 THR C C 172.637 0.3 . 308 89 93 THR CA C 60.263 0.3 . 309 89 93 THR CB C 70.389 0.3 . 310 89 93 THR N N 113.528 0.3 . 311 90 94 LYS H H 8.346 0.02 . 312 90 94 LYS C C 175.707 0.3 . 313 90 94 LYS CA C 55.715 0.3 . 314 90 94 LYS CB C 33.157 0.3 . 315 90 94 LYS N N 126.003 0.3 . 316 91 95 VAL H H 8.561 0.02 . 317 91 95 VAL C C 174.914 0.3 . 318 91 95 VAL CA C 59.779 0.3 . 319 91 95 VAL CB C 34.033 0.3 . 320 91 95 VAL N N 125.072 0.3 . 321 92 96 ASN H H 8.845 0.02 . 322 92 96 ASN C C 174.258 0.3 . 323 92 96 ASN CA C 53.048 0.3 . 324 92 96 ASN CB C 36.76 0.3 . 325 92 96 ASN N N 126.034 0.3 . 326 93 97 LEU H H 8.92 0.02 . 327 93 97 LEU C C 175.282 0.3 . 328 93 97 LEU CA C 55.429 0.3 . 329 93 97 LEU CB C 41.07 0.3 . 330 93 97 LEU N N 124.329 0.3 . 331 94 98 LEU H H 7.145 0.02 . 332 94 98 LEU C C 175.362 0.3 . 333 94 98 LEU CA C 52.459 0.3 . 334 94 98 LEU CB C 47.057 0.3 . 335 94 98 LEU N N 116.488 0.3 . 336 95 99 SER H H 8.544 0.02 . 337 95 99 SER C C 172.119 0.3 . 338 95 99 SER CA C 56.862 0.3 . 339 95 99 SER CB C 64.654 0.3 . 340 95 99 SER N N 117.441 0.3 . 341 96 100 ALA H H 8.796 0.02 . 342 96 100 ALA C C 174.204 0.3 . 343 96 100 ALA CA C 51.492 0.3 . 344 96 100 ALA CB C 22.612 0.3 . 345 96 100 ALA N N 123.075 0.3 . 346 98 102 LYS H H 8.877 0.02 . 347 98 102 LYS CA C 53.814 0.3 . 348 98 102 LYS CB C 38.271 0.3 . 349 98 102 LYS N N 122.01 0.3 . 350 99 103 SER H H 8.778 0.02 . 351 99 103 SER CA C 52.322 0.3 . 352 99 103 SER CB C 63.952 0.3 . 353 99 103 SER N N 116.76 0.3 . 354 101 105 CYS H H 8.268 0.02 . 355 101 105 CYS C C 173.807 0.3 . 356 101 105 CYS CA C 55.236 0.3 . 357 101 105 CYS CB C 44.936 0.3 . 358 101 105 CYS N N 117.395 0.3 . 359 103 107 ARG H H 7.748 0.02 . 360 103 107 ARG C C 174.911 0.3 . 361 103 107 ARG CA C 54.712 0.3 . 362 103 107 ARG CB C 31.074 0.3 . 363 103 107 ARG N N 119.043 0.3 . 364 104 108 GLU H H 8.683 0.02 . 365 104 108 GLU C C 176.469 0.3 . 366 104 108 GLU CA C 55.695 0.3 . 367 104 108 GLU CB C 29.424 0.3 . 368 104 108 GLU N N 123.763 0.3 . 369 107 111 GLU H H 8.466 0.02 . 370 107 111 GLU C C 177.674 0.3 . 371 107 111 GLU CA C 57.177 0.3 . 372 107 111 GLU CB C 28.911 0.3 . 373 107 111 GLU N N 122.502 0.3 . 374 108 112 GLY H H 8.599 0.02 . 375 108 112 GLY C C 174.034 0.3 . 376 108 112 GLY CA C 44.797 0.3 . 377 108 112 GLY N N 113.019 0.3 . 378 109 113 ALA H H 7.869 0.02 . 379 109 113 ALA C C 177.38 0.3 . 380 109 113 ALA CA C 51.131 0.3 . 381 109 113 ALA CB C 18.995 0.3 . 382 109 113 ALA N N 124.068 0.3 . 383 110 114 GLU H H 8.339 0.02 . 384 110 114 GLU C C 175.96 0.3 . 385 110 114 GLU CA C 55.736 0.3 . 386 110 114 GLU CB C 29.226 0.3 . 387 110 114 GLU N N 120.543 0.3 . 388 111 115 ALA H H 8.326 0.02 . 389 111 115 ALA C C 176.621 0.3 . 390 111 115 ALA CA C 51.105 0.3 . 391 111 115 ALA CB C 17.81 0.3 . 392 111 115 ALA N N 128.039 0.3 . 393 112 116 LYS H H 8.178 0.02 . 394 112 116 LYS C C 174.5 0.3 . 395 112 116 LYS CA C 52.833 0.3 . 396 112 116 LYS CB C 31.231 0.3 . 397 112 116 LYS N N 123.804 0.3 . 398 114 118 TRP H H 8.072 0.02 . 399 114 118 TRP C C 174.12 0.3 . 400 114 118 TRP CA C 53.098 0.3 . 401 114 118 TRP CB C 31.404 0.3 . 402 114 118 TRP N N 120.114 0.3 . 403 115 119 TYR H H 8.393 0.02 . 404 115 119 TYR C C 176.811 0.3 . 405 115 119 TYR CA C 56.425 0.3 . 406 115 119 TYR CB C 43.218 0.3 . 407 115 119 TYR N N 117.354 0.3 . 408 116 120 GLU H H 9.51 0.02 . 409 116 120 GLU C C 174.97 0.3 . 410 116 120 GLU CA C 51.777 0.3 . 411 116 120 GLU CB C 33.427 0.3 . 412 116 120 GLU N N 118.958 0.3 . 413 118 122 ILE H H 8.85 0.02 . 414 118 122 ILE C C 172.64 0.3 . 415 118 122 ILE CA C 62.434 0.3 . 416 118 122 ILE CB C 40.525 0.3 . 417 118 122 ILE N N 122.288 0.3 . 418 119 123 TYR H H 8.296 0.02 . 419 119 123 TYR C C 172.952 0.3 . 420 119 123 TYR CA C 57.216 0.3 . 421 119 123 TYR CB C 41.874 0.3 . 422 119 123 TYR N N 129.422 0.3 . 423 120 124 LEU H H 7.961 0.02 . 424 120 124 LEU CA C 52.401 0.3 . 425 120 124 LEU CB C 45.394 0.3 . 426 120 124 LEU N N 125.251 0.3 . 427 121 125 GLY H H 7.099 0.02 . 428 121 125 GLY CA C 46.151 0.3 . 429 121 125 GLY N N 105.33 0.3 . 430 122 126 GLY H H 8.736 0.02 . 431 122 126 GLY C C 181.142 0.3 . 432 122 126 GLY CA C 45.927 0.3 . 433 122 126 GLY N N 108.791 0.3 . 434 124 128 PHE H H 8.527 0.02 . 435 124 128 PHE CA C 55.529 0.3 . 436 124 128 PHE CB C 42.578 0.3 . 437 124 128 PHE N N 119.554 0.3 . 438 125 129 GLN H H 9.054 0.02 . 439 125 129 GLN C C 175.103 0.3 . 440 125 129 GLN CA C 54.972 0.3 . 441 125 129 GLN CB C 27.664 0.3 . 442 125 129 GLN N N 123.876 0.3 . 443 126 130 LEU H H 8.99 0.02 . 444 126 130 LEU C C 175.725 0.3 . 445 126 130 LEU CA C 52.29 0.3 . 446 126 130 LEU CB C 43.758 0.3 . 447 126 130 LEU N N 128.505 0.3 . 448 127 131 GLU H H 8.648 0.02 . 449 127 131 GLU C C 175.405 0.3 . 450 127 131 GLU CA C 54.015 0.3 . 451 127 131 GLU CB C 30.951 0.3 . 452 127 131 GLU N N 121.034 0.3 . 453 128 132 LYS H H 8.226 0.02 . 454 128 132 LYS C C 177.363 0.3 . 455 128 132 LYS CA C 58.101 0.3 . 456 128 132 LYS CB C 31.319 0.3 . 457 128 132 LYS N N 120.549 0.3 . 458 129 133 GLY H H 8.552 0.02 . 459 129 133 GLY C C 174.429 0.3 . 460 129 133 GLY CA C 44.52 0.3 . 461 129 133 GLY N N 116.152 0.3 . 462 130 134 ASP H H 7.99 0.02 . 463 130 134 ASP C C 174.551 0.3 . 464 130 134 ASP CA C 55.377 0.3 . 465 130 134 ASP CB C 40.984 0.3 . 466 130 134 ASP N N 123.145 0.3 . 467 131 135 ARG H H 8.127 0.02 . 468 131 135 ARG C C 175.862 0.3 . 469 131 135 ARG CA C 53.098 0.3 . 470 131 135 ARG CB C 32.4 0.3 . 471 131 135 ARG N N 117.157 0.3 . 472 132 136 LEU H H 9.351 0.02 . 473 132 136 LEU C C 175.729 0.3 . 474 132 136 LEU CA C 51.855 0.3 . 475 132 136 LEU CB C 44.749 0.3 . 476 132 136 LEU N N 123.192 0.3 . 477 133 137 SER H H 8.55 0.02 . 478 133 137 SER C C 172.169 0.3 . 479 133 137 SER CA C 55.03 0.3 . 480 133 137 SER CB C 65.751 0.3 . 481 133 137 SER N N 116.423 0.3 . 482 134 138 ALA H H 8.49 0.02 . 483 134 138 ALA C C 175.718 0.3 . 484 134 138 ALA CA C 50.388 0.3 . 485 134 138 ALA CB C 17.301 0.3 . 486 134 138 ALA N N 129.604 0.3 . 487 135 139 GLU H H 8.785 0.02 . 488 135 139 GLU C C 175.293 0.3 . 489 135 139 GLU CA C 54.455 0.3 . 490 135 139 GLU CB C 33.653 0.3 . 491 135 139 GLU N N 121.397 0.3 . 492 136 140 ILE H H 8.288 0.02 . 493 136 140 ILE C C 175.811 0.3 . 494 136 140 ILE CA C 57.797 0.3 . 495 136 140 ILE CB C 40.348 0.3 . 496 136 140 ILE N N 116.285 0.3 . 497 137 141 ASN H H 8.371 0.02 . 498 137 141 ASN C C 176.777 0.3 . 499 137 141 ASN CA C 53.952 0.3 . 500 137 141 ASN CB C 37.256 0.3 . 501 137 141 ASN N N 118.507 0.3 . 502 138 142 ARG H H 6.556 0.02 . 503 138 142 ARG C C 173.689 0.3 . 504 138 142 ARG CA C 50.008 0.3 . 505 138 142 ARG CB C 28.99 0.3 . 506 138 142 ARG N N 118.909 0.3 . 507 140 144 ASP H H 9.433 0.02 . 508 140 144 ASP C C 176.57 0.3 . 509 140 144 ASP CA C 54.266 0.3 . 510 140 144 ASP CB C 37.055 0.3 . 511 140 144 ASP N N 115.601 0.3 . 512 141 145 TYR H H 7.607 0.02 . 513 141 145 TYR C C 175.155 0.3 . 514 141 145 TYR CA C 55.952 0.3 . 515 141 145 TYR CB C 39.087 0.3 . 516 141 145 TYR N N 117.716 0.3 . 517 142 146 LEU H H 7.28 0.02 . 518 142 146 LEU C C 176.259 0.3 . 519 142 146 LEU CA C 55.378 0.3 . 520 142 146 LEU CB C 42.547 0.3 . 521 142 146 LEU N N 122.567 0.3 . 522 143 147 ASP H H 8.347 0.02 . 523 143 147 ASP C C 174.728 0.3 . 524 143 147 ASP CA C 52.904 0.3 . 525 143 147 ASP CB C 42.45 0.3 . 526 143 147 ASP N N 124.225 0.3 . 527 144 148 PHE H H 7.885 0.02 . 528 144 148 PHE C C 176.26 0.3 . 529 144 148 PHE CA C 54.7 0.3 . 530 144 148 PHE CB C 37.679 0.3 . 531 144 148 PHE N N 121.417 0.3 . 532 145 149 ALA H H 8.06 0.02 . 533 145 149 ALA C C 178.175 0.3 . 534 145 149 ALA CA C 54.49 0.3 . 535 145 149 ALA CB C 18.445 0.3 . 536 145 149 ALA N N 123.796 0.3 . 537 146 150 GLU H H 7.374 0.02 . 538 146 150 GLU C C 176.596 0.3 . 539 146 150 GLU CA C 53.645 0.3 . 540 146 150 GLU CB C 30.372 0.3 . 541 146 150 GLU N N 115.677 0.3 . 542 147 151 SER H H 8.598 0.02 . 543 147 151 SER C C 175.31 0.3 . 544 147 151 SER CA C 59.539 0.3 . 545 147 151 SER CB C 63.11 0.3 . 546 147 151 SER N N 118.915 0.3 . 547 148 152 GLY H H 8.713 0.02 . 548 148 152 GLY C C 174.189 0.3 . 549 148 152 GLY CA C 45.484 0.3 . 550 148 152 GLY N N 110.977 0.3 . 551 149 153 GLN H H 7.754 0.02 . 552 149 153 GLN C C 175.733 0.3 . 553 149 153 GLN CA C 56.186 0.3 . 554 149 153 GLN CB C 28.887 0.3 . 555 149 153 GLN N N 116.545 0.3 . 556 150 154 VAL H H 7.681 0.02 . 557 150 154 VAL C C 176.328 0.3 . 558 150 154 VAL CA C 60.514 0.3 . 559 150 154 VAL CB C 33.063 0.3 . 560 150 154 VAL N N 117.961 0.3 . 561 151 155 TYR H H 9.117 0.02 . 562 151 155 TYR C C 174.406 0.3 . 563 151 155 TYR CA C 56.382 0.3 . 564 151 155 TYR CB C 40.21 0.3 . 565 151 155 TYR N N 124.988 0.3 . 566 152 156 PHE H H 8.495 0.02 . 567 152 156 PHE C C 171.443 0.3 . 568 152 156 PHE CA C 52.818 0.3 . 569 152 156 PHE CB C 38.815 0.3 . 570 152 156 PHE N N 126.738 0.3 . 571 153 157 GLY H H 8.661 0.02 . 572 153 157 GLY C C 170.686 0.3 . 573 153 157 GLY CA C 45.085 0.3 . 574 153 157 GLY N N 117.085 0.3 . 575 154 158 ILE H H 8.52 0.02 . 576 154 158 ILE C C 174.308 0.3 . 577 154 158 ILE CA C 57.43 0.3 . 578 154 158 ILE CB C 42.002 0.3 . 579 154 158 ILE N N 109.975 0.3 . 580 155 159 ILE H H 8.747 0.02 . 581 155 159 ILE C C 173.268 0.3 . 582 155 159 ILE CA C 59.247 0.3 . 583 155 159 ILE CB C 39.25 0.3 . 584 155 159 ILE N N 118.002 0.3 . 585 156 160 ALA H H 7.746 0.02 . 586 156 160 ALA C C 175.572 0.3 . 587 156 160 ALA CA C 51.479 0.3 . 588 156 160 ALA CB C 19.074 0.3 . 589 156 160 ALA N N 130.765 0.3 . 590 157 161 LEU H H 7.845 0.02 . 591 157 161 LEU C C 175.608 0.3 . 592 157 161 LEU CA C 54.706 0.3 . 593 157 161 LEU CB C 42.748 0.3 . 594 157 161 LEU N N 128.55 0.3 . stop_ save_