data_26528 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; UBCH10 in complex with WHB ; _BMRB_accession_number 26528 _BMRB_flat_file_name bmr26528.str _Entry_type original _Submission_date 2015-03-02 _Accession_date 2015-03-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Grace Christy R. . 2 Brown Nicholas G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 136 "13C chemical shifts" 367 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-12-21 update BMRB 'update entry citation' 2015-06-17 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26526 UBCH10 26527 WHB 26529 'WHB in complex with UBCH10' stop_ _Original_release_date 2015-06-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25825779 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brown Nicholas G. . 2 VanderLinden Ryan . . 3 Watson Edmond R. . 4 Qiao Renping . . 5 Grace Christy R. . 6 Yamaguchi Masaya . . 7 Weissmann Florian . . 8 Frye Jeremiah J. . 9 Dube Prakash . . 10 Cho Shein E. . 11 Actis Marcelo L. . 12 Rodrigues Patrick . . 13 Fujii Naoaki . . 14 Peters Jan-Michael . . 15 Stark Holger . . 16 Schulman Brenda A. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_name_full 112 _Journal_volume 17 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5272 _Page_last 5279 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'UBCH10 in complex with WHB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Molecule_3 $Molecule_3 WHB $Molecule_1 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_Molecule_3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Molecule_3 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 187 _Mol_residue_sequence ; MASQNRDPAATSVAAARKGA EPSGGGARGPVGKRLQQELM TLMMSGDKGISAFPESDNLF KWVGTIHGAAGTVYEDLRYK LSLEFPSGYPYNAPTVKFLT PCYHPNVDTQGNISLDILKE KWSALYDVRTILLSIQSLLG EPNIDSPLNTHAAELWKNPT AFKKYLQETYSKQVTSQEPG SHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 SER 4 4 GLN 5 5 ASN 6 6 ARG 7 7 ASP 8 8 PRO 9 9 ALA 10 10 ALA 11 11 THR 12 12 SER 13 13 VAL 14 14 ALA 15 15 ALA 16 16 ALA 17 17 ARG 18 18 LYS 19 19 GLY 20 20 ALA 21 21 GLU 22 22 PRO 23 23 SER 24 24 GLY 25 25 GLY 26 26 GLY 27 27 ALA 28 28 ARG 29 29 GLY 30 30 PRO 31 31 VAL 32 32 GLY 33 33 LYS 34 34 ARG 35 35 LEU 36 36 GLN 37 37 GLN 38 38 GLU 39 39 LEU 40 40 MET 41 41 THR 42 42 LEU 43 43 MET 44 44 MET 45 45 SER 46 46 GLY 47 47 ASP 48 48 LYS 49 49 GLY 50 50 ILE 51 51 SER 52 52 ALA 53 53 PHE 54 54 PRO 55 55 GLU 56 56 SER 57 57 ASP 58 58 ASN 59 59 LEU 60 60 PHE 61 61 LYS 62 62 TRP 63 63 VAL 64 64 GLY 65 65 THR 66 66 ILE 67 67 HIS 68 68 GLY 69 69 ALA 70 70 ALA 71 71 GLY 72 72 THR 73 73 VAL 74 74 TYR 75 75 GLU 76 76 ASP 77 77 LEU 78 78 ARG 79 79 TYR 80 80 LYS 81 81 LEU 82 82 SER 83 83 LEU 84 84 GLU 85 85 PHE 86 86 PRO 87 87 SER 88 88 GLY 89 89 TYR 90 90 PRO 91 91 TYR 92 92 ASN 93 93 ALA 94 94 PRO 95 95 THR 96 96 VAL 97 97 LYS 98 98 PHE 99 99 LEU 100 100 THR 101 101 PRO 102 102 CYS 103 103 TYR 104 104 HIS 105 105 PRO 106 106 ASN 107 107 VAL 108 108 ASP 109 109 THR 110 110 GLN 111 111 GLY 112 112 ASN 113 113 ILE 114 114 SER 115 115 LEU 116 116 ASP 117 117 ILE 118 118 LEU 119 119 LYS 120 120 GLU 121 121 LYS 122 122 TRP 123 123 SER 124 124 ALA 125 125 LEU 126 126 TYR 127 127 ASP 128 128 VAL 129 129 ARG 130 130 THR 131 131 ILE 132 132 LEU 133 133 LEU 134 134 SER 135 135 ILE 136 136 GLN 137 137 SER 138 138 LEU 139 139 LEU 140 140 GLY 141 141 GLU 142 142 PRO 143 143 ASN 144 144 ILE 145 145 ASP 146 146 SER 147 147 PRO 148 148 LEU 149 149 ASN 150 150 THR 151 151 HIS 152 152 ALA 153 153 ALA 154 154 GLU 155 155 LEU 156 156 TRP 157 157 LYS 158 158 ASN 159 159 PRO 160 160 THR 161 161 ALA 162 162 PHE 163 163 LYS 164 164 LYS 165 165 TYR 166 166 LEU 167 167 GLN 168 168 GLU 169 169 THR 170 170 TYR 171 171 SER 172 172 LYS 173 173 GLN 174 174 VAL 175 175 THR 176 176 SER 177 177 GLN 178 178 GLU 179 179 PRO 180 180 GLY 181 181 SER 182 182 HIS 183 183 HIS 184 184 HIS 185 185 HIS 186 186 HIS 187 187 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_Molecule_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Molecule_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 90 _Mol_residue_sequence ; GSESDSGMASQADQKEEELL LFWTYIQAMLTNLESLSLDR IYNMLRMFVVTGPALAEIDL QELQGYLQKKVRDQQLVYSA GVYRLPKNCS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 SER 3 3 GLU 4 4 SER 5 5 ASP 6 6 SER 7 7 GLY 8 8 MET 9 9 ALA 10 10 SER 11 11 GLN 12 12 ALA 13 13 ASP 14 14 GLN 15 15 LYS 16 16 GLU 17 17 GLU 18 18 GLU 19 19 LEU 20 20 LEU 21 21 LEU 22 22 PHE 23 23 TRP 24 24 THR 25 25 TYR 26 26 ILE 27 27 GLN 28 28 ALA 29 29 MET 30 30 LEU 31 31 THR 32 32 ASN 33 33 LEU 34 34 GLU 35 35 SER 36 36 LEU 37 37 SER 38 38 LEU 39 39 ASP 40 40 ARG 41 41 ILE 42 42 TYR 43 43 ASN 44 44 MET 45 45 LEU 46 46 ARG 47 47 MET 48 48 PHE 49 49 VAL 50 50 VAL 51 51 THR 52 52 GLY 53 53 PRO 54 54 ALA 55 55 LEU 56 56 ALA 57 57 GLU 58 58 ILE 59 59 ASP 60 60 LEU 61 61 GLN 62 62 GLU 63 63 LEU 64 64 GLN 65 65 GLY 66 66 TYR 67 67 LEU 68 68 GLN 69 69 LYS 70 70 LYS 71 71 VAL 72 72 ARG 73 73 ASP 74 74 GLN 75 75 GLN 76 76 LEU 77 77 VAL 78 78 TYR 79 79 SER 80 80 ALA 81 81 GLY 82 82 VAL 83 83 TYR 84 84 ARG 85 85 LEU 86 86 PRO 87 87 LYS 88 88 ASN 89 89 CYS 90 90 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Molecule_3 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 $Molecule_3 'recombinant technology' . Escherichia coli . PRSF1B 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 $Molecule_3 0.5 mM '[U-13C; U-15N; U-2H]' $Molecule_1 0.6 mM 'natural abundance' DTT 0.01 mM 'natural abundance' 'sodium chloride' 0.1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . 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 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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' 200 . mM pH 6.0 . 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 . 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 . 'separate tube (no insert) similar to the experimental sample tube' . 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 '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' 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 Molecule_3 _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 26 26 GLY H H 8.469 0.020 1 2 26 26 GLY C C 174.662 0.3 1 3 26 26 GLY CA C 45.446 0.3 1 4 26 26 GLY N N 110.388 0.3 1 5 27 27 ALA H H 8.239 0.020 1 6 27 27 ALA C C 177.814 0.3 1 7 27 27 ALA CA C 53.115 0.3 1 8 27 27 ALA CB C 18.822 0.3 1 9 27 27 ALA N N 124.747 0.3 1 10 28 28 ARG H H 8.242 0.020 1 11 28 28 ARG C C 177.088 0.3 1 12 28 28 ARG CA C 56.287 0.3 1 13 28 28 ARG CB C 30.253 0.3 1 14 28 28 ARG N N 119.175 0.3 1 15 29 29 GLY H H 8.109 0.020 1 16 29 29 GLY C C 172.999 0.3 1 17 29 29 GLY CA C 45.696 0.3 1 18 29 29 GLY N N 109.868 0.3 1 19 31 31 VAL H H 8.241 0.020 1 20 31 31 VAL C C 177.566 0.3 1 21 31 31 VAL CA C 66.371 0.3 1 22 31 31 VAL CB C 31.250 0.3 1 23 31 31 VAL N N 120.975 0.3 1 24 32 32 GLY H H 8.067 0.020 1 25 32 32 GLY C C 175.786 0.3 1 26 32 32 GLY CA C 47.590 0.3 1 27 32 32 GLY N N 109.305 0.3 1 28 33 33 LYS H H 7.897 0.020 1 29 33 33 LYS C C 179.276 0.3 1 30 33 33 LYS CA C 59.486 0.3 1 31 33 33 LYS CB C 31.914 0.3 1 32 33 33 LYS N N 120.762 0.3 1 33 34 34 ARG H H 7.536 0.020 1 34 34 34 ARG C C 178.339 0.3 1 35 34 34 ARG CA C 59.053 0.3 1 36 34 34 ARG CB C 28.925 0.3 1 37 34 34 ARG N N 121.150 0.3 1 38 35 35 LEU H H 8.330 0.020 1 39 35 35 LEU C C 179.276 0.3 1 40 35 35 LEU CA C 58.553 0.3 1 41 35 35 LEU CB C 41.279 0.3 1 42 35 35 LEU N N 120.932 0.3 1 43 36 36 GLN H H 8.244 0.020 1 44 36 36 GLN C C 178.620 0.3 1 45 36 36 GLN CA C 59.925 0.3 1 46 36 36 GLN CB C 28.521 0.3 1 47 36 36 GLN N N 119.076 0.3 1 48 37 37 GLN H H 7.844 0.020 1 49 37 37 GLN C C 179.065 0.3 1 50 37 37 GLN CA C 59.105 0.3 1 51 37 37 GLN CB C 28.079 0.3 1 52 37 37 GLN N N 121.771 0.3 1 53 38 38 GLU H H 8.862 0.020 1 54 38 38 GLU C C 180.742 0.3 1 55 38 38 GLU CA C 60.987 0.3 1 56 38 38 GLU CB C 28.762 0.3 1 57 38 38 GLU N N 122.106 0.3 1 58 39 39 LEU H H 8.312 0.020 1 59 39 39 LEU C C 178.292 0.3 1 60 39 39 LEU CA C 58.023 0.3 1 61 39 39 LEU CB C 40.273 0.3 1 62 39 39 LEU N N 121.810 0.3 1 63 40 40 MET H H 7.492 0.020 1 64 40 40 MET C C 178.527 0.3 1 65 40 40 MET CA C 59.486 0.3 1 66 40 40 MET CB C 31.379 0.3 1 67 40 40 MET N N 119.964 0.3 1 68 41 41 THR H H 8.632 0.020 1 69 41 41 THR C C 177.379 0.3 1 70 41 41 THR CA C 66.679 0.3 1 71 41 41 THR CB C 68.402 0.3 1 72 41 41 THR N N 116.623 0.3 1 73 42 42 LEU H H 7.932 0.020 1 74 42 42 LEU C C 179.258 0.3 1 75 42 42 LEU CA C 58.859 0.3 1 76 42 42 LEU CB C 41.611 0.3 1 77 42 42 LEU N N 124.201 0.3 1 78 43 43 MET H H 8.454 0.020 1 79 43 43 MET C C 178.714 0.3 1 80 43 43 MET CA C 57.500 0.3 1 81 43 43 MET CB C 33.362 0.3 1 82 43 43 MET N N 118.267 0.3 1 83 44 44 MET H H 7.986 0.020 1 84 44 44 MET C C 177.894 0.3 1 85 44 44 MET CA C 55.933 0.3 1 86 44 44 MET CB C 32.289 0.3 1 87 44 44 MET N N 114.780 0.3 1 88 45 45 SER H H 7.520 0.020 1 89 45 45 SER C C 175.435 0.3 1 90 45 45 SER CA C 61.889 0.3 1 91 45 45 SER CB C 63.648 0.3 1 92 45 45 SER N N 115.286 0.3 1 93 46 46 GLY H H 7.716 0.020 1 94 46 46 GLY C C 174.920 0.3 1 95 46 46 GLY CA C 47.086 0.3 1 96 46 46 GLY N N 108.994 0.3 1 97 47 47 ASP H H 8.046 0.020 1 98 47 47 ASP C C 176.208 0.3 1 99 47 47 ASP CA C 55.264 0.3 1 100 47 47 ASP CB C 42.017 0.3 1 101 47 47 ASP N N 119.384 0.3 1 102 48 48 LYS H H 8.600 0.020 1 103 48 48 LYS C C 178.433 0.3 1 104 48 48 LYS CA C 56.915 0.3 1 105 48 48 LYS CB C 32.146 0.3 1 106 48 48 LYS N N 122.834 0.3 1 107 49 49 GLY H H 8.698 0.020 1 108 49 49 GLY C C 172.718 0.3 1 109 49 49 GLY CA C 46.331 0.3 1 110 49 49 GLY N N 111.673 0.3 1 111 50 50 ILE H H 6.796 0.020 1 112 50 50 ILE C C 174.793 0.3 1 113 50 50 ILE CA C 59.237 0.3 1 114 50 50 ILE CB C 41.611 0.3 1 115 50 50 ILE N N 109.857 0.3 1 116 51 51 SER H H 7.985 0.020 1 117 51 51 SER C C 172.297 0.3 1 118 51 51 SER CA C 58.253 0.3 1 119 51 51 SER CB C 64.593 0.3 1 120 51 51 SER N N 114.875 0.3 1 121 52 52 ALA H H 7.389 0.020 1 122 52 52 ALA C C 173.023 0.3 1 123 52 52 ALA CA C 52.820 0.3 1 124 52 52 ALA CB C 21.920 0.3 1 125 52 52 ALA N N 122.190 0.3 1 126 53 53 PHE H H 8.806 0.020 1 127 53 53 PHE C C 172.275 0.3 1 128 53 53 PHE CA C 58.097 0.3 1 129 53 53 PHE CB C 42.616 0.3 1 130 53 53 PHE N N 116.739 0.3 1 131 55 55 GLU H H 8.394 0.020 1 132 55 55 GLU CA C 57.798 0.3 1 133 55 55 GLU N N 119.650 0.3 1 134 56 56 SER H H 8.466 0.020 1 135 56 56 SER CA C 58.595 0.3 1 136 56 56 SER N N 113.384 0.3 1 137 57 57 ASP H H 8.413 0.020 1 138 57 57 ASP C C 175.402 0.3 1 139 57 57 ASP CA C 54.268 0.3 1 140 57 57 ASP CB C 40.993 0.3 1 141 57 57 ASP N N 118.865 0.3 1 142 58 58 ASN H H 8.129 0.020 1 143 58 58 ASN C C 173.725 0.3 1 144 58 58 ASN CA C 52.646 0.3 1 145 58 58 ASN CB C 38.397 0.3 1 146 58 58 ASN N N 117.507 0.3 1 147 59 59 LEU H H 8.467 0.020 1 148 59 59 LEU CA C 56.386 0.3 1 149 59 59 LEU CB C 41.463 0.3 1 150 59 59 LEU N N 122.377 0.3 1 151 60 60 PHE H H 8.023 0.020 1 152 60 60 PHE C C 175.203 0.3 1 153 60 60 PHE CA C 58.497 0.3 1 154 60 60 PHE CB C 37.813 0.3 1 155 60 60 PHE N N 113.392 0.3 1 156 61 61 LYS H H 7.550 0.020 1 157 61 61 LYS CA C 56.860 0.3 1 158 61 61 LYS CB C 35.356 0.3 1 159 61 61 LYS N N 121.854 0.3 1 160 62 62 TRP H H 9.818 0.020 1 161 62 62 TRP C C 176.184 0.3 1 162 62 62 TRP CA C 54.631 0.3 1 163 62 62 TRP CB C 32.602 0.3 1 164 62 62 TRP N N 126.148 0.3 1 165 63 63 VAL H H 8.748 0.020 1 166 63 63 VAL C C 176.432 0.3 1 167 63 63 VAL CA C 61.299 0.3 1 168 63 63 VAL CB C 33.831 0.3 1 169 63 63 VAL N N 122.557 0.3 1 170 64 64 GLY H H 8.997 0.020 1 171 64 64 GLY CA C 43.603 0.3 1 172 64 64 GLY N N 111.543 0.3 1 173 65 65 THR H H 8.709 0.020 1 174 65 65 THR C C 173.772 0.3 1 175 65 65 THR CA C 62.203 0.3 1 176 65 65 THR CB C 71.481 0.3 1 177 65 65 THR N N 116.490 0.3 1 178 66 66 ILE H H 8.894 0.020 1 179 66 66 ILE C C 174.572 0.3 1 180 66 66 ILE CA C 58.985 0.3 1 181 66 66 ILE CB C 41.577 0.3 1 182 66 66 ILE N N 121.722 0.3 1 183 68 68 GLY H H 8.282 0.020 1 184 68 68 GLY C C 173.468 0.3 1 185 68 68 GLY CA C 45.414 0.3 1 186 68 68 GLY N N 111.291 0.3 1 187 69 69 ALA H H 7.955 0.020 1 188 69 69 ALA CA C 52.088 0.3 1 189 69 69 ALA CB C 19.191 0.3 1 190 69 69 ALA N N 124.011 0.3 1 191 70 70 ALA H H 8.561 0.020 1 192 70 70 ALA C C 178.808 0.3 1 193 70 70 ALA CA C 53.442 0.3 1 194 70 70 ALA CB C 18.027 0.3 1 195 70 70 ALA N N 125.379 0.3 1 196 71 71 GLY H H 9.034 0.020 1 197 71 71 GLY C C 174.498 0.3 1 198 71 71 GLY CA C 45.575 0.3 1 199 71 71 GLY N N 111.051 0.3 1 200 72 72 THR H H 7.538 0.020 1 201 72 72 THR C C 177.566 0.3 1 202 72 72 THR CA C 60.761 0.3 1 203 72 72 THR CB C 73.999 0.3 1 204 72 72 THR N N 109.202 0.3 1 205 73 73 VAL H H 9.058 0.020 1 206 73 73 VAL C C 174.756 0.3 1 207 73 73 VAL CA C 64.592 0.3 1 208 73 73 VAL CB C 31.581 0.3 1 209 73 73 VAL N N 117.111 0.3 1 210 74 74 TYR H H 6.937 0.020 1 211 74 74 TYR C C 176.983 0.3 1 212 74 74 TYR CA C 58.450 0.3 1 213 74 74 TYR CB C 39.029 0.3 1 214 74 74 TYR N N 114.390 0.3 1 215 79 79 TYR H H 9.013 0.020 1 216 79 79 TYR C C 173.784 0.3 1 217 79 79 TYR CA C 58.219 0.3 1 218 79 79 TYR CB C 42.957 0.3 1 219 79 79 TYR N N 122.971 0.3 1 220 80 80 LYS H H 8.856 0.020 1 221 80 80 LYS C C 176.643 0.3 1 222 80 80 LYS CA C 54.143 0.3 1 223 80 80 LYS CB C 33.572 0.3 1 224 80 80 LYS N N 120.585 0.3 1 225 81 81 LEU H H 9.320 0.020 1 226 81 81 LEU C C 174.685 0.3 1 227 81 81 LEU CA C 54.481 0.3 1 228 81 81 LEU CB C 45.814 0.3 1 229 81 81 LEU N N 123.832 0.3 1 230 82 82 SER H H 9.067 0.020 1 231 82 82 SER CA C 56.198 0.3 1 232 82 82 SER CB C 65.173 0.3 1 233 82 82 SER N N 114.644 0.3 1 234 83 83 LEU H H 8.181 0.020 1 235 83 83 LEU CA C 55.258 0.3 1 236 83 83 LEU CB C 43.381 0.3 1 237 83 83 LEU N N 123.132 0.3 1 238 84 84 GLU H H 8.216 0.020 1 239 84 84 GLU C C 174.442 0.3 1 240 84 84 GLU CA C 54.368 0.3 1 241 84 84 GLU CB C 32.097 0.3 1 242 84 84 GLU N N 122.278 0.3 1 243 85 85 PHE H H 8.488 0.020 1 244 85 85 PHE CA C 55.606 0.3 1 245 85 85 PHE CB C 39.029 0.3 1 246 85 85 PHE N N 125.390 0.3 1 247 87 87 SER H H 8.556 0.020 1 248 87 87 SER CA C 61.375 0.3 1 249 87 87 SER CB C 62.850 0.3 1 250 87 87 SER N N 114.915 0.3 1 251 88 88 GLY H H 8.167 0.020 1 252 88 88 GLY C C 175.361 0.3 1 253 88 88 GLY CA C 45.104 0.3 1 254 88 88 GLY N N 109.022 0.3 1 255 89 89 TYR H H 7.754 0.020 1 256 89 89 TYR C C 175.004 0.3 1 257 89 89 TYR CA C 57.766 0.3 1 258 89 89 TYR CB C 38.846 0.3 1 259 89 89 TYR N N 126.044 0.3 1 260 91 91 TYR H H 8.075 0.020 1 261 91 91 TYR C C 176.161 0.3 1 262 91 91 TYR CA C 61.109 0.3 1 263 91 91 TYR CB C 36.522 0.3 1 264 91 91 TYR N N 125.608 0.3 1 265 92 92 ASN H H 7.058 0.020 1 266 92 92 ASN C C 171.969 0.3 1 267 92 92 ASN CA C 51.566 0.3 1 268 92 92 ASN CB C 41.501 0.3 1 269 92 92 ASN N N 115.899 0.3 1 270 93 93 ALA H H 7.272 0.020 1 271 93 93 ALA C C 175.191 0.3 1 272 93 93 ALA CA C 49.640 0.3 1 273 93 93 ALA CB C 17.875 0.3 1 274 93 93 ALA N N 121.470 0.3 1 275 95 95 THR H H 8.211 0.020 1 276 95 95 THR C C 174.418 0.3 1 277 95 95 THR CA C 61.863 0.3 1 278 95 95 THR CB C 69.681 0.3 1 279 95 95 THR N N 116.430 0.3 1 280 96 96 VAL H H 8.818 0.020 1 281 96 96 VAL C C 173.435 0.3 1 282 96 96 VAL CA C 60.355 0.3 1 283 96 96 VAL CB C 32.834 0.3 1 284 96 96 VAL N N 131.375 0.3 1 285 97 97 LYS H H 8.068 0.020 1 286 97 97 LYS C C 176.222 0.3 1 287 97 97 LYS CA C 54.248 0.3 1 288 97 97 LYS CB C 36.301 0.3 1 289 97 97 LYS N N 123.558 0.3 1 290 98 98 PHE H H 9.419 0.020 1 291 98 98 PHE C C 176.676 0.3 1 292 98 98 PHE CA C 60.683 0.3 1 293 98 98 PHE CB C 38.806 0.3 1 294 98 98 PHE N N 121.095 0.3 1 295 99 99 LEU H H 9.236 0.020 1 296 99 99 LEU C C 178.283 0.3 1 297 99 99 LEU CA C 55.574 0.3 1 298 99 99 LEU CB C 42.420 0.3 1 299 99 99 LEU N N 125.635 0.3 1 300 100 100 THR H H 7.576 0.020 1 301 100 100 THR C C 171.875 0.3 1 302 100 100 THR CA C 60.169 0.3 1 303 100 100 THR CB C 70.626 0.3 1 304 100 100 THR N N 118.713 0.3 1 305 102 102 CYS H H 8.292 0.020 1 306 102 102 CYS C C 172.966 0.3 1 307 102 102 CYS CA C 57.865 0.3 1 308 102 102 CYS CB C 28.483 0.3 1 309 102 102 CYS N N 126.308 0.3 1 310 103 103 TYR H H 7.929 0.020 1 311 103 103 TYR CA C 58.352 0.3 1 312 103 103 TYR CB C 37.628 0.3 1 313 103 103 TYR N N 133.030 0.3 1 314 104 104 HIS H H 8.335 0.020 1 315 104 104 HIS C C 173.271 0.3 1 316 104 104 HIS CA C 56.243 0.3 1 317 104 104 HIS CB C 34.826 0.3 1 318 104 104 HIS N N 128.417 0.3 1 319 106 106 ASN H H 12.036 0.020 1 320 106 106 ASN C C 170.774 0.3 1 321 106 106 ASN CA C 54.631 0.3 1 322 106 106 ASN CB C 41.463 0.3 1 323 106 106 ASN N N 119.410 0.3 1 324 107 107 VAL H H 7.321 0.020 1 325 107 107 VAL C C 176.138 0.3 1 326 107 107 VAL CA C 60.657 0.3 1 327 107 107 VAL CB C 34.829 0.3 1 328 107 107 VAL N N 120.358 0.3 1 329 108 108 ASP H H 8.258 0.020 1 330 108 108 ASP C C 178.704 0.3 1 331 108 108 ASP CA C 52.228 0.3 1 332 108 108 ASP CB C 42.091 0.3 1 333 108 108 ASP N N 126.298 0.3 1 334 109 109 THR H H 7.667 0.020 1 335 109 109 THR C C 175.753 0.3 1 336 109 109 THR CA C 64.453 0.3 1 337 109 109 THR CB C 68.713 0.3 1 338 109 109 THR N N 108.736 0.3 1 339 110 110 GLN H H 7.887 0.020 1 340 110 110 GLN C C 175.682 0.3 1 341 110 110 GLN CA C 55.605 0.3 1 342 110 110 GLN CB C 29.232 0.3 1 343 110 110 GLN N N 119.832 0.3 1 344 111 111 GLY H H 7.773 0.020 1 345 111 111 GLY C C 174.686 0.3 1 346 111 111 GLY CA C 45.970 0.3 1 347 111 111 GLY N N 108.188 0.3 1 348 112 112 ASN H H 8.626 0.020 1 349 112 112 ASN C C 173.561 0.3 1 350 112 112 ASN CA C 54.226 0.3 1 351 112 112 ASN CB C 38.346 0.3 1 352 112 112 ASN N N 119.601 0.3 1 353 113 113 ILE H H 8.546 0.020 1 354 113 113 ILE C C 176.208 0.3 1 355 113 113 ILE CA C 60.217 0.3 1 356 113 113 ILE CB C 41.509 0.3 1 357 113 113 ILE N N 118.260 0.3 1 358 114 114 SER H H 8.435 0.020 1 359 114 114 SER C C 172.390 0.3 1 360 114 114 SER CA C 56.198 0.3 1 361 114 114 SER CB C 62.667 0.3 1 362 114 114 SER N N 122.512 0.3 1 363 115 115 LEU H H 7.227 0.020 1 364 115 115 LEU C C 176.255 0.3 1 365 115 115 LEU CA C 54.064 0.3 1 366 115 115 LEU CB C 44.044 0.3 1 367 115 115 LEU N N 127.081 0.3 1 368 116 116 ASP H H 9.046 0.020 1 369 116 116 ASP C C 180.072 0.3 1 370 116 116 ASP CA C 58.258 0.3 1 371 116 116 ASP CB C 38.882 0.3 1 372 116 116 ASP N N 131.365 0.3 1 373 117 117 ILE H H 8.061 0.020 1 374 117 117 ILE C C 173.317 0.3 1 375 117 117 ILE CA C 64.379 0.3 1 376 117 117 ILE N N 118.024 0.3 1 377 118 118 LEU H H 7.077 0.020 1 378 118 118 LEU C C 176.887 0.3 1 379 118 118 LEU CA C 54.178 0.3 1 380 118 118 LEU CB C 41.337 0.3 1 381 118 118 LEU N N 113.680 0.3 1 382 119 119 LYS H H 7.631 0.020 1 383 119 119 LYS C C 176.713 0.3 1 384 119 119 LYS CA C 56.255 0.3 1 385 119 119 LYS CB C 32.200 0.3 1 386 119 119 LYS N N 122.454 0.3 1 387 120 120 GLU H H 9.390 0.020 1 388 120 120 GLU CA C 59.864 0.3 1 389 120 120 GLU CB C 28.685 0.3 1 390 120 120 GLU N N 124.562 0.3 1 391 121 121 LYS H H 7.786 0.020 1 392 121 121 LYS C C 175.338 0.3 1 393 121 121 LYS CA C 54.612 0.3 1 394 121 121 LYS CB C 31.347 0.3 1 395 121 121 LYS N N 115.843 0.3 1 396 122 122 TRP H H 7.169 0.020 1 397 122 122 TRP C C 175.823 0.3 1 398 122 122 TRP CA C 59.736 0.3 1 399 122 122 TRP CB C 29.989 0.3 1 400 122 122 TRP N N 121.950 0.3 1 401 124 124 ALA H H 7.926 0.020 1 402 124 124 ALA C C 176.690 0.3 1 403 124 124 ALA CA C 53.432 0.3 1 404 124 124 ALA CB C 18.197 0.3 1 405 124 124 ALA N N 125.399 0.3 1 406 125 125 LEU H H 6.979 0.020 1 407 125 125 LEU C C 178.329 0.3 1 408 125 125 LEU CA C 55.426 0.3 1 409 125 125 LEU CB C 41.353 0.3 1 410 125 125 LEU N N 116.422 0.3 1 411 126 126 TYR H H 6.868 0.020 1 412 126 126 TYR C C 172.999 0.3 1 413 126 126 TYR CA C 56.145 0.3 1 414 126 126 TYR CB C 36.966 0.3 1 415 126 126 TYR N N 120.203 0.3 1 416 127 127 ASP H H 7.222 0.020 1 417 127 127 ASP C C 176.653 0.3 1 418 127 127 ASP CA C 51.287 0.3 1 419 127 127 ASP CB C 43.187 0.3 1 420 127 127 ASP N N 116.059 0.3 1 421 128 128 VAL H H 8.565 0.020 1 422 128 128 VAL C C 177.543 0.3 1 423 128 128 VAL CA C 67.563 0.3 1 424 128 128 VAL CB C 31.111 0.3 1 425 128 128 VAL N N 120.129 0.3 1 426 129 129 ARG H H 8.053 0.020 1 427 129 129 ARG C C 176.559 0.3 1 428 129 129 ARG CA C 60.814 0.3 1 429 129 129 ARG CB C 29.046 0.3 1 430 129 129 ARG N N 119.173 0.3 1 431 130 130 THR H H 8.095 0.020 1 432 130 130 THR CA C 67.762 0.3 1 433 130 130 THR CB C 68.824 0.3 1 434 130 130 THR N N 115.508 0.3 1 435 131 131 ILE H H 8.145 0.020 1 436 131 131 ILE C C 177.238 0.3 1 437 131 131 ILE CA C 66.334 0.3 1 438 131 131 ILE CB C 37.589 0.3 1 439 131 131 ILE N N 124.227 0.3 1 440 132 132 LEU H H 8.419 0.020 1 441 132 132 LEU C C 179.243 0.3 1 442 132 132 LEU CA C 58.650 0.3 1 443 132 132 LEU CB C 41.067 0.3 1 444 132 132 LEU N N 118.697 0.3 1 445 133 133 LEU H H 8.543 0.020 1 446 133 133 LEU C C 180.414 0.3 1 447 133 133 LEU CA C 58.044 0.3 1 448 133 133 LEU N N 119.234 0.3 1 449 134 134 SER H H 7.936 0.020 1 450 134 134 SER CA C 62.739 0.3 1 451 134 134 SER N N 116.911 0.3 1 452 135 135 ILE H H 7.931 0.020 1 453 135 135 ILE C C 176.278 0.3 1 454 135 135 ILE CA C 65.485 0.3 1 455 135 135 ILE CB C 37.084 0.3 1 456 135 135 ILE N N 124.489 0.3 1 457 136 136 GLN H H 8.318 0.020 1 458 136 136 GLN CA C 60.138 0.3 1 459 136 136 GLN CB C 29.193 0.3 1 460 136 136 GLN N N 119.852 0.3 1 461 137 137 SER H H 8.379 0.020 1 462 137 137 SER CA C 61.841 0.3 1 463 137 137 SER CB C 62.730 0.3 1 464 137 137 SER N N 115.555 0.3 1 465 138 138 LEU H H 7.435 0.020 1 466 138 138 LEU C C 178.854 0.3 1 467 138 138 LEU CA C 56.554 0.3 1 468 138 138 LEU CB C 41.611 0.3 1 469 138 138 LEU N N 124.113 0.3 1 470 139 139 LEU H H 7.196 0.020 1 471 139 139 LEU C C 175.974 0.3 1 472 139 139 LEU CA C 57.505 0.3 1 473 139 139 LEU CB C 39.878 0.3 1 474 139 139 LEU N N 116.764 0.3 1 475 140 140 GLY H H 6.705 0.020 1 476 140 140 GLY CA C 45.540 0.3 1 477 140 140 GLY N N 100.214 0.3 1 478 141 141 GLU H H 7.519 0.020 1 479 141 141 GLU C C 170.675 0.3 1 480 141 141 GLU CA C 53.671 0.3 1 481 141 141 GLU CB C 30.291 0.3 1 482 141 141 GLU N N 121.289 0.3 1 483 143 143 ASN H H 8.848 0.020 1 484 143 143 ASN CA C 51.601 0.3 1 485 143 143 ASN CB C 38.108 0.3 1 486 143 143 ASN N N 118.538 0.3 1 487 144 144 ILE H H 8.191 0.020 1 488 144 144 ILE C C 175.144 0.3 1 489 144 144 ILE CA C 61.666 0.3 1 490 144 144 ILE CB C 36.583 0.3 1 491 144 144 ILE N N 122.366 0.3 1 492 145 145 ASP H H 7.688 0.020 1 493 145 145 ASP C C 176.432 0.3 1 494 145 145 ASP CA C 55.780 0.3 1 495 145 145 ASP CB C 41.102 0.3 1 496 145 145 ASP N N 118.694 0.3 1 497 146 146 SER H H 6.928 0.020 1 498 146 146 SER CA C 54.910 0.3 1 499 146 146 SER CB C 63.440 0.3 1 500 146 146 SER N N 112.852 0.3 1 501 148 148 LEU H H 8.614 0.020 1 502 148 148 LEU C C 176.887 0.3 1 503 148 148 LEU CA C 55.362 0.3 1 504 148 148 LEU CB C 42.091 0.3 1 505 148 148 LEU N N 118.913 0.3 1 506 149 149 ASN H H 7.546 0.020 1 507 149 149 ASN C C 176.409 0.3 1 508 149 149 ASN CA C 51.914 0.3 1 509 149 149 ASN CB C 38.346 0.3 1 510 149 149 ASN N N 118.601 0.3 1 511 150 150 THR H H 8.735 0.020 1 512 150 150 THR C C 176.278 0.3 1 513 150 150 THR CA C 65.498 0.3 1 514 150 150 THR CB C 67.790 0.3 1 515 150 150 THR N N 117.823 0.3 1 516 151 151 HIS H H 8.015 0.020 1 517 151 151 HIS C C 178.041 0.3 1 518 151 151 HIS CA C 60.168 0.3 1 519 151 151 HIS CB C 30.078 0.3 1 520 151 151 HIS N N 124.846 0.3 1 521 152 152 ALA H H 7.233 0.020 1 522 152 152 ALA C C 179.417 0.3 1 523 152 152 ALA CA C 54.039 0.3 1 524 152 152 ALA CB C 17.428 0.3 1 525 152 152 ALA N N 120.973 0.3 1 526 153 153 ALA H H 7.803 0.020 1 527 153 153 ALA C C 178.119 0.3 1 528 153 153 ALA CA C 55.407 0.3 1 529 153 153 ALA CB C 18.278 0.3 1 530 153 153 ALA N N 118.727 0.3 1 531 154 154 GLU H H 7.579 0.020 1 532 154 154 GLU C C 179.477 0.3 1 533 154 154 GLU CA C 58.567 0.3 1 534 154 154 GLU CB C 29.299 0.3 1 535 154 154 GLU N N 116.544 0.3 1 536 155 155 LEU H H 7.912 0.020 1 537 155 155 LEU C C 177.543 0.3 1 538 155 155 LEU CA C 56.655 0.3 1 539 155 155 LEU CB C 41.873 0.3 1 540 155 155 LEU N N 122.005 0.3 1 541 156 156 TRP H H 8.051 0.020 1 542 156 156 TRP C C 176.339 0.3 1 543 156 156 TRP CA C 59.525 0.3 1 544 156 156 TRP CB C 29.147 0.3 1 545 156 156 TRP N N 119.458 0.3 1 546 157 157 LYS H H 6.842 0.020 1 547 157 157 LYS C C 174.910 0.3 1 548 157 157 LYS CA C 57.696 0.3 1 549 157 157 LYS CB C 32.136 0.3 1 550 157 157 LYS N N 112.172 0.3 1 551 158 158 ASN H H 8.067 0.020 1 552 158 158 ASN CA C 55.112 0.3 1 553 158 158 ASN CB C 38.698 0.3 1 554 158 158 ASN N N 119.339 0.3 1 555 160 160 THR H H 7.961 0.020 1 556 160 160 THR C C 176.532 0.3 1 557 160 160 THR CA C 66.543 0.3 1 558 160 160 THR CB C 68.354 0.3 1 559 160 160 THR N N 113.549 0.3 1 560 161 161 ALA H H 7.108 0.020 1 561 161 161 ALA C C 180.554 0.3 1 562 161 161 ALA CA C 54.392 0.3 1 563 161 161 ALA CB C 18.935 0.3 1 564 161 161 ALA N N 125.740 0.3 1 565 162 162 PHE H H 9.011 0.020 1 566 162 162 PHE CA C 62.518 0.3 1 567 162 162 PHE CB C 39.214 0.3 1 568 162 162 PHE N N 122.219 0.3 1 569 163 163 LYS H H 8.274 0.020 1 570 163 163 LYS CA C 60.206 0.3 1 571 163 163 LYS CB C 32.903 0.3 1 572 163 163 LYS N N 118.014 0.3 1 573 164 164 LYS H H 7.145 0.020 1 574 164 164 LYS C C 178.048 0.3 1 575 164 164 LYS CA C 59.569 0.3 1 576 164 164 LYS CB C 32.504 0.3 1 577 164 164 LYS N N 117.766 0.3 1 578 165 165 TYR H H 7.694 0.020 1 579 165 165 TYR C C 178.728 0.3 1 580 165 165 TYR CA C 61.771 0.3 1 581 165 165 TYR CB C 39.036 0.3 1 582 165 165 TYR N N 120.895 0.3 1 583 166 166 LEU H H 8.666 0.020 1 584 166 166 LEU CA C 58.010 0.3 1 585 166 166 LEU CB C 42.321 0.3 1 586 166 166 LEU N N 122.096 0.3 1 587 167 167 GLN H H 8.062 0.020 1 588 167 167 GLN CA C 59.403 0.3 1 589 167 167 GLN CB C 27.571 0.3 1 590 167 167 GLN N N 116.772 0.3 1 591 168 168 GLU H H 7.887 0.020 1 592 168 168 GLU CA C 59.020 0.3 1 593 168 168 GLU CB C 29.221 0.3 1 594 168 168 GLU N N 119.525 0.3 1 595 169 169 THR H H 7.700 0.020 1 596 169 169 THR C C 175.646 0.3 1 597 169 169 THR CA C 64.681 0.3 1 598 169 169 THR CB C 69.229 0.3 1 599 169 169 THR N N 112.012 0.3 1 600 171 171 SER H H 7.843 0.020 1 601 171 171 SER C C 177.192 0.3 1 602 171 171 SER CA C 60.191 0.3 1 603 171 171 SER CB C 63.184 0.3 1 604 171 171 SER N N 115.759 0.3 1 605 172 172 LYS H H 7.519 0.020 1 606 172 172 LYS C C 177.253 0.3 1 607 172 172 LYS CA C 57.452 0.3 1 608 172 172 LYS CB C 32.650 0.3 1 609 172 172 LYS N N 121.268 0.3 1 610 173 173 GLN H H 7.974 0.020 1 611 173 173 GLN C C 176.374 0.3 1 612 173 173 GLN CA C 56.706 0.3 1 613 173 173 GLN CB C 29.111 0.3 1 614 173 173 GLN N N 118.582 0.3 1 615 174 174 VAL H H 7.956 0.020 1 616 174 174 VAL C C 176.632 0.3 1 617 174 174 VAL CA C 63.067 0.3 1 618 174 174 VAL CB C 32.209 0.3 1 619 174 174 VAL N N 120.509 0.3 1 620 175 175 THR H H 7.858 0.020 1 621 175 175 THR C C 174.840 0.3 1 622 175 175 THR CA C 62.747 0.3 1 623 175 175 THR CB C 69.450 0.3 1 624 175 175 THR N N 117.039 0.3 1 625 176 176 SER H H 8.087 0.020 1 626 176 176 SER C C 174.149 0.3 1 627 176 176 SER CA C 58.741 0.3 1 628 176 176 SER CB C 63.624 0.3 1 629 176 176 SER N N 117.569 0.3 1 630 177 177 GLN H H 8.034 0.020 1 631 177 177 GLN C C 175.437 0.3 1 632 177 177 GLN CA C 55.517 0.3 1 633 177 177 GLN CB C 29.232 0.3 1 634 177 177 GLN N N 121.891 0.3 1 635 178 178 GLU H H 8.059 0.020 1 636 178 178 GLU C C 173.681 0.3 1 637 178 178 GLU CA C 54.490 0.3 1 638 178 178 GLU CB C 29.711 0.3 1 639 178 178 GLU N N 124.044 0.3 1 stop_ save_