data_26526 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; UBCH10 ; _BMRB_accession_number 26526 _BMRB_flat_file_name bmr26526.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 Nicholus G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 135 "13C chemical shifts" 367 "15N chemical shifts" 135 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 26527 WHB 26528 'UBCH10 in complex with 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 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label molecule_2 $Molecule_2 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_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Molecule_2 _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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Molecule_2 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_2 '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_2 0.5 mM '[U-100% 13C; U-100% 15N]' 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' 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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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 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 HNCACB' '3D HNCO' '3D CBCA(CO)NH' '3D HN(CA)CO' 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_2 _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 8.485 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 110.510 0.3 1 5 27 27 ALA H H 8.252 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 124.830 0.3 1 10 28 28 ARG H H 8.245 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 118.587 0.3 1 15 29 29 GLY H H 8.084 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 109.711 0.3 1 19 31 31 VAL H H 8.178 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 121.155 0.3 1 24 32 32 GLY H H 8.144 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 109.262 0.3 1 28 33 33 LYS H H 7.795 0.020 1 29 33 33 LYS C C 179.276 0.3 1 30 33 33 LYS CA C 60.012 0.3 1 31 33 33 LYS CB C 31.914 0.3 1 32 33 33 LYS N N 120.631 0.3 1 33 34 34 ARG H H 7.529 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 121.494 0.3 1 38 35 35 LEU H H 8.304 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 120.717 0.3 1 43 36 36 GLN H H 8.022 0.020 1 44 36 36 GLN C C 178.620 0.3 1 45 36 36 GLN CA C 59.860 0.3 1 46 36 36 GLN CB C 28.521 0.3 1 47 36 36 GLN N N 118.184 0.3 1 48 37 37 GLN H H 7.768 0.020 1 49 37 37 GLN C C 179.065 0.3 1 50 37 37 GLN CA C 59.241 0.3 1 51 37 37 GLN CB C 28.079 0.3 1 52 37 37 GLN N N 120.390 0.3 1 53 38 38 GLU H H 8.786 0.020 1 54 38 38 GLU C C 180.742 0.3 1 55 38 38 GLU CA C 60.847 0.3 1 56 38 38 GLU CB C 28.762 0.3 1 57 38 38 GLU N N 121.656 0.3 1 58 39 39 LEU H H 8.319 0.020 1 59 39 39 LEU C C 178.292 0.3 1 60 39 39 LEU CA C 58.014 0.3 1 61 39 39 LEU CB C 40.273 0.3 1 62 39 39 LEU N N 122.166 0.3 1 63 40 40 MET H H 7.802 0.020 1 64 40 40 MET C C 178.527 0.3 1 65 40 40 MET CA C 59.218 0.3 1 66 40 40 MET CB C 31.379 0.3 1 67 40 40 MET N N 119.451 0.3 1 68 41 41 THR H H 8.489 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 116.630 0.3 1 73 42 42 LEU H H 7.969 0.020 1 74 42 42 LEU C C 179.258 0.3 1 75 42 42 LEU CA C 58.885 0.3 1 76 42 42 LEU CB C 41.611 0.3 1 77 42 42 LEU N N 124.624 0.3 1 78 43 43 MET H H 8.485 0.020 1 79 43 43 MET C C 178.714 0.3 1 80 43 43 MET CA C 59.209 0.3 1 81 43 43 MET CB C 33.362 0.3 1 82 43 43 MET N N 118.525 0.3 1 83 44 44 MET H H 7.974 0.020 1 84 44 44 MET C C 177.894 0.3 1 85 44 44 MET CA C 56.259 0.3 1 86 44 44 MET CB C 32.289 0.3 1 87 44 44 MET N N 115.607 0.3 1 88 45 45 SER H H 7.579 0.020 1 89 45 45 SER C C 175.435 0.3 1 90 45 45 SER CA C 61.568 0.3 1 91 45 45 SER CB C 63.648 0.3 1 92 45 45 SER N N 115.405 0.3 1 93 46 46 GLY H H 7.782 0.020 1 94 46 46 GLY C C 174.920 0.3 1 95 46 46 GLY CA C 47.336 0.3 1 96 46 46 GLY N N 108.900 0.3 1 97 47 47 ASP H H 8.117 0.020 1 98 47 47 ASP C C 176.208 0.3 1 99 47 47 ASP CA C 55.402 0.3 1 100 47 47 ASP CB C 42.017 0.3 1 101 47 47 ASP N N 119.623 0.3 1 102 48 48 LYS H H 8.599 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 123.130 0.3 1 107 49 49 GLY H H 8.606 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 111.315 0.3 1 111 50 50 ILE H H 6.805 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 111.070 0.3 1 116 51 51 SER H H 7.939 0.020 1 117 51 51 SER C C 172.297 0.3 1 118 51 51 SER CA C 57.771 0.3 1 119 51 51 SER CB C 64.593 0.3 1 120 51 51 SER N N 115.477 0.3 1 121 52 52 ALA H H 7.896 0.020 1 122 52 52 ALA C C 173.023 0.3 1 123 52 52 ALA CA C 53.410 0.3 1 124 52 52 ALA CB C 21.920 0.3 1 125 52 52 ALA N N 122.350 0.3 1 126 53 53 PHE H H 8.002 0.020 1 127 53 53 PHE C C 172.275 0.3 1 128 53 53 PHE CA C 55.715 0.3 1 129 53 53 PHE CB C 42.616 0.3 1 130 53 53 PHE N N 113.841 0.3 1 131 56 56 SER H H 8.787 0.020 1 132 56 56 SER CA C 60.315 0.3 1 133 56 56 SER CB C 62.969 0.3 1 134 56 56 SER N N 118.707 0.3 1 135 57 57 ASP H H 8.392 0.020 1 136 57 57 ASP C C 175.402 0.3 1 137 57 57 ASP CA C 54.009 0.3 1 138 57 57 ASP CB C 40.993 0.3 1 139 57 57 ASP N N 118.656 0.3 1 140 58 58 ASN H H 7.472 0.020 1 141 58 58 ASN C C 173.725 0.3 1 142 58 58 ASN CA C 52.685 0.3 1 143 58 58 ASN CB C 38.397 0.3 1 144 58 58 ASN N N 117.288 0.3 1 145 59 59 LEU H H 8.394 0.020 1 146 59 59 LEU CA C 56.213 0.3 1 147 59 59 LEU CB C 41.463 0.3 1 148 59 59 LEU N N 123.941 0.3 1 149 60 60 PHE H H 7.786 0.020 1 150 60 60 PHE C C 175.203 0.3 1 151 60 60 PHE CA C 58.014 0.3 1 152 60 60 PHE CB C 37.813 0.3 1 153 60 60 PHE N N 112.264 0.3 1 154 61 61 LYS H H 7.661 0.020 1 155 61 61 LYS CA C 56.660 0.3 1 156 61 61 LYS CB C 35.356 0.3 1 157 61 61 LYS N N 123.309 0.3 1 158 62 62 TRP H H 9.711 0.020 1 159 62 62 TRP C C 176.184 0.3 1 160 62 62 TRP CA C 54.262 0.3 1 161 62 62 TRP CB C 32.602 0.3 1 162 62 62 TRP N N 124.656 0.3 1 163 63 63 VAL H H 8.472 0.020 1 164 63 63 VAL C C 176.432 0.3 1 165 63 63 VAL CA C 61.299 0.3 1 166 63 63 VAL CB C 33.831 0.3 1 167 63 63 VAL N N 121.135 0.3 1 168 64 64 GLY H H 9.206 0.020 1 169 64 64 GLY CA C 43.734 0.3 1 170 64 64 GLY N N 114.108 0.3 1 171 65 65 THR H H 8.902 0.020 1 172 65 65 THR C C 173.772 0.3 1 173 65 65 THR CA C 62.203 0.3 1 174 65 65 THR CB C 71.481 0.3 1 175 65 65 THR N N 116.419 0.3 1 176 66 66 ILE H H 8.870 0.020 1 177 66 66 ILE C C 174.572 0.3 1 178 66 66 ILE CA C 59.129 0.3 1 179 66 66 ILE CB C 41.577 0.3 1 180 66 66 ILE N N 121.904 0.3 1 181 68 68 GLY H H 8.291 0.020 1 182 68 68 GLY C C 173.468 0.3 1 183 68 68 GLY CA C 45.372 0.3 1 184 68 68 GLY N N 111.265 0.3 1 185 69 69 ALA H H 7.965 0.020 1 186 69 69 ALA CA C 52.304 0.3 1 187 69 69 ALA CB C 19.191 0.3 1 188 69 69 ALA N N 124.046 0.3 1 189 70 70 ALA H H 8.591 0.020 1 190 70 70 ALA C C 178.808 0.3 1 191 70 70 ALA CA C 53.442 0.3 1 192 70 70 ALA CB C 18.027 0.3 1 193 70 70 ALA N N 125.577 0.3 1 194 71 71 GLY H H 9.062 0.020 1 195 71 71 GLY C C 174.498 0.3 1 196 71 71 GLY CA C 45.411 0.3 1 197 71 71 GLY N N 111.030 0.3 1 198 72 72 THR H H 7.524 0.020 1 199 72 72 THR C C 177.566 0.3 1 200 72 72 THR CA C 60.206 0.3 1 201 72 72 THR CB C 73.999 0.3 1 202 72 72 THR N N 109.124 0.3 1 203 73 73 VAL H H 9.083 0.020 1 204 73 73 VAL C C 174.756 0.3 1 205 73 73 VAL CA C 64.832 0.3 1 206 73 73 VAL CB C 31.581 0.3 1 207 73 73 VAL N N 117.187 0.3 1 208 74 74 TYR H H 6.969 0.020 1 209 74 74 TYR C C 176.983 0.3 1 210 74 74 TYR CA C 58.397 0.3 1 211 74 74 TYR CB C 39.029 0.3 1 212 74 74 TYR N N 114.417 0.3 1 213 79 79 TYR H H 8.900 0.020 1 214 79 79 TYR C C 173.784 0.3 1 215 79 79 TYR CA C 58.153 0.3 1 216 79 79 TYR CB C 42.957 0.3 1 217 79 79 TYR N N 121.783 0.3 1 218 80 80 LYS H H 8.855 0.020 1 219 80 80 LYS C C 176.643 0.3 1 220 80 80 LYS CA C 54.450 0.3 1 221 80 80 LYS CB C 33.572 0.3 1 222 80 80 LYS N N 121.411 0.3 1 223 81 81 LEU H H 9.216 0.020 1 224 81 81 LEU C C 174.685 0.3 1 225 81 81 LEU CA C 54.481 0.3 1 226 81 81 LEU CB C 45.814 0.3 1 227 81 81 LEU N N 124.113 0.3 1 228 82 82 SER H H 9.106 0.020 1 229 82 82 SER CA C 55.970 0.3 1 230 82 82 SER CB C 65.173 0.3 1 231 82 82 SER N N 115.355 0.3 1 232 83 83 LEU H H 8.289 0.020 1 233 83 83 LEU CA C 55.097 0.3 1 234 83 83 LEU CB C 43.381 0.3 1 235 83 83 LEU N N 122.765 0.3 1 236 84 84 GLU H H 8.208 0.020 1 237 84 84 GLU C C 174.442 0.3 1 238 84 84 GLU CA C 54.368 0.3 1 239 84 84 GLU CB C 32.097 0.3 1 240 84 84 GLU N N 121.975 0.3 1 241 85 85 PHE H H 8.491 0.020 1 242 85 85 PHE CA C 55.770 0.3 1 243 85 85 PHE CB C 39.029 0.3 1 244 85 85 PHE N N 125.226 0.3 1 245 87 87 SER H H 8.585 0.020 1 246 87 87 SER CA C 61.375 0.3 1 247 87 87 SER CB C 62.850 0.3 1 248 87 87 SER N N 114.989 0.3 1 249 88 88 GLY H H 8.152 0.020 1 250 88 88 GLY C C 175.361 0.3 1 251 88 88 GLY CA C 45.104 0.3 1 252 88 88 GLY N N 108.752 0.3 1 253 89 89 TYR H H 7.737 0.020 1 254 89 89 TYR C C 175.004 0.3 1 255 89 89 TYR CA C 57.986 0.3 1 256 89 89 TYR CB C 38.846 0.3 1 257 89 89 TYR N N 125.955 0.3 1 258 91 91 TYR H H 8.123 0.020 1 259 91 91 TYR C C 176.161 0.3 1 260 91 91 TYR CA C 61.375 0.3 1 261 91 91 TYR CB C 36.522 0.3 1 262 91 91 TYR N N 125.648 0.3 1 263 92 92 ASN H H 7.058 0.020 1 264 92 92 ASN C C 171.969 0.3 1 265 92 92 ASN CA C 51.370 0.3 1 266 92 92 ASN CB C 41.501 0.3 1 267 92 92 ASN N N 115.899 0.3 1 268 93 93 ALA H H 7.295 0.020 1 269 93 93 ALA C C 175.191 0.3 1 270 93 93 ALA CA C 49.640 0.3 1 271 93 93 ALA CB C 17.875 0.3 1 272 93 93 ALA N N 121.575 0.3 1 273 95 95 THR H H 8.191 0.020 1 274 95 95 THR C C 174.418 0.3 1 275 95 95 THR CA C 61.863 0.3 1 276 95 95 THR CB C 69.681 0.3 1 277 95 95 THR N N 116.396 0.3 1 278 96 96 VAL H H 8.842 0.020 1 279 96 96 VAL C C 173.435 0.3 1 280 96 96 VAL CA C 60.355 0.3 1 281 96 96 VAL CB C 32.834 0.3 1 282 96 96 VAL N N 131.401 0.3 1 283 97 97 LYS H H 8.070 0.020 1 284 97 97 LYS C C 176.222 0.3 1 285 97 97 LYS CA C 54.590 0.3 1 286 97 97 LYS CB C 36.301 0.3 1 287 97 97 LYS N N 123.825 0.3 1 288 98 98 PHE H H 9.435 0.020 1 289 98 98 PHE C C 176.676 0.3 1 290 98 98 PHE CA C 60.683 0.3 1 291 98 98 PHE CB C 38.806 0.3 1 292 98 98 PHE N N 121.436 0.3 1 293 99 99 LEU H H 9.194 0.020 1 294 99 99 LEU C C 178.283 0.3 1 295 99 99 LEU CA C 55.574 0.3 1 296 99 99 LEU CB C 42.420 0.3 1 297 99 99 LEU N N 125.364 0.3 1 298 100 100 THR H H 7.544 0.020 1 299 100 100 THR C C 171.875 0.3 1 300 100 100 THR CA C 59.662 0.3 1 301 100 100 THR CB C 70.626 0.3 1 302 100 100 THR N N 118.713 0.3 1 303 102 102 CYS H H 8.292 0.020 1 304 102 102 CYS C C 172.966 0.3 1 305 102 102 CYS CA C 57.865 0.3 1 306 102 102 CYS CB C 28.483 0.3 1 307 102 102 CYS N N 126.308 0.3 1 308 103 103 TYR H H 7.931 0.020 1 309 103 103 TYR CA C 58.352 0.3 1 310 103 103 TYR CB C 37.628 0.3 1 311 103 103 TYR N N 133.065 0.3 1 312 104 104 HIS H H 8.341 0.020 1 313 104 104 HIS C C 173.271 0.3 1 314 104 104 HIS CA C 56.243 0.3 1 315 104 104 HIS CB C 34.826 0.3 1 316 104 104 HIS N N 128.475 0.3 1 317 106 106 ASN H H 12.041 0.020 1 318 106 106 ASN C C 170.774 0.3 1 319 106 106 ASN CA C 54.438 0.3 1 320 106 106 ASN CB C 41.463 0.3 1 321 106 106 ASN N N 119.383 0.3 1 322 107 107 VAL H H 7.332 0.020 1 323 107 107 VAL C C 176.138 0.3 1 324 107 107 VAL CA C 60.832 0.3 1 325 107 107 VAL CB C 34.829 0.3 1 326 107 107 VAL N N 120.393 0.3 1 327 108 108 ASP H H 8.287 0.020 1 328 108 108 ASP C C 178.704 0.3 1 329 108 108 ASP CA C 52.452 0.3 1 330 108 108 ASP CB C 42.091 0.3 1 331 108 108 ASP N N 126.402 0.3 1 332 109 109 THR H H 7.680 0.020 1 333 109 109 THR C C 175.753 0.3 1 334 109 109 THR CA C 64.706 0.3 1 335 109 109 THR CB C 68.713 0.3 1 336 109 109 THR N N 108.764 0.3 1 337 110 110 GLN H H 7.904 0.020 1 338 110 110 GLN C C 175.682 0.3 1 339 110 110 GLN CA C 55.605 0.3 1 340 110 110 GLN CB C 29.232 0.3 1 341 110 110 GLN N N 119.849 0.3 1 342 111 111 GLY H H 7.774 0.020 1 343 111 111 GLY C C 174.686 0.3 1 344 111 111 GLY CA C 45.970 0.3 1 345 111 111 GLY N N 108.188 0.3 1 346 112 112 ASN H H 8.637 0.020 1 347 112 112 ASN C C 173.561 0.3 1 348 112 112 ASN CA C 54.064 0.3 1 349 112 112 ASN CB C 38.346 0.3 1 350 112 112 ASN N N 119.636 0.3 1 351 113 113 ILE H H 8.498 0.020 1 352 113 113 ILE C C 176.208 0.3 1 353 113 113 ILE CA C 60.002 0.3 1 354 113 113 ILE CB C 41.509 0.3 1 355 113 113 ILE N N 118.198 0.3 1 356 114 114 SER H H 8.418 0.020 1 357 114 114 SER C C 172.390 0.3 1 358 114 114 SER CA C 56.398 0.3 1 359 114 114 SER CB C 62.667 0.3 1 360 114 114 SER N N 122.445 0.3 1 361 115 115 LEU H H 7.262 0.020 1 362 115 115 LEU C C 176.255 0.3 1 363 115 115 LEU CA C 54.064 0.3 1 364 115 115 LEU CB C 44.044 0.3 1 365 115 115 LEU N N 127.151 0.3 1 366 116 116 ASP H H 9.049 0.020 1 367 116 116 ASP C C 180.072 0.3 1 368 116 116 ASP CA C 58.258 0.3 1 369 116 116 ASP CB C 38.882 0.3 1 370 116 116 ASP N N 131.365 0.3 1 371 117 117 ILE H H 8.053 0.020 1 372 117 117 ILE C C 173.317 0.3 1 373 117 117 ILE CA C 64.379 0.3 1 374 117 117 ILE N N 117.711 0.3 1 375 118 118 LEU H H 7.085 0.020 1 376 118 118 LEU C C 176.887 0.3 1 377 118 118 LEU CA C 54.443 0.3 1 378 118 118 LEU CB C 41.337 0.3 1 379 118 118 LEU N N 113.732 0.3 1 380 119 119 LYS H H 7.624 0.020 1 381 119 119 LYS C C 176.713 0.3 1 382 119 119 LYS CA C 56.255 0.3 1 383 119 119 LYS CB C 32.200 0.3 1 384 119 119 LYS N N 122.346 0.3 1 385 120 120 GLU H H 9.382 0.020 1 386 120 120 GLU CA C 59.864 0.3 1 387 120 120 GLU CB C 28.685 0.3 1 388 120 120 GLU N N 124.551 0.3 1 389 121 121 LYS H H 7.771 0.020 1 390 121 121 LYS C C 175.338 0.3 1 391 121 121 LYS CA C 54.766 0.3 1 392 121 121 LYS CB C 31.347 0.3 1 393 121 121 LYS N N 115.860 0.3 1 394 122 122 TRP H H 7.185 0.020 1 395 122 122 TRP C C 175.823 0.3 1 396 122 122 TRP CA C 59.736 0.3 1 397 122 122 TRP CB C 29.989 0.3 1 398 122 122 TRP N N 121.993 0.3 1 399 124 124 ALA H H 7.941 0.020 1 400 124 124 ALA C C 176.690 0.3 1 401 124 124 ALA CA C 53.277 0.3 1 402 124 124 ALA CB C 18.197 0.3 1 403 124 124 ALA N N 125.479 0.3 1 404 125 125 LEU H H 6.988 0.020 1 405 125 125 LEU C C 178.329 0.3 1 406 125 125 LEU CA C 55.770 0.3 1 407 125 125 LEU CB C 41.353 0.3 1 408 125 125 LEU N N 116.326 0.3 1 409 126 126 TYR H H 6.899 0.020 1 410 126 126 TYR C C 172.999 0.3 1 411 126 126 TYR CA C 56.145 0.3 1 412 126 126 TYR CB C 36.966 0.3 1 413 126 126 TYR N N 120.348 0.3 1 414 127 127 ASP H H 7.217 0.020 1 415 127 127 ASP C C 176.653 0.3 1 416 127 127 ASP CA C 51.115 0.3 1 417 127 127 ASP CB C 43.187 0.3 1 418 127 127 ASP N N 115.917 0.3 1 419 128 128 VAL H H 8.739 0.020 1 420 128 128 VAL C C 177.543 0.3 1 421 128 128 VAL CA C 67.563 0.3 1 422 128 128 VAL CB C 31.111 0.3 1 423 128 128 VAL N N 120.353 0.3 1 424 129 129 ARG H H 8.196 0.020 1 425 129 129 ARG C C 176.559 0.3 1 426 129 129 ARG CA C 60.814 0.3 1 427 129 129 ARG CB C 29.046 0.3 1 428 129 129 ARG N N 119.399 0.3 1 429 130 130 THR H H 8.136 0.020 1 430 130 130 THR CA C 67.340 0.3 1 431 130 130 THR CB C 68.824 0.3 1 432 130 130 THR N N 115.616 0.3 1 433 131 131 ILE H H 8.110 0.020 1 434 131 131 ILE C C 177.238 0.3 1 435 131 131 ILE CA C 66.169 0.3 1 436 131 131 ILE CB C 37.589 0.3 1 437 131 131 ILE N N 124.131 0.3 1 438 132 132 LEU H H 8.472 0.020 1 439 132 132 LEU C C 179.243 0.3 1 440 132 132 LEU CA C 58.946 0.3 1 441 132 132 LEU CB C 41.067 0.3 1 442 132 132 LEU N N 118.479 0.3 1 443 133 133 LEU H H 8.576 0.020 1 444 133 133 LEU C C 180.414 0.3 1 445 133 133 LEU CA C 58.545 0.3 1 446 133 133 LEU N N 119.243 0.3 1 447 134 134 SER H H 7.930 0.020 1 448 134 134 SER CA C 62.739 0.3 1 449 134 134 SER N N 116.929 0.3 1 450 135 135 ILE H H 7.937 0.020 1 451 135 135 ILE C C 176.278 0.3 1 452 135 135 ILE CA C 65.485 0.3 1 453 135 135 ILE CB C 37.084 0.3 1 454 135 135 ILE N N 124.489 0.3 1 455 136 136 GLN H H 8.312 0.020 1 456 136 136 GLN CA C 60.138 0.3 1 457 136 136 GLN CB C 29.193 0.3 1 458 136 136 GLN N N 119.909 0.3 1 459 137 137 SER H H 8.379 0.020 1 460 137 137 SER CA C 61.841 0.3 1 461 137 137 SER CB C 62.730 0.3 1 462 137 137 SER N N 115.550 0.3 1 463 138 138 LEU H H 7.460 0.020 1 464 138 138 LEU C C 178.854 0.3 1 465 138 138 LEU CA C 56.554 0.3 1 466 138 138 LEU CB C 41.611 0.3 1 467 138 138 LEU N N 124.276 0.3 1 468 139 139 LEU H H 7.219 0.020 1 469 139 139 LEU C C 175.974 0.3 1 470 139 139 LEU CA C 57.505 0.3 1 471 139 139 LEU CB C 39.878 0.3 1 472 139 139 LEU N N 116.899 0.3 1 473 140 140 GLY H H 6.728 0.020 1 474 140 140 GLY CA C 45.298 0.3 1 475 140 140 GLY N N 100.314 0.3 1 476 141 141 GLU H H 7.532 0.020 1 477 141 141 GLU C C 170.675 0.3 1 478 141 141 GLU CA C 53.671 0.3 1 479 141 141 GLU CB C 30.291 0.3 1 480 141 141 GLU N N 121.271 0.3 1 481 143 143 ASN H H 8.852 0.020 1 482 143 143 ASN CA C 51.431 0.3 1 483 143 143 ASN CB C 38.108 0.3 1 484 143 143 ASN N N 118.567 0.3 1 485 144 144 ILE H H 8.204 0.020 1 486 144 144 ILE C C 175.144 0.3 1 487 144 144 ILE CA C 61.666 0.3 1 488 144 144 ILE CB C 36.583 0.3 1 489 144 144 ILE N N 122.479 0.3 1 490 145 145 ASP H H 7.700 0.020 1 491 145 145 ASP C C 176.432 0.3 1 492 145 145 ASP CA C 55.715 0.3 1 493 145 145 ASP CB C 41.102 0.3 1 494 145 145 ASP N N 118.746 0.3 1 495 146 146 SER H H 6.940 0.020 1 496 146 146 SER CA C 54.654 0.3 1 497 146 146 SER CB C 63.440 0.3 1 498 146 146 SER N N 112.887 0.3 1 499 148 148 LEU H H 8.616 0.020 1 500 148 148 LEU C C 176.887 0.3 1 501 148 148 LEU CA C 55.131 0.3 1 502 148 148 LEU CB C 42.091 0.3 1 503 148 148 LEU N N 119.026 0.3 1 504 149 149 ASN H H 7.549 0.020 1 505 149 149 ASN C C 176.409 0.3 1 506 149 149 ASN CA C 51.745 0.3 1 507 149 149 ASN CB C 38.346 0.3 1 508 149 149 ASN N N 118.619 0.3 1 509 150 150 THR H H 8.747 0.020 1 510 150 150 THR C C 176.278 0.3 1 511 150 150 THR CA C 65.572 0.3 1 512 150 150 THR CB C 67.790 0.3 1 513 150 150 THR N N 117.893 0.3 1 514 151 151 HIS H H 8.024 0.020 1 515 151 151 HIS C C 178.041 0.3 1 516 151 151 HIS CA C 60.168 0.3 1 517 151 151 HIS CB C 30.078 0.3 1 518 151 151 HIS N N 124.899 0.3 1 519 152 152 ALA H H 7.241 0.020 1 520 152 152 ALA C C 179.417 0.3 1 521 152 152 ALA CA C 53.802 0.3 1 522 152 152 ALA CB C 17.428 0.3 1 523 152 152 ALA N N 120.999 0.3 1 524 153 153 ALA H H 7.817 0.020 1 525 153 153 ALA C C 178.119 0.3 1 526 153 153 ALA CA C 55.407 0.3 1 527 153 153 ALA CB C 18.278 0.3 1 528 153 153 ALA N N 118.794 0.3 1 529 154 154 GLU H H 7.597 0.020 1 530 154 154 GLU C C 179.477 0.3 1 531 154 154 GLU CA C 58.536 0.3 1 532 154 154 GLU CB C 29.299 0.3 1 533 154 154 GLU N N 116.616 0.3 1 534 155 155 LEU H H 7.921 0.020 1 535 155 155 LEU C C 177.543 0.3 1 536 155 155 LEU CA C 56.377 0.3 1 537 155 155 LEU CB C 41.873 0.3 1 538 155 155 LEU N N 122.049 0.3 1 539 156 156 TRP H H 8.072 0.020 1 540 156 156 TRP C C 176.339 0.3 1 541 156 156 TRP CA C 59.525 0.3 1 542 156 156 TRP CB C 29.147 0.3 1 543 156 156 TRP N N 119.440 0.3 1 544 157 157 LYS H H 6.848 0.020 1 545 157 157 LYS C C 174.910 0.3 1 546 157 157 LYS CA C 57.504 0.3 1 547 157 157 LYS CB C 32.136 0.3 1 548 157 157 LYS N N 112.207 0.3 1 549 158 158 ASN H H 8.084 0.020 1 550 158 158 ASN CA C 55.112 0.3 1 551 158 158 ASN CB C 38.698 0.3 1 552 158 158 ASN N N 119.470 0.3 1 553 160 160 THR H H 7.965 0.020 1 554 160 160 THR C C 176.532 0.3 1 555 160 160 THR CA C 66.384 0.3 1 556 160 160 THR CB C 68.354 0.3 1 557 160 160 THR N N 113.595 0.3 1 558 161 161 ALA H H 7.121 0.020 1 559 161 161 ALA C C 180.554 0.3 1 560 161 161 ALA CA C 54.392 0.3 1 561 161 161 ALA CB C 18.935 0.3 1 562 161 161 ALA N N 125.774 0.3 1 563 162 162 PHE H H 9.026 0.020 1 564 162 162 PHE CA C 62.518 0.3 1 565 162 162 PHE CB C 39.214 0.3 1 566 162 162 PHE N N 122.323 0.3 1 567 163 163 LYS H H 8.310 0.020 1 568 163 163 LYS CA C 60.206 0.3 1 569 163 163 LYS CB C 32.903 0.3 1 570 163 163 LYS N N 118.049 0.3 1 571 164 164 LYS H H 7.164 0.020 1 572 164 164 LYS C C 178.048 0.3 1 573 164 164 LYS CA C 59.569 0.3 1 574 164 164 LYS CB C 32.504 0.3 1 575 164 164 LYS N N 117.829 0.3 1 576 165 165 TYR H H 7.702 0.020 1 577 165 165 TYR C C 178.728 0.3 1 578 165 165 TYR CA C 61.339 0.3 1 579 165 165 TYR CB C 39.036 0.3 1 580 165 165 TYR N N 120.972 0.3 1 581 166 166 LEU H H 8.677 0.020 1 582 166 166 LEU CA C 57.822 0.3 1 583 166 166 LEU CB C 42.321 0.3 1 584 166 166 LEU N N 122.093 0.3 1 585 167 167 GLN H H 8.082 0.020 1 586 167 167 GLN CA C 59.218 0.3 1 587 167 167 GLN CB C 27.571 0.3 1 588 167 167 GLN N N 116.851 0.3 1 589 168 168 GLU H H 7.892 0.020 1 590 168 168 GLU CA C 58.954 0.3 1 591 168 168 GLU CB C 29.221 0.3 1 592 168 168 GLU N N 119.569 0.3 1 593 169 169 THR H H 7.716 0.020 1 594 169 169 THR C C 175.646 0.3 1 595 169 169 THR CA C 64.681 0.3 1 596 169 169 THR CB C 69.229 0.3 1 597 169 169 THR N N 112.122 0.3 1 598 171 171 SER H H 7.841 0.020 1 599 171 171 SER C C 177.192 0.3 1 600 171 171 SER CA C 60.191 0.3 1 601 171 171 SER CB C 63.184 0.3 1 602 171 171 SER N N 115.637 0.3 1 603 172 172 LYS H H 7.510 0.020 1 604 172 172 LYS C C 177.253 0.3 1 605 172 172 LYS CA C 57.277 0.3 1 606 172 172 LYS CB C 32.650 0.3 1 607 172 172 LYS N N 121.249 0.3 1 608 173 173 GLN H H 7.955 0.020 1 609 173 173 GLN C C 176.374 0.3 1 610 173 173 GLN CA C 56.562 0.3 1 611 173 173 GLN CB C 29.111 0.3 1 612 173 173 GLN N N 118.713 0.3 1 613 174 174 VAL H H 7.966 0.020 1 614 174 174 VAL C C 176.632 0.3 1 615 174 174 VAL CA C 63.067 0.3 1 616 174 174 VAL CB C 32.209 0.3 1 617 174 174 VAL N N 120.718 0.3 1 618 175 175 THR H H 7.878 0.020 1 619 175 175 THR C C 174.840 0.3 1 620 175 175 THR CA C 62.747 0.3 1 621 175 175 THR CB C 69.450 0.3 1 622 175 175 THR N N 116.993 0.3 1 623 176 176 SER H H 8.069 0.020 1 624 176 176 SER C C 174.149 0.3 1 625 176 176 SER CA C 58.579 0.3 1 626 176 176 SER CB C 63.624 0.3 1 627 176 176 SER N N 117.610 0.3 1 628 177 177 GLN H H 8.061 0.020 1 629 177 177 GLN C C 175.437 0.3 1 630 177 177 GLN CA C 55.517 0.3 1 631 177 177 GLN CB C 29.232 0.3 1 632 177 177 GLN N N 121.917 0.3 1 633 178 178 GLU H H 8.095 0.020 1 634 178 178 GLU C C 173.681 0.3 1 635 178 178 GLU CA C 54.490 0.3 1 636 178 178 GLU CB C 29.711 0.3 1 637 178 178 GLU N N 124.122 0.3 1 stop_ save_