data_27300 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone HN, N, CA, and CB assignment of human UBC9_P123L ; _BMRB_accession_number 27300 _BMRB_flat_file_name bmr27300.str _Entry_type original _Submission_date 2017-11-02 _Accession_date 2017-11-02 _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 Placzek William WJP . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 295 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-02-19 update BMRB 'update entry citation' 2019-01-10 original author 'original release' stop_ _Original_release_date 2017-11-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; UBC9 mutant reveals the impact of protein dynamics on substrate selectivity and SUMO chain linkages ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30574775 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wright Christine M. . 2 Whitaker Robert H. . 3 Onuiri Joshua E. . 4 Blackburn Tessa . . 5 McGarity Sierra . . 6 Bjornsti Mary-Ann . . 7 Placzek William J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 58 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 621 _Page_last 632 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'UBC9_P123L monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'UBC9_P123L monomer' $UBC9(P123L) stop_ _System_molecular_weight 20170 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UBC9(P123L) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common UBC9(P123L) _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 178 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MSGIALSRLAQERKAWRKDH PFGFVAVPTKNPDGTMNLMN WECAIPGKKGTPWEGGLFKL RMLFKDDYPSSPPKCKFEPP LFHPNVYPSGTVCLSILEED KDWRPAITIKQILLGIQELL NELNIQDPAQAEAYTIYCQN RVEYEKRVRAQAKKFAPS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -19 MET 2 -18 GLY 3 -17 SER 4 -16 SER 5 -15 HIS 6 -14 HIS 7 -13 HIS 8 -12 HIS 9 -11 HIS 10 -10 HIS 11 -9 SER 12 -8 SER 13 -7 GLY 14 -6 LEU 15 -5 VAL 16 -4 PRO 17 -3 ARG 18 -2 GLY 19 -1 SER 20 0 HIS 21 1 MET 22 2 SER 23 3 GLY 24 4 ILE 25 5 ALA 26 6 LEU 27 7 SER 28 8 ARG 29 9 LEU 30 10 ALA 31 11 GLN 32 12 GLU 33 13 ARG 34 14 LYS 35 15 ALA 36 16 TRP 37 17 ARG 38 18 LYS 39 19 ASP 40 20 HIS 41 21 PRO 42 22 PHE 43 23 GLY 44 24 PHE 45 25 VAL 46 26 ALA 47 27 VAL 48 28 PRO 49 29 THR 50 30 LYS 51 31 ASN 52 32 PRO 53 33 ASP 54 34 GLY 55 35 THR 56 36 MET 57 37 ASN 58 38 LEU 59 39 MET 60 40 ASN 61 41 TRP 62 42 GLU 63 43 CYS 64 44 ALA 65 45 ILE 66 46 PRO 67 47 GLY 68 48 LYS 69 49 LYS 70 50 GLY 71 51 THR 72 52 PRO 73 53 TRP 74 54 GLU 75 55 GLY 76 56 GLY 77 57 LEU 78 58 PHE 79 59 LYS 80 60 LEU 81 61 ARG 82 62 MET 83 63 LEU 84 64 PHE 85 65 LYS 86 66 ASP 87 67 ASP 88 68 TYR 89 69 PRO 90 70 SER 91 71 SER 92 72 PRO 93 73 PRO 94 74 LYS 95 75 CYS 96 76 LYS 97 77 PHE 98 78 GLU 99 79 PRO 100 80 PRO 101 81 LEU 102 82 PHE 103 83 HIS 104 84 PRO 105 85 ASN 106 86 VAL 107 87 TYR 108 88 PRO 109 89 SER 110 90 GLY 111 91 THR 112 92 VAL 113 93 CYS 114 94 LEU 115 95 SER 116 96 ILE 117 97 LEU 118 98 GLU 119 99 GLU 120 100 ASP 121 101 LYS 122 102 ASP 123 103 TRP 124 104 ARG 125 105 PRO 126 106 ALA 127 107 ILE 128 108 THR 129 109 ILE 130 110 LYS 131 111 GLN 132 112 ILE 133 113 LEU 134 114 LEU 135 115 GLY 136 116 ILE 137 117 GLN 138 118 GLU 139 119 LEU 140 120 LEU 141 121 ASN 142 122 GLU 143 123 LEU 144 124 ASN 145 125 ILE 146 126 GLN 147 127 ASP 148 128 PRO 149 129 ALA 150 130 GLN 151 131 ALA 152 132 GLU 153 133 ALA 154 134 TYR 155 135 THR 156 136 ILE 157 137 TYR 158 138 CYS 159 139 GLN 160 140 ASN 161 141 ARG 162 142 VAL 163 143 GLU 164 144 TYR 165 145 GLU 166 146 LYS 167 147 ARG 168 148 VAL 169 149 ARG 170 150 ALA 171 151 GLN 172 152 ALA 173 153 LYS 174 154 LYS 175 155 PHE 176 156 ALA 177 157 PRO 178 158 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 $UBC9(P123L) 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 $UBC9(P123L) 'recombinant technology' . Escherichia coli . pET28b 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 $UBC9(P123L) 500 uM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 120 mM 'natural abundance' D2O 5 % 'natural abundance' 'Glutamic acid' 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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 Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.14 . M pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_Standard _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 internal indirect . . . 0.25145 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.11329 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $Standard _Mol_system_component_name 'UBC9_P123L monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 21 MET H H 8.357 . . 2 1 21 MET CA C 56.431 . . 3 1 21 MET CB C 32.623 . . 4 1 21 MET N N 120.986 . . 5 2 22 SER H H 8.47 . . 6 2 22 SER CA C 59.568 . . 7 2 22 SER CB C 64 . . 8 2 22 SER N N 116.321 . . 9 3 23 GLY H H 8.506 . . 10 3 23 GLY CA C 46.823 . . 11 3 23 GLY N N 110.218 . . 12 4 24 ILE H H 8.025 . . 13 4 24 ILE CA C 63.968 . . 14 4 24 ILE CB C 37.766 . . 15 4 24 ILE N N 121.42 . . 16 5 25 ALA H H 8.204 . . 17 5 25 ALA CA C 56.75 . . 18 5 25 ALA CB C 19.006 . . 19 5 25 ALA N N 124.688 . . 20 6 26 LEU H H 8.427 . . 21 6 26 LEU CA C 58.394 . . 22 6 26 LEU CB C 41.649 . . 23 6 26 LEU N N 115.122 . . 24 7 27 SER H H 8.148 . . 25 7 27 SER CA C 61.968 . . 26 7 27 SER CB C 62.92 . . 27 7 27 SER N N 115.578 . . 28 8 28 ARG H H 8.175 . . 29 8 28 ARG CA C 57.979 . . 30 8 28 ARG CB C 28.077 . . 31 8 28 ARG N N 123.441 . . 32 9 29 LEU H H 9.158 . . 33 9 29 LEU CA C 58.966 . . 34 9 29 LEU CB C 42.629 . . 35 9 29 LEU N N 121.816 . . 36 10 30 ALA H H 8.355 . . 37 10 30 ALA CA C 55.626 . . 38 10 30 ALA CB C 18.04 . . 39 10 30 ALA N N 121.976 . . 40 11 31 GLN H H 7.84 . . 41 11 31 GLN CA C 59.437 . . 42 11 31 GLN CB C 28.14 . . 43 11 31 GLN N N 120.192 . . 44 12 32 GLU H H 9.158 . . 45 12 32 GLU CA C 60.111 . . 46 12 32 GLU CB C 29.705 . . 47 12 32 GLU N N 121.7 . . 48 13 33 ARG H H 8.788 . . 49 13 33 ARG CA C 60.713 . . 50 13 33 ARG CB C 29.069 . . 51 13 33 ARG N N 120.314 . . 52 14 34 LYS H H 7.952 . . 53 14 34 LYS CA C 60.398 . . 54 14 34 LYS CB C 32.762 . . 55 14 34 LYS N N 119.807 . . 56 15 35 ALA H H 8.521 . . 57 15 35 ALA CA C 55.489 . . 58 15 35 ALA CB C 18.528 . . 59 15 35 ALA N N 121.837 . . 60 16 36 TRP H H 8.833 . . 61 16 36 TRP CA C 60.608 . . 62 16 36 TRP CB C 29.082 . . 63 16 36 TRP N N 119.85 . . 64 17 37 ARG H H 8.342 . . 65 17 37 ARG CA C 59.607 . . 66 17 37 ARG CB C 30.501 . . 67 17 37 ARG N N 116.581 . . 68 18 38 LYS H H 7.497 . . 69 18 38 LYS CA C 58.497 . . 70 18 38 LYS CB C 33.22 . . 71 18 38 LYS N N 117.489 . . 72 19 39 ASP H H 7.803 . . 73 19 39 ASP CA C 54.51 . . 74 19 39 ASP CB C 42.81 . . 75 19 39 ASP N N 117.737 . . 76 20 40 HIS H H 7.706 . . 77 20 40 HIS CA C 53.152 . . 78 20 40 HIS CB C 26.3 . . 79 20 40 HIS N N 117.349 . . 80 21 41 PRO CA C 62.297 . . 81 21 41 PRO CB C 31.5 . . 82 22 42 PHE H H 8.823 . . 83 22 42 PHE CA C 60.739 . . 84 22 42 PHE CB C 39.403 . . 85 22 42 PHE N N 124.375 . . 86 23 43 GLY H H 8.657 . . 87 23 43 GLY CA C 45.223 . . 88 23 43 GLY N N 115.622 . . 89 24 44 PHE H H 7.833 . . 90 24 44 PHE CA C 57.708 . . 91 24 44 PHE CB C 42.337 . . 92 24 44 PHE N N 117.544 . . 93 25 45 VAL H H 8.718 . . 94 25 45 VAL CA C 61.523 . . 95 25 45 VAL CB C 35.593 . . 96 25 45 VAL N N 120.555 . . 97 26 46 ALA H H 8.36 . . 98 26 46 ALA CA C 53.955 . . 99 26 46 ALA CB C 17.806 . . 100 26 46 ALA N N 127.711 . . 101 27 47 VAL H H 8.499 . . 102 27 47 VAL CA C 57.997 . . 103 27 47 VAL CB C 35.9 . . 104 27 47 VAL N N 120.46 . . 105 28 48 PRO CA C 62.563 . . 106 28 48 PRO CB C 32.102 . . 107 29 49 THR H H 8.272 . . 108 29 49 THR CA C 62.234 . . 109 29 49 THR CB C 71.184 . . 110 29 49 THR N N 114.046 . . 111 30 50 LYS H H 8.372 . . 112 30 50 LYS CA C 55.376 . . 113 30 50 LYS CB C 34.756 . . 114 30 50 LYS N N 118.951 . . 115 31 51 ASN H H 9.212 . . 116 31 51 ASN CA C 52.466 . . 117 31 51 ASN CB C 38.6 . . 118 31 51 ASN N N 121.85 . . 119 32 52 PRO CA C 65.907 . . 120 32 52 PRO CB C 31.707 . . 121 33 53 ASP H H 7.55 . . 122 33 53 ASP CA C 53.455 . . 123 33 53 ASP CB C 39.983 . . 124 33 53 ASP N N 113.082 . . 125 34 54 GLY H H 8.409 . . 126 34 54 GLY CA C 45.537 . . 127 34 54 GLY N N 108.289 . . 128 35 55 THR H H 8.082 . . 129 35 55 THR CA C 61.968 . . 130 35 55 THR CB C 71.76 . . 131 35 55 THR N N 112.075 . . 132 36 56 MET H H 8.682 . . 133 36 56 MET CA C 56.223 . . 134 36 56 MET CB C 33.806 . . 135 36 56 MET N N 118.73 . . 136 37 57 ASN H H 9.169 . . 137 37 57 ASN CA C 51.152 . . 138 37 57 ASN CB C 37.23 . . 139 37 57 ASN N N 122.733 . . 140 38 58 LEU H H 8.542 . . 141 38 58 LEU CA C 56.221 . . 142 38 58 LEU CB C 42.037 . . 143 38 58 LEU N N 120.194 . . 144 39 59 MET H H 7.823 . . 145 39 59 MET CA C 55.308 . . 146 39 59 MET CB C 30.822 . . 147 39 59 MET N N 110.213 . . 148 40 60 ASN H H 7.292 . . 149 40 60 ASN CA C 52.837 . . 150 40 60 ASN CB C 40.621 . . 151 40 60 ASN N N 119.591 . . 152 41 61 TRP H H 9.861 . . 153 41 61 TRP CA C 56.668 . . 154 41 61 TRP CB C 31.1 . . 155 41 61 TRP N N 126.031 . . 156 42 62 GLU H H 9.083 . . 157 42 62 GLU CA C 56.528 . . 158 42 62 GLU CB C 31.087 . . 159 42 62 GLU N N 121.846 . . 160 43 63 CYS H H 9.125 . . 161 43 63 CYS CA C 55.319 . . 162 43 63 CYS CB C 31.978 . . 163 43 63 CYS N N 121.836 . . 164 44 64 ALA H H 9.434 . . 165 44 64 ALA CA C 52.523 . . 166 44 64 ALA CB C 21.655 . . 167 44 64 ALA N N 124.756 . . 168 45 65 ILE H H 8.738 . . 169 45 65 ILE CA C 56.679 . . 170 45 65 ILE N N 119.533 . . 171 46 66 PRO CA C 61.481 . . 172 46 66 PRO CB C 31.969 . . 173 47 67 GLY H H 8.484 . . 174 47 67 GLY CA C 45.55 . . 175 47 67 GLY N N 105.898 . . 176 48 68 LYS H H 9.138 . . 177 48 68 LYS CA C 57.866 . . 178 48 68 LYS CB C 33.439 . . 179 48 68 LYS N N 124.919 . . 180 49 69 LYS H H 8.977 . . 181 49 69 LYS CA C 58.335 . . 182 49 69 LYS CB C 32.559 . . 183 49 69 LYS N N 127.867 . . 184 50 70 GLY H H 9.557 . . 185 50 70 GLY CA C 45.819 . . 186 50 70 GLY N N 112.58 . . 187 51 71 THR H H 7.736 . . 188 51 71 THR CA C 59.721 . . 189 51 71 THR CB C 71.4 . . 190 51 71 THR N N 108.787 . . 191 52 72 PRO CA C 64.83 . . 192 52 72 PRO CB C 31.284 . . 193 53 73 TRP H H 7.443 . . 194 53 73 TRP CA C 56.921 . . 195 53 73 TRP CB C 29.195 . . 196 53 73 TRP N N 117.629 . . 197 54 74 GLU H H 7.828 . . 198 54 74 GLU CA C 58.699 . . 199 54 74 GLU CB C 30.009 . . 200 54 74 GLU N N 120.523 . . 201 55 75 GLY H H 9.399 . . 202 55 75 GLY CA C 44.886 . . 203 55 75 GLY N N 114.844 . . 204 56 76 GLY H H 7.798 . . 205 56 76 GLY CA C 45.315 . . 206 56 76 GLY N N 103.975 . . 207 57 77 LEU H H 7.933 . . 208 57 77 LEU CA C 54.739 . . 209 57 77 LEU CB C 44.123 . . 210 57 77 LEU N N 126.454 . . 211 58 78 PHE H H 8.709 . . 212 58 78 PHE CA C 57.394 . . 213 58 78 PHE CB C 40.105 . . 214 58 78 PHE N N 126.294 . . 215 59 79 LYS H H 8.449 . . 216 59 79 LYS CA C 57.427 . . 217 59 79 LYS CB C 33.4 . . 218 59 79 LYS N N 125.06 . . 219 60 80 LEU H H 8.685 . . 220 60 80 LEU CA C 54 . . 221 60 80 LEU CB C 46.297 . . 222 60 80 LEU N N 124.814 . . 223 61 81 ARG H H 9.325 . . 224 61 81 ARG CA C 54.4 . . 225 61 81 ARG CB C 33.203 . . 226 61 81 ARG N N 127.319 . . 227 62 82 MET H H 9.067 . . 228 62 82 MET CA C 54.907 . . 229 62 82 MET CB C 36.758 . . 230 62 82 MET N N 125.974 . . 231 63 83 LEU H H 8.664 . . 232 63 83 LEU CA C 53.594 . . 233 63 83 LEU CB C 43.997 . . 234 63 83 LEU N N 124.224 . . 235 64 84 PHE H H 8.635 . . 236 64 84 PHE CA C 57.8 . . 237 64 84 PHE CB C 41.952 . . 238 64 84 PHE N N 123.035 . . 239 65 85 LYS H H 8.69 . . 240 65 85 LYS CA C 55.294 . . 241 65 85 LYS CB C 34.406 . . 242 65 85 LYS N N 120.984 . . 243 66 86 ASP H H 8.441 . . 244 66 86 ASP CA C 57.068 . . 245 66 86 ASP CB C 40.839 . . 246 66 86 ASP N N 117.083 . . 247 67 87 ASP H H 7.893 . . 248 67 87 ASP CA C 52.779 . . 249 67 87 ASP CB C 39.675 . . 250 67 87 ASP N N 112.882 . . 251 68 88 TYR H H 8.037 . . 252 68 88 TYR CA C 57.623 . . 253 68 88 TYR CB C 39 . . 254 68 88 TYR N N 126.303 . . 255 69 89 PRO CA C 64.25 . . 256 69 89 PRO CB C 32.469 . . 257 70 90 SER H H 9.191 . . 258 70 90 SER CA C 62.868 . . 259 70 90 SER CB C 62.868 . . 260 70 90 SER N N 121.892 . . 261 71 91 SER H H 7.284 . . 262 71 91 SER CA C 53.492 . . 263 71 91 SER N N 112.798 . . 264 73 93 PRO CA C 61.681 . . 265 73 93 PRO CB C 30.596 . . 266 74 94 LYS H H 8.325 . . 267 74 94 LYS CA C 55.237 . . 268 74 94 LYS CB C 33.563 . . 269 74 94 LYS N N 119.572 . . 270 75 95 CYS H H 8.929 . . 271 75 95 CYS CA C 57.65 . . 272 75 95 CYS CB C 29.916 . . 273 75 95 CYS N N 123.033 . . 274 76 96 LYS H H 8.867 . . 275 76 96 LYS CA C 54.094 . . 276 76 96 LYS CB C 36.174 . . 277 76 96 LYS N N 122.567 . . 278 77 97 PHE H H 9.005 . . 279 77 97 PHE CA C 61.023 . . 280 77 97 PHE CB C 40.337 . . 281 77 97 PHE N N 126.424 . . 282 78 98 GLU H H 7.983 . . 283 78 98 GLU CA C 52.879 . . 284 78 98 GLU CB C 33.1 . . 285 78 98 GLU N N 123.872 . . 286 80 100 PRO CA C 64.566 . . 287 80 100 PRO CB C 33 . . 288 81 101 LEU H H 5.64 . . 289 81 101 LEU CA C 53.326 . . 290 81 101 LEU CB C 45.782 . . 291 81 101 LEU N N 118.589 . . 292 82 102 PHE H H 9.505 . . 293 82 102 PHE CA C 58.834 . . 294 82 102 PHE CB C 39.5 . . 295 82 102 PHE N N 124.724 . . 296 83 103 HIS H H 6.854 . . 297 83 103 HIS CA C 57.2 . . 298 83 103 HIS N N 124.496 . . 299 84 104 PRO CA C 66.7 . . 300 85 105 ASN H H 12.08 . . 301 85 105 ASN CA C 54.145 . . 302 85 105 ASN CB C 42.4 . . 303 85 105 ASN N N 117.686 . . 304 86 106 VAL H H 7.301 . . 305 86 106 VAL CA C 61.6 . . 306 86 106 VAL CB C 34 . . 307 86 106 VAL N N 122.816 . . 308 87 107 TYR H H 9.121 . . 309 87 107 TYR CA C 59.5 . . 310 87 107 TYR N N 125.679 . . 311 88 108 PRO CA C 65.914 . . 312 88 108 PRO CB C 31.671 . . 313 89 109 SER H H 7.616 . . 314 89 109 SER CA C 58.923 . . 315 89 109 SER CB C 64.355 . . 316 89 109 SER N N 107.182 . . 317 90 110 GLY H H 9.136 . . 318 90 110 GLY CA C 45.35 . . 319 90 110 GLY N N 111.295 . . 320 91 111 THR H H 7.885 . . 321 91 111 THR CA C 64.996 . . 322 91 111 THR CB C 69.2 . . 323 91 111 THR N N 119.608 . . 324 92 112 VAL H H 8.41 . . 325 92 112 VAL CA C 63.408 . . 326 92 112 VAL CB C 33.406 . . 327 92 112 VAL N N 126.211 . . 328 93 113 CYS H H 8.388 . . 329 93 113 CYS CA C 58.221 . . 330 93 113 CYS CB C 27.24 . . 331 93 113 CYS N N 127.723 . . 332 94 114 LEU H H 7.686 . . 333 94 114 LEU CA C 54.25 . . 334 94 114 LEU CB C 46.31 . . 335 94 114 LEU N N 125.95 . . 336 95 115 SER H H 9.309 . . 337 95 115 SER CA C 63.81 . . 338 95 115 SER CB C 62.314 . . 339 95 115 SER N N 124.042 . . 340 96 116 ILE H H 7.471 . . 341 96 116 ILE CA C 64.6 . . 342 96 116 ILE CB C 38.589 . . 343 96 116 ILE N N 114.207 . . 344 97 117 LEU H H 7.785 . . 345 97 117 LEU CA C 53.108 . . 346 97 117 LEU CB C 41.395 . . 347 97 117 LEU N N 114.448 . . 348 98 118 GLU H H 7.415 . . 349 98 118 GLU CA C 55.41 . . 350 98 118 GLU CB C 31.6 . . 351 98 118 GLU N N 118.335 . . 352 99 119 GLU H H 9.602 . . 353 99 119 GLU CA C 59.91 . . 354 99 119 GLU CB C 30.039 . . 355 99 119 GLU N N 128.128 . . 356 100 120 ASP H H 8.948 . . 357 100 120 ASP CA C 54.252 . . 358 100 120 ASP CB C 40.137 . . 359 100 120 ASP N N 114.351 . . 360 101 121 LYS H H 7.713 . . 361 101 121 LYS CA C 56.066 . . 362 101 121 LYS CB C 33.089 . . 363 101 121 LYS N N 120.088 . . 364 102 122 ASP H H 7.582 . . 365 102 122 ASP CA C 55.194 . . 366 102 122 ASP CB C 42.81 . . 367 102 122 ASP N N 118.086 . . 368 103 123 TRP H H 7.559 . . 369 103 123 TRP CA C 60.01 . . 370 103 123 TRP CB C 29.939 . . 371 103 123 TRP N N 120.09 . . 372 104 124 ARG H H 5.935 . . 373 104 124 ARG CA C 52.221 . . 374 104 124 ARG CB C 32.8 . . 375 104 124 ARG N N 126.369 . . 376 105 125 PRO CA C 64.481 . . 377 105 125 PRO CB C 32.185 . . 378 106 126 ALA H H 7.031 . . 379 106 126 ALA CA C 52.863 . . 380 106 126 ALA CB C 19.311 . . 381 106 126 ALA N N 114.562 . . 382 107 127 ILE H H 7.328 . . 383 107 127 ILE CA C 63.811 . . 384 107 127 ILE CB C 36.109 . . 385 107 127 ILE N N 121.485 . . 386 108 128 THR H H 7.793 . . 387 108 128 THR CA C 60.397 . . 388 108 128 THR CB C 73.021 . . 389 108 128 THR N N 117.18 . . 390 109 129 ILE H H 9.743 . . 391 109 129 ILE CA C 67.3 . . 392 109 129 ILE CB C 37.223 . . 393 109 129 ILE N N 121.094 . . 394 110 130 LYS H H 8.262 . . 395 110 130 LYS CA C 61.426 . . 396 110 130 LYS CB C 32.854 . . 397 110 130 LYS N N 117.835 . . 398 111 131 GLN H H 7.75 . . 399 111 131 GLN CA C 59.6 . . 400 111 131 GLN CB C 29.005 . . 401 111 131 GLN N N 116.833 . . 402 112 132 ILE H H 8.335 . . 403 112 132 ILE CA C 66.568 . . 404 112 132 ILE CB C 38.539 . . 405 112 132 ILE N N 120.954 . . 406 113 133 LEU H H 8.489 . . 407 113 133 LEU CA C 58.894 . . 408 113 133 LEU CB C 41.208 . . 409 113 133 LEU N N 117.566 . . 410 114 134 LEU H H 8.628 . . 411 114 134 LEU CA C 58.626 . . 412 114 134 LEU CB C 42.5 . . 413 114 134 LEU N N 119.76 . . 414 115 135 GLY H H 8.275 . . 415 115 135 GLY CA C 47.081 . . 416 115 135 GLY N N 109.278 . . 417 116 136 ILE H H 8.669 . . 418 116 136 ILE CA C 65.882 . . 419 116 136 ILE CB C 37.571 . . 420 116 136 ILE N N 123.635 . . 421 117 137 GLN H H 8.537 . . 422 117 137 GLN CA C 60.031 . . 423 117 137 GLN CB C 29.1 . . 424 117 137 GLN N N 118.464 . . 425 118 138 GLU CA C 59.3 . . 426 118 138 GLU CB C 29.603 . . 427 119 139 LEU H H 7.416 . . 428 119 139 LEU CA C 56.152 . . 429 119 139 LEU CB C 43.6 . . 430 119 139 LEU N N 119.698 . . 431 120 140 LEU CA C 57.6 . . 432 120 140 LEU CB C 39.3 . . 433 121 141 ASN CA C 55 . . 434 121 141 ASN CB C 41.6 . . 435 122 142 GLU CA C 53.8 . . 436 122 142 GLU CB C 30.9 . . 437 123 143 LEU CA C 63.779 . . 438 123 143 LEU CB C 32.8 . . 439 124 144 ASN H H 9.345 . . 440 124 144 ASN CA C 52.1 . . 441 124 144 ASN CB C 39.5 . . 442 124 144 ASN N N 121.852 . . 443 126 146 GLN H H 8.089 . . 444 126 146 GLN CA C 56.692 . . 445 126 146 GLN CB C 29.2 . . 446 126 146 GLN N N 118.476 . . 447 127 147 ASP CA C 52.2 . . 448 127 147 ASP CB C 42.6 . . 449 128 148 PRO CA C 63.5 . . 450 128 148 PRO CB C 32.491 . . 451 129 149 ALA H H 8.308 . . 452 129 149 ALA CA C 56.997 . . 453 129 149 ALA CB C 18.411 . . 454 129 149 ALA N N 123.673 . . 455 130 150 GLN CA C 56.605 . . 456 130 150 GLN CB C 31.4 . . 457 131 151 ALA H H 8.582 . . 458 131 151 ALA CA C 55.64 . . 459 131 151 ALA CB C 18.971 . . 460 131 151 ALA N N 126.401 . . 461 132 152 GLU H H 9.291 . . 462 132 152 GLU CA C 55.534 . . 463 132 152 GLU CB C 42.633 . . 464 132 152 GLU N N 119.975 . . 465 133 153 ALA H H 7.853 . . 466 133 153 ALA CA C 59.305 . . 467 133 153 ALA CB C 17.6 . . 468 133 153 ALA N N 118.859 . . 469 134 154 TYR H H 7.756 . . 470 134 154 TYR CA C 62.5 . . 471 134 154 TYR N N 116.082 . . 472 135 155 THR H H 8.73 . . 473 135 155 THR CA C 69.783 . . 474 135 155 THR CB C 69.7 . . 475 135 155 THR N N 116.91 . . 476 136 156 ILE CA C 65.7 . . 477 136 156 ILE CB C 38.8 . . 478 137 157 TYR H H 8.26 . . 479 137 157 TYR CA C 63.9 . . 480 137 157 TYR CB C 38.9 . . 481 137 157 TYR N N 119.675 . . 482 138 158 CYS H H 7.645 . . 483 138 158 CYS CA C 58.778 . . 484 138 158 CYS CB C 28.403 . . 485 138 158 CYS N N 112.616 . . 486 139 159 GLN H H 8.409 . . 487 139 159 GLN CA C 57.221 . . 488 139 159 GLN CB C 29.843 . . 489 139 159 GLN N N 117.348 . . 490 140 160 ASN H H 9.054 . . 491 140 160 ASN CA C 52.397 . . 492 140 160 ASN CB C 38.4 . . 493 140 160 ASN N N 119.159 . . 494 141 161 ARG H H 8.792 . . 495 141 161 ARG CA C 58.3 . . 496 141 161 ARG CB C 29.266 . . 497 141 161 ARG N N 125.333 . . 498 142 162 VAL H H 8.036 . . 499 142 162 VAL CA C 66.587 . . 500 142 162 VAL CB C 32.4 . . 501 142 162 VAL N N 118.216 . . 502 143 163 GLU H H 7.371 . . 503 143 163 GLU CA C 58.439 . . 504 143 163 GLU CB C 29.005 . . 505 143 163 GLU N N 122.212 . . 506 144 164 TYR H H 8.493 . . 507 144 164 TYR CA C 63.723 . . 508 144 164 TYR CB C 42.5 . . 509 144 164 TYR N N 120.147 . . 510 145 165 GLU H H 8.581 . . 511 145 165 GLU CA C 60.739 . . 512 145 165 GLU CB C 29.5 . . 513 145 165 GLU N N 117.329 . . 514 146 166 LYS H H 8 . . 515 146 166 LYS CA C 60.676 . . 516 146 166 LYS CB C 33.2 . . 517 146 166 LYS N N 119.927 . . 518 147 167 ARG H H 8.017 . . 519 147 167 ARG CA C 60.503 . . 520 147 167 ARG CB C 32.612 . . 521 147 167 ARG N N 119.86 . . 522 148 168 VAL H H 8.152 . . 523 148 168 VAL CA C 58.88 . . 524 148 168 VAL CB C 31.5 . . 525 148 168 VAL N N 120.089 . . 526 149 169 ARG CA C 60.6 . . 527 149 169 ARG CB C 30.7 . . 528 150 170 ALA CA C 55.9 . . 529 150 170 ALA CB C 18.5 . . 530 151 171 GLN H H 7.742 . . 531 151 171 GLN CA C 58.905 . . 532 151 171 GLN CB C 30.737 . . 533 151 171 GLN N N 120.539 . . 534 152 172 ALA H H 8.403 . . 535 152 172 ALA CA C 55.966 . . 536 152 172 ALA CB C 19 . . 537 152 172 ALA N N 122.927 . . 538 153 173 LYS CA C 58.8 . . 539 153 173 LYS CB C 32.9 . . 540 154 174 LYS CA C 59 . . 541 154 174 LYS CB C 32.9 . . 542 155 175 PHE CA C 56.779 . . 543 155 175 PHE CB C 37.439 . . 544 156 176 ALA H H 7.236 . . 545 156 176 ALA CA C 51.066 . . 546 156 176 ALA CB C 18.7 . . 547 156 176 ALA N N 126.247 . . 548 157 177 PRO CA C 63.7 . . 549 157 177 PRO CB C 32.5 . . 550 158 178 SER H H 8.04 . . 551 158 178 SER CA C 60.168 . . 552 158 178 SER CB C 65.7 . . 553 158 178 SER N N 121.719 . . stop_ save_