data_27512 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance ssignment of the human ubiquitin G76C mutant ; _BMRB_accession_number 27512 _BMRB_flat_file_name bmr27512.str _Entry_type original _Submission_date 2018-06-06 _Accession_date 2018-06-06 _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 Wiesner Silke . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 70 "13C chemical shifts" 142 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-12-07 update BMRB 'update entry citation' 2018-07-12 original author 'original release' stop_ _Original_release_date 2018-06-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Beta-Sheet Augmentation Is a Conserved Mechanism of Priming HECT E3 Ligases for Ubiquitin Ligation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29964046 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jaeckl Magnus . . 2 Stollmaier Carsten . . 3 Strohaeker Timo . . 4 Hyz Karolina . . 5 Maspero Elena . . 6 Polo Simona . . 7 Wiesner Silke . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 430 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3218 _Page_last 3233 _Year 2018 _Details . loop_ _Keyword 'HECT domain' thioester ubiquitin 'ubiquitin ligation' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ub _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ub $ub stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ubiquitination stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ub _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ub _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function ubiquitination stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 80 _Mol_residue_sequence ; GAMGMQIFVKTLTGKTITLE VEPSDTIENVKAKIQDKEGI PPDQQRLIFAGKQLEDGRTL SDYNIQKESTLHLVLRLRGC ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 ALA 3 -1 MET 4 0 GLY 5 1 MET 6 2 GLN 7 3 ILE 8 4 PHE 9 5 VAL 10 6 LYS 11 7 THR 12 8 LEU 13 9 THR 14 10 GLY 15 11 LYS 16 12 THR 17 13 ILE 18 14 THR 19 15 LEU 20 16 GLU 21 17 VAL 22 18 GLU 23 19 PRO 24 20 SER 25 21 ASP 26 22 THR 27 23 ILE 28 24 GLU 29 25 ASN 30 26 VAL 31 27 LYS 32 28 ALA 33 29 LYS 34 30 ILE 35 31 GLN 36 32 ASP 37 33 LYS 38 34 GLU 39 35 GLY 40 36 ILE 41 37 PRO 42 38 PRO 43 39 ASP 44 40 GLN 45 41 GLN 46 42 ARG 47 43 LEU 48 44 ILE 49 45 PHE 50 46 ALA 51 47 GLY 52 48 LYS 53 49 GLN 54 50 LEU 55 51 GLU 56 52 ASP 57 53 GLY 58 54 ARG 59 55 THR 60 56 LEU 61 57 SER 62 58 ASP 63 59 TYR 64 60 ASN 65 61 ILE 66 62 GLN 67 63 LYS 68 64 GLU 69 65 SER 70 66 THR 71 67 LEU 72 68 HIS 73 69 LEU 74 70 VAL 75 71 LEU 76 72 ARG 77 73 LEU 78 74 ARG 79 75 GLY 80 76 CYS 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 $ub 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 $ub 'recombinant technology' . Escherichia coli . pET-M11 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 $ub 2 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' DTT 1 mM 'natural abundance' D2O 10 '% w/v' '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . 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_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(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' 0.2 . M pH 6.4 . 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 water C 13 protons ppm 4.7 na indirect . . . 1 water H 1 protons ppm 4.7 internal indirect . . . 1 water N 15 protons ppm 4.7 na indirect . . . 1 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 HNCACB' '3D CBCA(CO)NH' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ub _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 5 MET H H 8.947 0.000 . 2 1 5 MET CA C 54.967 0.000 . 3 1 5 MET CB C 34.958 0.000 . 4 1 5 MET N N 119.902 0.000 . 5 2 6 GLN H H 8.255 0.000 . 6 2 6 GLN CA C 54.567 0.000 . 7 2 6 GLN CB C 30.956 0.000 . 8 2 6 GLN N N 121.324 0.000 . 9 3 7 ILE H H 8.330 0.000 . 10 3 7 ILE CA C 59.598 0.000 . 11 3 7 ILE CB C 42.218 0.000 . 12 3 7 ILE N N 114.417 0.000 . 13 4 8 PHE H H 8.624 0.000 . 14 4 8 PHE CA C 55.367 0.000 . 15 4 8 PHE CB C 41.304 0.000 . 16 4 8 PHE N N 118.784 0.000 . 17 5 9 VAL H H 9.312 0.000 . 18 5 9 VAL CA C 60.512 0.000 . 19 5 9 VAL CB C 34.272 0.000 . 20 5 9 VAL N N 121.527 0.000 . 21 6 10 LYS H H 8.997 0.000 . 22 6 10 LYS CA C 54.910 0.000 . 23 6 10 LYS CB C 34.386 0.000 . 24 6 10 LYS N N 128.128 0.000 . 25 7 11 THR H H 8.743 0.000 . 26 7 11 THR CA C 60.741 0.000 . 27 7 11 THR CB C 70.860 0.000 . 28 7 11 THR N N 115.433 0.000 . 29 8 12 LEU H H 9.098 0.000 . 30 8 12 LEU CA C 57.614 0.267 . 31 8 12 LEU CB C 42.061 0.175 . 32 8 12 LEU N N 121.324 0.000 . 33 9 13 THR H H 7.661 0.000 . 34 9 13 THR CA C 61.672 0.000 . 35 9 13 THR CB C 69.374 0.000 . 36 9 13 THR N N 132.015 0.000 . 37 10 14 GLY H H 7.837 0.000 . 38 10 14 GLY CA C 45.660 0.126 . 39 10 14 GLY N N 109.238 0.000 . 40 11 15 LYS H H 7.287 0.000 . 41 11 15 LYS CA C 56.511 0.000 . 42 11 15 LYS CB C 33.472 0.000 . 43 11 15 LYS N N 121.933 0.000 . 44 12 16 THR H H 8.622 0.000 . 45 12 16 THR CA C 62.513 0.000 . 46 12 16 THR CB C 70.002 0.000 . 47 12 16 THR N N 120.613 0.000 . 48 13 17 ILE H H 9.563 0.000 . 49 13 17 ILE CA C 60.398 0.000 . 50 13 17 ILE CB C 41.018 0.000 . 51 13 17 ILE N N 127.824 0.000 . 52 14 18 THR H H 8.742 0.000 . 53 14 18 THR CA C 62.399 0.000 . 54 14 18 THR CB C 69.774 0.000 . 55 14 18 THR N N 122.136 0.000 . 56 15 19 LEU H H 8.818 0.000 . 57 15 19 LEU CA C 53.023 0.000 . 58 15 19 LEU CB C 46.735 0.000 . 59 15 19 LEU N N 125.488 0.000 . 60 16 20 GLU H H 8.166 0.000 . 61 16 20 GLU CA C 55.939 0.000 . 62 16 20 GLU CB C 29.927 0.000 . 63 16 20 GLU N N 122.238 0.000 . 64 17 21 VAL H H 8.693 0.000 . 65 17 21 VAL CA C 59.111 0.028 . 66 17 21 VAL CB C 36.787 0.058 . 67 17 21 VAL N N 116.855 0.000 . 68 18 22 GLU H H 8.582 0.000 . 69 18 22 GLU CA C 54.030 0.000 . 70 18 22 GLU CB C 31.706 0.000 . 71 18 22 GLU N N 118.480 0.000 . 72 19 23 PRO CA C 65.772 0.000 . 73 19 23 PRO CB C 31.985 0.000 . 74 20 24 SER H H 7.121 0.000 . 75 20 24 SER CA C 57.711 0.000 . 76 20 24 SER CB C 63.485 0.000 . 77 20 24 SER N N 129.956 0.000 . 78 21 25 ASP H H 8.050 0.000 . 79 21 25 ASP CA C 56.317 0.060 . 80 21 25 ASP CB C 41.214 0.000 . 81 21 25 ASP N N 123.964 0.000 . 82 22 26 THR H H 7.831 0.000 . 83 22 26 THR CA C 59.907 0.081 . 84 22 26 THR CB C 71.486 0.054 . 85 22 26 THR N N 109.672 0.000 . 86 23 27 ILE H H 8.532 0.000 . 87 23 27 ILE CA C 62.755 0.000 . 88 23 27 ILE CB C 35.016 0.000 . 89 23 27 ILE N N 121.527 0.000 . 90 24 28 GLU CA C 60.855 0.000 . 91 24 28 GLU CB C 28.784 0.000 . 92 25 29 ASN H H 7.947 0.000 . 93 25 29 ASN CA C 56.168 0.000 . 94 25 29 ASN CB C 38.445 0.000 . 95 25 29 ASN N N 121.425 0.000 . 96 26 30 VAL H H 8.129 0.000 . 97 26 30 VAL CA C 68.116 0.000 . 98 26 30 VAL CB C 31.242 0.000 . 99 26 30 VAL N N 122.339 0.000 . 100 27 31 LYS H H 8.568 0.000 . 101 27 31 LYS CA C 59.426 0.000 . 102 27 31 LYS CB C 34.043 0.000 . 103 27 31 LYS N N 119.191 0.000 . 104 28 32 ALA H H 7.992 0.000 . 105 28 32 ALA CA C 55.596 0.000 . 106 28 32 ALA CB C 17.750 0.000 . 107 28 32 ALA N N 123.558 0.000 . 108 29 33 LYS H H 7.908 0.000 . 109 29 33 LYS CA C 60.112 0.000 . 110 29 33 LYS CB C 33.472 0.000 . 111 29 33 LYS N N 120.409 0.000 . 112 30 34 ILE H H 8.302 0.000 . 113 30 34 ILE CA C 66.344 0.000 . 114 30 34 ILE CB C 36.902 0.000 . 115 30 34 ILE N N 121.425 0.000 . 116 31 35 GLN H H 8.562 0.000 . 117 31 35 GLN CA C 60.284 0.000 . 118 31 35 GLN CB C 27.812 0.000 . 119 31 35 GLN N N 123.659 0.000 . 120 32 36 ASP H H 8.044 0.000 . 121 32 36 ASP CA C 57.711 0.000 . 122 32 36 ASP CB C 41.514 0.000 . 123 32 36 ASP N N 120.003 0.000 . 124 33 37 LYS H H 7.488 0.000 . 125 33 37 LYS CA C 58.340 0.000 . 126 33 37 LYS CB C 34.043 0.000 . 127 33 37 LYS N N 115.636 0.000 . 128 34 38 GLU H H 8.735 0.000 . 129 34 38 GLU CA C 55.653 0.000 . 130 34 38 GLU CB C 33.357 0.000 . 131 34 38 GLU N N 114.519 0.000 . 132 35 39 GLY H H 8.502 0.000 . 133 35 39 GLY CA C 46.163 0.000 . 134 35 39 GLY N N 108.933 0.000 . 135 36 40 ILE H H 6.175 0.000 . 136 36 40 ILE CA C 58.242 0.000 . 137 36 40 ILE CB C 40.853 0.000 . 138 36 40 ILE N N 120.511 0.000 . 139 38 42 PRO CA C 66.286 0.000 . 140 38 42 PRO CB C 32.900 0.000 . 141 39 43 ASP H H 8.544 0.000 . 142 39 43 ASP CA C 56.110 0.000 . 143 39 43 ASP CB C 39.989 0.000 . 144 39 43 ASP N N 113.706 0.000 . 145 40 44 GLN H H 7.815 0.000 . 146 40 44 GLN CA C 55.767 0.000 . 147 40 44 GLN CB C 30.099 0.000 . 148 40 44 GLN N N 116.956 0.000 . 149 41 45 GLN H H 7.482 0.000 . 150 41 45 GLN CA C 56.854 0.000 . 151 41 45 GLN CB C 31.528 0.000 . 152 41 45 GLN N N 118.074 0.000 . 153 42 46 ARG H H 8.508 0.000 . 154 42 46 ARG CA C 55.253 0.000 . 155 42 46 ARG CB C 31.757 0.000 . 156 42 46 ARG N N 123.152 0.000 . 157 43 47 LEU H H 8.793 0.000 . 158 43 47 LEU CA C 53.252 0.000 . 159 43 47 LEU CB C 45.877 0.000 . 160 43 47 LEU N N 124.472 0.000 . 161 44 48 ILE H H 9.149 0.000 . 162 44 48 ILE CA C 59.083 0.000 . 163 44 48 ILE CB C 41.361 0.000 . 164 44 48 ILE N N 122.644 0.000 . 165 45 49 PHE H H 8.859 0.000 . 166 45 49 PHE CA C 43.705 0.000 . 167 45 49 PHE CB C 56.739 0.000 . 168 45 49 PHE N N 125.081 0.000 . 169 46 50 ALA H H 9.005 0.000 . 170 46 50 ALA CA C 52.852 0.000 . 171 46 50 ALA CB C 16.550 0.000 . 172 46 50 ALA N N 133.003 0.000 . 173 47 51 GLY H H 8.093 0.000 . 174 47 51 GLY CA C 45.477 0.000 . 175 47 51 GLY N N 128.534 0.000 . 176 48 52 LYS H H 7.988 0.000 . 177 48 52 LYS CA C 54.681 0.000 . 178 48 52 LYS CB C 34.386 0.000 . 179 48 52 LYS N N 122.034 0.000 . 180 49 53 GLN H H 8.650 0.000 . 181 49 53 GLN CA C 56.282 0.000 . 182 49 53 GLN CB C 29.070 0.000 . 183 49 53 GLN N N 123.253 0.000 . 184 50 54 LEU H H 8.570 0.000 . 185 50 54 LEU CA C 54.510 0.000 . 186 50 54 LEU CB C 41.532 0.000 . 187 50 54 LEU N N 125.894 0.000 . 188 51 55 GLU H H 8.409 0.000 . 189 51 55 GLU CA C 56.225 0.000 . 190 51 55 GLU CB C 31.928 0.000 . 191 51 55 GLU N N 123.253 0.000 . 192 52 56 ASP H H 8.167 0.000 . 193 52 56 ASP CA C 56.557 0.000 . 194 52 56 ASP CB C 41.093 0.000 . 195 52 56 ASP N N 120.511 0.000 . 196 53 57 GLY H H 7.831 0.000 . 197 53 57 GLY CA C 45.485 0.122 . 198 53 57 GLY N N 109.672 0.000 . 199 54 58 ARG H H 7.477 0.000 . 200 54 58 ARG CA C 54.510 0.000 . 201 54 58 ARG CB C 32.786 0.000 . 202 54 58 ARG N N 119.394 0.000 . 203 55 59 THR H H 8.850 0.000 . 204 55 59 THR CA C 60.055 0.000 . 205 55 59 THR CB C 72.575 0.000 . 206 55 59 THR N N 108.933 0.000 . 207 56 60 LEU H H 8.208 0.000 . 208 56 60 LEU CA C 58.855 0.000 . 209 56 60 LEU CB C 40.503 0.000 . 210 56 60 LEU N N 117.972 0.000 . 211 57 61 SER H H 8.391 0.000 . 212 57 61 SER CA C 61.313 0.000 . 213 57 61 SER CB C 62.742 0.000 . 214 57 61 SER N N 113.402 0.000 . 215 58 62 ASP H H 7.964 0.000 . 216 58 62 ASP CA C 57.711 0.000 . 217 58 62 ASP CB C 40.389 0.000 . 218 58 62 ASP N N 124.675 0.000 . 219 59 63 TYR H H 7.263 0.000 . 220 59 63 TYR CA C 58.569 0.000 . 221 59 63 TYR CB C 40.103 0.000 . 222 59 63 TYR N N 115.839 0.000 . 223 60 64 ASN H H 8.164 0.000 . 224 60 64 ASN CA C 54.453 0.000 . 225 60 64 ASN CB C 37.531 0.000 . 226 60 64 ASN N N 116.042 0.000 . 227 61 65 ILE H H 7.297 0.000 . 228 61 65 ILE CA C 62.628 0.000 . 229 61 65 ILE CB C 36.787 0.000 . 230 61 65 ILE N N 119.089 0.000 . 231 62 66 GLN H H 7.643 0.000 . 232 62 66 GLN CA C 53.881 0.000 . 233 62 66 GLN CB C 31.871 0.000 . 234 62 66 GLN N N 124.878 0.000 . 235 63 67 LYS H H 8.475 0.000 . 236 63 67 LYS CA C 58.283 0.000 . 237 63 67 LYS CB C 32.671 0.000 . 238 63 67 LYS N N 120.308 0.000 . 239 64 68 GLU H H 9.279 0.000 . 240 64 68 GLU CA C 58.740 0.000 . 241 64 68 GLU CB C 26.097 0.000 . 242 64 68 GLU N N 115.027 0.000 . 243 65 69 SER H H 7.707 0.000 . 244 65 69 SER CA C 61.370 0.000 . 245 65 69 SER CB C 65.143 0.000 . 246 65 69 SER N N 115.128 0.000 . 247 66 70 THR H H 8.701 0.000 . 248 66 70 THR CA C 62.685 0.000 . 249 66 70 THR CB C 70.577 0.000 . 250 66 70 THR N N 117.566 0.000 . 251 67 71 LEU H H 9.433 0.000 . 252 67 71 LEU CA C 54.167 0.000 . 253 67 71 LEU CB C 44.677 0.000 . 254 67 71 LEU N N 128.027 0.000 . 255 68 72 HIS H H 9.226 0.000 . 256 68 72 HIS CA C 56.396 0.000 . 257 68 72 HIS CB C 32.614 0.000 . 258 68 72 HIS N N 119.800 0.000 . 259 69 73 LEU H H 8.315 0.000 . 260 69 73 LEU CA C 54.052 0.000 . 261 69 73 LEU CB C 44.334 0.000 . 262 69 73 LEU N N 123.964 0.000 . 263 70 74 VAL H H 9.170 0.000 . 264 70 74 VAL CA C 60.855 0.000 . 265 70 74 VAL CB C 34.901 0.000 . 266 70 74 VAL N N 126.706 0.000 . 267 71 75 LEU H H 8.088 0.000 . 268 71 75 LEU CA C 54.167 0.000 . 269 71 75 LEU CB C 42.962 0.000 . 270 71 75 LEU N N 123.253 0.000 . 271 72 76 ARG H H 8.605 0.000 . 272 72 76 ARG CA C 55.996 0.000 . 273 72 76 ARG CB C 31.185 0.000 . 274 72 76 ARG N N 123.761 0.000 . 275 73 77 LEU H H 8.346 0.000 . 276 73 77 LEU CA C 55.424 0.000 . 277 73 77 LEU CB C 42.561 0.000 . 278 73 77 LEU N N 125.183 0.000 . 279 74 78 ARG H H 7.852 0.000 . 280 74 78 ARG CA C 57.701 0.000 . 281 74 78 ARG CB C 32.007 0.000 . 282 74 78 ARG N N 125.995 0.000 . stop_ save_