data_50362 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; BBP28(50-148) reduced ; _BMRB_accession_number 50362 _BMRB_flat_file_name bmr50362.str _Entry_type original _Submission_date 2020-06-25 _Accession_date 2020-06-25 _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 Fridmanis Jekabs . . 2 Otikovs Martins . . 3 Brangulis Kalvis . . 4 Jaudzems Kristaps . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 95 "13C chemical shifts" 183 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-11-03 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 50360 'BBP28(23-148) oxidized' stop_ _Original_release_date 2020-06-25 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32949018 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fridmanis Jekabs . . 2 Otikovs Martins . . 3 Brangulis Kalvis . . 4 Tars Kaspars . . 5 Jaudzems Kristaps . . stop_ _Journal_abbreviation 'Proteins: Struct. Funct. Bioinf.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'BBP28(50-148) reduced' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BBP28 $entity_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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; GAMGPKSKEELLREKLSEDQ KTHLDWLKEALGNDGEFDKF LGYDESKIKTALDHIKSELD KCNGNDADQQKTTFKQTVQG ALSGGIDGFGSNNAVTTCGN GS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 GLY 5 PRO 6 LYS 7 SER 8 LYS 9 GLU 10 GLU 11 LEU 12 LEU 13 ARG 14 GLU 15 LYS 16 LEU 17 SER 18 GLU 19 ASP 20 GLN 21 LYS 22 THR 23 HIS 24 LEU 25 ASP 26 TRP 27 LEU 28 LYS 29 GLU 30 ALA 31 LEU 32 GLY 33 ASN 34 ASP 35 GLY 36 GLU 37 PHE 38 ASP 39 LYS 40 PHE 41 LEU 42 GLY 43 TYR 44 ASP 45 GLU 46 SER 47 LYS 48 ILE 49 LYS 50 THR 51 ALA 52 LEU 53 ASP 54 HIS 55 ILE 56 LYS 57 SER 58 GLU 59 LEU 60 ASP 61 LYS 62 CYS 63 ASN 64 GLY 65 ASN 66 ASP 67 ALA 68 ASP 69 GLN 70 GLN 71 LYS 72 THR 73 THR 74 PHE 75 LYS 76 GLN 77 THR 78 VAL 79 GLN 80 GLY 81 ALA 82 LEU 83 SER 84 GLY 85 GLY 86 ILE 87 ASP 88 GLY 89 PHE 90 GLY 91 SER 92 ASN 93 ASN 94 ALA 95 VAL 96 THR 97 THR 98 CYS 99 GLY 100 ASN 101 GLY 102 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'Borreliella burgdorferi' 224326 Bacteria . Borreliella burgdorferi stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli . plasmid pETm11 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 $entity_1 2 mM '[U-100% 13C; U-100% 15N]' 'sodium azide' 0.03 % 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' EDTA 1 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name TOPSPIN _Version 3.5 loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.08 . M pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 4.77 internal indirect . . . . water H 1 protons ppm 4.77 internal direct . . . 1 water N 15 protons ppm 4.77 internal indirect . . . . 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' '3D HNCO' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name BBP28 _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 5 5 PRO CA C 62.944 0.3 1 2 5 5 PRO CB C 32.154 0.3 1 3 6 6 LYS H H 8.302 0.02 1 4 6 6 LYS CA C 56.53 0.3 1 5 6 6 LYS CB C 34.446 0.3 1 6 6 6 LYS N N 121.732 0.3 1 7 7 7 SER H H 8.81 0.02 1 8 7 7 SER CA C 57.496 0.3 1 9 7 7 SER CB C 65.422 0.3 1 10 7 7 SER N N 118.875 0.3 1 11 8 8 LYS H H 8.756 0.02 1 12 8 8 LYS CA C 60.109 0.3 1 13 8 8 LYS CB C 32.704 0.3 1 14 8 8 LYS N N 120.995 0.3 1 15 9 9 GLU H H 8.748 0.02 1 16 9 9 GLU CA C 60.082 0.3 1 17 9 9 GLU CB C 29.8 0.3 1 18 9 9 GLU N N 119.662 0.3 1 19 10 10 GLU H H 7.952 0.02 1 20 10 10 GLU CA C 60.073 0.3 1 21 10 10 GLU CB C 29.968 0.3 1 22 10 10 GLU N N 120.284 0.3 1 23 11 11 LEU H H 8.298 0.02 1 24 11 11 LEU CA C 57.865 0.3 1 25 11 11 LEU CB C 42.145 0.3 1 26 11 11 LEU N N 119.15 0.3 1 27 12 12 LEU CA C 57.551 0.3 1 28 12 12 LEU CB C 41.015 0.3 1 29 13 13 ARG H H 8.427 0.02 1 30 13 13 ARG CA C 60.979 0.3 1 31 13 13 ARG CB C 30.58 0.3 1 32 13 13 ARG N N 117.137 0.3 1 33 14 14 GLU H H 7.301 0.02 1 34 14 14 GLU CA C 58.836 0.3 1 35 14 14 GLU CB C 29.993 0.3 1 36 14 14 GLU N N 115.047 0.3 1 37 15 15 LYS H H 7.975 0.02 1 38 15 15 LYS CA C 55.856 0.3 1 39 15 15 LYS CB C 33.188 0.3 1 40 15 15 LYS N N 116.697 0.3 1 41 16 16 LEU H H 7.19 0.02 1 42 16 16 LEU CA C 53.847 0.3 1 43 16 16 LEU CB C 43.642 0.3 1 44 16 16 LEU N N 118.43 0.3 1 45 17 17 SER H H 8.88 0.02 1 46 17 17 SER CA C 57.162 0.3 1 47 17 17 SER CB C 65.325 0.3 1 48 17 17 SER N N 117.241 0.3 1 49 18 18 GLU H H 9.002 0.02 1 50 18 18 GLU CA C 60.51 0.3 1 51 18 18 GLU CB C 29.025 0.3 1 52 18 18 GLU N N 120.738 0.3 1 53 19 19 ASP H H 8.607 0.02 1 54 19 19 ASP CA C 57.63 0.3 1 55 19 19 ASP CB C 40.835 0.3 1 56 19 19 ASP N N 117.931 0.3 1 57 20 20 GLN H H 7.881 0.02 1 58 20 20 GLN CA C 58.834 0.3 1 59 20 20 GLN CB C 28.741 0.3 1 60 20 20 GLN N N 120.879 0.3 1 61 21 21 LYS H H 8.691 0.02 1 62 21 21 LYS CA C 61.447 0.3 1 63 21 21 LYS CB C 32.607 0.3 1 64 21 21 LYS N N 120.783 0.3 1 65 22 22 THR H H 7.888 0.02 1 66 22 22 THR CA C 66.135 0.3 1 67 22 22 THR CB C 68.714 0.3 1 68 22 22 THR N N 115.539 0.3 1 69 23 23 HIS H H 7.887 0.02 1 70 23 23 HIS CA C 62.452 0.3 1 71 23 23 HIS CB C 28.735 0.3 1 72 23 23 HIS N N 120.671 0.3 1 73 24 24 LEU H H 8.914 0.02 1 74 24 24 LEU CA C 58.147 0.3 1 75 24 24 LEU CB C 41.125 0.3 1 76 24 24 LEU N N 126.497 0.3 1 77 25 25 ASP H H 7.935 0.02 1 78 25 25 ASP CA C 57.93 0.3 1 79 25 25 ASP CB C 39.825 0.3 1 80 25 25 ASP N N 119.428 0.3 1 81 26 26 TRP H H 7.728 0.02 1 82 26 26 TRP CA C 61.761 0.3 1 83 26 26 TRP CB C 29.025 0.3 1 84 26 26 TRP N N 121.363 0.3 1 85 27 27 LEU H H 8.671 0.02 1 86 27 27 LEU CA C 57.932 0.3 1 87 27 27 LEU CB C 42.384 0.3 1 88 27 27 LEU N N 121.814 0.3 1 89 28 28 LYS H H 8.38 0.02 1 90 28 28 LYS CA C 60.108 0.3 1 91 28 28 LYS CB C 32.801 0.3 1 92 28 28 LYS N N 119.926 0.3 1 93 29 29 GLU H H 7.239 0.02 1 94 29 29 GLU CA C 58.6 0.3 1 95 29 29 GLU CB C 29.219 0.3 1 96 29 29 GLU N N 117.874 0.3 1 97 30 30 ALA H H 7.946 0.02 1 98 30 30 ALA CA C 54.75 0.3 1 99 30 30 ALA CB C 17.99 0.3 1 100 30 30 ALA N N 121.713 0.3 1 101 31 31 LEU H H 8.183 0.02 1 102 31 31 LEU CA C 56.454 0.3 1 103 31 31 LEU CB C 42.098 0.3 1 104 31 31 LEU N N 114.754 0.3 1 105 32 32 GLY H H 7.302 0.02 1 106 32 32 GLY CA C 46.971 0.3 1 107 32 32 GLY N N 105.421 0.3 1 108 33 33 ASN H H 8.332 0.02 1 109 33 33 ASN CA C 53.419 0.3 1 110 33 33 ASN CB C 39.964 0.3 1 111 33 33 ASN N N 117.072 0.3 1 112 34 34 ASP H H 8.779 0.02 1 113 34 34 ASP CA C 56.841 0.3 1 114 34 34 ASP CB C 40.646 0.3 1 115 34 34 ASP N N 124.863 0.3 1 116 35 35 GLY H H 8.433 0.02 1 117 35 35 GLY CA C 47.03 0.3 1 118 35 35 GLY N N 108.987 0.3 1 119 36 36 GLU H H 8.252 0.02 1 120 36 36 GLU CA C 58.694 0.3 1 121 36 36 GLU CB C 29.999 0.3 1 122 36 36 GLU N N 122.19 0.3 1 123 37 37 PHE H H 8.576 0.02 1 124 37 37 PHE CA C 61.849 0.3 1 125 37 37 PHE CB C 38.899 0.3 1 126 37 37 PHE N N 122.131 0.3 1 127 38 38 ASP H H 8.233 0.02 1 128 38 38 ASP CA C 57.898 0.3 1 129 38 38 ASP CB C 41.25 0.3 1 130 38 38 ASP N N 117.741 0.3 1 131 39 39 LYS H H 7.457 0.02 1 132 39 39 LYS CA C 59.539 0.3 1 133 39 39 LYS CB C 32.413 0.3 1 134 39 39 LYS N N 118.882 0.3 1 135 40 40 PHE H H 7.527 0.02 1 136 40 40 PHE CA C 60.508 0.3 1 137 40 40 PHE CB C 38.609 0.3 1 138 40 40 PHE N N 121.891 0.3 1 139 41 41 LEU H H 7.427 0.02 1 140 41 41 LEU CA C 55.856 0.3 1 141 41 41 LEU CB C 42.19 0.3 1 142 41 41 LEU N N 112.801 0.3 1 143 42 42 GLY H H 7.312 0.02 1 144 42 42 GLY CA C 44.901 0.3 1 145 42 42 GLY N N 104.119 0.3 1 146 43 43 TYR H H 7.119 0.02 1 147 43 43 TYR CA C 56.458 0.3 1 148 43 43 TYR CB C 38.517 0.3 1 149 43 43 TYR N N 120.679 0.3 1 150 44 44 ASP H H 8.181 0.02 1 151 44 44 ASP CA C 55.019 0.3 1 152 44 44 ASP CB C 42.674 0.3 1 153 44 44 ASP N N 117.178 0.3 1 154 45 45 GLU H H 8.848 0.02 1 155 45 45 GLU CA C 60.542 0.3 1 156 45 45 GLU CB C 30.381 0.3 1 157 45 45 GLU N N 124.066 0.3 1 158 46 46 SER H H 8.532 0.02 1 159 46 46 SER CA C 61.849 0.3 1 160 46 46 SER CB C 62.142 0.3 1 161 46 46 SER N N 113.867 0.3 1 162 47 47 LYS H H 7.455 0.02 1 163 47 47 LYS CA C 59.102 0.3 1 164 47 47 LYS CB C 32.704 0.3 1 165 47 47 LYS N N 123.535 0.3 1 166 48 48 ILE H H 8.158 0.02 1 167 48 48 ILE CA C 66.152 0.3 1 168 48 48 ILE CB C 38.226 0.3 1 169 48 48 ILE N N 121.836 0.3 1 170 49 49 LYS H H 8.275 0.02 1 171 49 49 LYS CA C 61.893 0.3 1 172 49 49 LYS CB C 32.704 0.3 1 173 49 49 LYS N N 118.797 0.3 1 174 50 50 THR H H 7.888 0.02 1 175 50 50 THR CA C 66.805 0.3 1 176 50 50 THR CB C 68.811 0.3 1 177 50 50 THR N N 114.29 0.3 1 178 51 51 ALA H H 8.231 0.02 1 179 51 51 ALA CA C 55.988 0.3 1 180 51 51 ALA CB C 18.333 0.3 1 181 51 51 ALA N N 125.087 0.3 1 182 52 52 LEU H H 8.801 0.02 1 183 52 52 LEU CA C 58.3 0.3 1 184 52 52 LEU CB C 41.706 0.3 1 185 52 52 LEU N N 118.003 0.3 1 186 53 53 ASP H H 8.744 0.02 1 187 53 53 ASP CA C 57.595 0.3 1 188 53 53 ASP CB C 39.577 0.3 1 189 53 53 ASP N N 123.19 0.3 1 190 54 54 HIS H H 8.244 0.02 1 191 54 54 HIS CA C 59.564 0.3 1 192 54 54 HIS CB C 30.778 0.3 1 193 54 54 HIS N N 122.507 0.3 1 194 55 55 ILE H H 8.293 0.02 1 195 55 55 ILE CA C 65.743 0.3 1 196 55 55 ILE CB C 38.655 0.3 1 197 55 55 ILE N N 119.662 0.3 1 198 56 56 LYS H H 7.379 0.02 1 199 56 56 LYS CA C 59.874 0.3 1 200 56 56 LYS CB C 31.639 0.3 1 201 56 56 LYS N N 118.668 0.3 1 202 57 57 SER H H 7.663 0.02 1 203 57 57 SER CA C 61.447 0.3 1 204 57 57 SER CB C 62.809 0.3 1 205 57 57 SER N N 112.445 0.3 1 206 58 58 GLU H H 7.783 0.02 1 207 58 58 GLU CA C 58.3 0.3 1 208 58 58 GLU CB C 29.606 0.3 1 209 58 58 GLU N N 119.143 0.3 1 210 59 59 LEU H H 8.162 0.02 1 211 59 59 LEU CA C 58.198 0.3 1 212 59 59 LEU CB C 41.673 0.3 1 213 59 59 LEU N N 121.626 0.3 1 214 60 60 ASP H H 8.467 0.02 1 215 60 60 ASP CA C 56.659 0.3 1 216 60 60 ASP CB C 40.061 0.3 1 217 60 60 ASP N N 120.031 0.3 1 218 61 61 LYS H H 7.082 0.02 1 219 61 61 LYS CA C 57.697 0.3 1 220 61 61 LYS CB C 33.188 0.3 1 221 61 61 LYS N N 117.101 0.3 1 222 62 62 CYS H H 7.433 0.02 1 223 62 62 CYS CA C 59.104 0.3 1 224 62 62 CYS CB C 27.186 0.3 1 225 62 62 CYS N N 118.761 0.3 1 226 63 63 ASN H H 8.028 0.02 1 227 63 63 ASN CA C 53.345 0.3 1 228 63 63 ASN CB C 40.351 0.3 1 229 63 63 ASN N N 120.264 0.3 1 230 64 64 GLY H H 8.579 0.02 1 231 64 64 GLY CA C 44.804 0.3 1 232 64 64 GLY N N 108.995 0.3 1 233 65 65 ASN H H 8.727 0.02 1 234 65 65 ASN CA C 55.26 0.3 1 235 65 65 ASN CB C 38.238 0.3 1 236 65 65 ASN N N 119.424 0.3 1 237 66 66 ASP H H 8.571 0.02 1 238 66 66 ASP CA C 53.503 0.3 1 239 66 66 ASP CB C 40.545 0.3 1 240 66 66 ASP N N 119.124 0.3 1 241 67 67 ALA H H 7.593 0.02 1 242 67 67 ALA CA C 55.889 0.3 1 243 67 67 ALA CB C 19.442 0.3 1 244 67 67 ALA N N 122.984 0.3 1 245 68 68 ASP H H 8.517 0.02 1 246 68 68 ASP CA C 57.764 0.3 1 247 68 68 ASP CB C 40.448 0.3 1 248 68 68 ASP N N 116.584 0.3 1 249 69 69 GLN H H 8.114 0.02 1 250 69 69 GLN CA C 58.801 0.3 1 251 69 69 GLN CB C 28.555 0.3 1 252 69 69 GLN N N 121.289 0.3 1 253 70 70 GLN H H 8.312 0.02 1 254 70 70 GLN CA C 59.104 0.3 1 255 70 70 GLN CB C 28.838 0.3 1 256 70 70 GLN N N 120.071 0.3 1 257 71 71 LYS H H 8.56 0.02 1 258 71 71 LYS CA C 60.642 0.3 1 259 71 71 LYS CB C 32.897 0.3 1 260 71 71 LYS N N 120.947 0.3 1 261 72 72 THR H H 8.184 0.02 1 262 72 72 THR CA C 66.738 0.3 1 263 72 72 THR CB C 68.663 0.3 1 264 72 72 THR N N 117.546 0.3 1 265 73 73 THR H H 8.536 0.02 1 266 73 73 THR CA C 66.367 0.3 1 267 73 73 THR CB C 68.617 0.3 1 268 73 73 THR N N 119.755 0.3 1 269 74 74 PHE H H 8.324 0.02 1 270 74 74 PHE CA C 61.146 0.3 1 271 74 74 PHE CB C 38.807 0.3 1 272 74 74 PHE N N 122.865 0.3 1 273 75 75 LYS H H 8.302 0.02 1 274 75 75 LYS CA C 60.609 0.3 1 275 75 75 LYS CB C 32.704 0.3 1 276 75 75 LYS N N 119.763 0.3 1 277 76 76 GLN H H 7.717 0.02 1 278 76 76 GLN CA C 58.534 0.3 1 279 76 76 GLN CB C 28.638 0.3 1 280 76 76 GLN N N 116.735 0.3 1 281 77 77 THR H H 8.257 0.02 1 282 77 77 THR CA C 65.427 0.3 1 283 77 77 THR CB C 69.049 0.3 1 284 77 77 THR N N 117.04 0.3 1 285 78 78 VAL H H 8.076 0.02 1 286 78 78 VAL CA C 66.635 0.3 1 287 78 78 VAL CB C 31.434 0.3 1 288 78 78 VAL N N 122.201 0.3 1 289 79 79 GLN H H 8.083 0.02 1 290 79 79 GLN CA C 59.539 0.3 1 291 79 79 GLN CB C 28.445 0.3 1 292 79 79 GLN N N 119.005 0.3 1 293 80 80 GLY H H 8.159 0.02 1 294 80 80 GLY CA C 46.837 0.3 1 295 80 80 GLY N N 106.053 0.3 1 296 81 81 ALA H H 8.105 0.02 1 297 81 81 ALA CA C 54.758 0.3 1 298 81 81 ALA CB C 19.442 0.3 1 299 81 81 ALA N N 124.407 0.3 1 300 82 82 LEU H H 8.003 0.02 1 301 82 82 LEU CA C 56.223 0.3 1 302 82 82 LEU CB C 41.711 0.3 1 303 82 82 LEU N N 116.769 0.3 1 304 83 83 SER H H 7.788 0.02 1 305 83 83 SER CA C 60.799 0.3 1 306 83 83 SER CB C 63.101 0.3 1 307 83 83 SER N N 115.942 0.3 1 308 84 84 GLY H H 8.048 0.02 1 309 84 84 GLY CA C 45.385 0.3 1 310 84 84 GLY N N 109.127 0.3 1 311 85 85 GLY H H 7.781 0.02 1 312 85 85 GLY CA C 44.784 0.3 1 313 85 85 GLY N N 108.83 0.3 1 314 86 86 ILE H H 7.596 0.02 1 315 86 86 ILE CA C 60.969 0.3 1 316 86 86 ILE CB C 39.577 0.3 1 317 86 86 ILE N N 118.208 0.3 1 318 87 87 ASP H H 8.176 0.02 1 319 87 87 ASP CA C 56.156 0.3 1 320 87 87 ASP CB C 40.545 0.3 1 321 87 87 ASP N N 122.965 0.3 1 322 88 88 GLY H H 8.211 0.02 1 323 88 88 GLY CA C 45.385 0.3 1 324 88 88 GLY N N 108.727 0.3 1 325 89 89 PHE H H 7.798 0.02 1 326 89 89 PHE CA C 58.549 0.3 1 327 89 89 PHE CB C 39.678 0.3 1 328 89 89 PHE N N 121.207 0.3 1 329 90 90 GLY H H 8.178 0.02 1 330 90 90 GLY CA C 44.873 0.3 1 331 90 90 GLY N N 111.693 0.3 1 332 91 91 SER H H 7.936 0.02 1 333 91 91 SER CA C 58.7 0.3 1 334 91 91 SER CB C 63.873 0.3 1 335 91 91 SER N N 115.07 0.3 1 336 92 92 ASN H H 8.449 0.02 1 337 92 92 ASN CA C 56.686 0.3 1 338 92 92 ASN CB C 38.575 0.3 1 339 92 92 ASN N N 120.082 0.3 1 340 94 94 ALA H H 8.209 0.02 1 341 94 94 ALA CA C 53.032 0.3 1 342 94 94 ALA CB C 19.442 0.3 1 343 94 94 ALA N N 124.076 0.3 1 344 95 95 VAL H H 8.123 0.02 1 345 95 95 VAL CA C 62.084 0.3 1 346 95 95 VAL CB C 33.091 0.3 1 347 95 95 VAL N N 119.325 0.3 1 348 96 96 THR H H 8.291 0.02 1 349 96 96 THR CA C 61.581 0.3 1 350 96 96 THR CB C 69.972 0.3 1 351 96 96 THR N N 117.275 0.3 1 352 97 97 THR H H 8.148 0.02 1 353 97 97 THR CA C 61.58 0.3 1 354 97 97 THR CB C 67.876 0.3 1 355 97 97 THR N N 115.725 0.3 1 356 98 98 CYS H H 8.372 0.02 1 357 98 98 CYS CA C 58.668 0.3 1 358 98 98 CYS CB C 28.257 0.3 1 359 98 98 CYS N N 121.07 0.3 1 360 99 99 GLY H H 8.418 0.02 1 361 99 99 GLY CA C 45.454 0.3 1 362 99 99 GLY N N 111.994 0.3 1 363 100 100 ASN H H 8.403 0.02 1 364 100 100 ASN CA C 53.636 0.3 1 365 100 100 ASN CB C 39.291 0.3 1 366 100 100 ASN N N 118.696 0.3 1 367 101 101 GLY H H 8.473 0.02 1 368 101 101 GLY CA C 45.481 0.3 1 369 101 101 GLY N N 109.972 0.3 1 370 102 102 SER H H 7.847 0.02 1 371 102 102 SER CA C 60.001 0.3 1 372 102 102 SER CB C 65.037 0.3 1 373 102 102 SER N N 121.381 0.3 1 stop_ save_