data_50195 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Skp_A108L_monomer ; _BMRB_accession_number 50195 _BMRB_flat_file_name bmr50195.str _Entry_type original _Submission_date 2020-02-12 _Accession_date 2020-02-12 _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 Mas Guillaume . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 104 "13C chemical shifts" 203 "15N chemical shifts" 104 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-17 original BMRB . stop_ _Original_release_date 2020-02-12 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Regulation of chaperone function by coupled folding and oligomerization ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 33087350 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mas Guillaume . . 2 Burmann Bjorn M. . 3 Sharpe Timothy . . 4 Claudi Beatrice . . 5 Bumann Dirk . . 6 Hiller Sebastian . . stop_ _Journal_abbreviation 'Sci. Adv.' _Journal_name_full 'Science advances' _Journal_volume 6 _Journal_issue 43 _Journal_ISSN 2375-2548 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first eabc5822 _Page_last eabc5822 _Year 2020 _Details . loop_ _Keyword 'Gram-negative bacteria' 'NMR spectroscopy' 'bacterial periplasm' 'disordered proteins' 'molecular chaperones' 'protein dynamics' 'protein folding' 'protein structure' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name Skp_A108L _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Skp_A108L $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 Skp _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function Chaperone stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVLNSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -20 MET 2 -19 GLY 3 -18 SER 4 -17 SER 5 -16 HIS 6 -15 HIS 7 -14 HIS 8 -13 HIS 9 -12 HIS 10 -11 HIS 11 -10 SER 12 -9 SER 13 -8 GLY 14 -7 LEU 15 -6 VAL 16 -5 PRO 17 -4 ARG 18 -3 GLY 19 -2 SER 20 -1 HIS 21 0 MET 22 1 ALA 23 2 ASP 24 3 LYS 25 4 ILE 26 5 ALA 27 6 ILE 28 7 VAL 29 8 ASN 30 9 MET 31 10 GLY 32 11 SER 33 12 LEU 34 13 PHE 35 14 GLN 36 15 GLN 37 16 VAL 38 17 ALA 39 18 GLN 40 19 LYS 41 20 THR 42 21 GLY 43 22 VAL 44 23 SER 45 24 ASN 46 25 THR 47 26 LEU 48 27 GLU 49 28 ASN 50 29 GLU 51 30 PHE 52 31 LYS 53 32 GLY 54 33 ARG 55 34 ALA 56 35 SER 57 36 GLU 58 37 LEU 59 38 GLN 60 39 ARG 61 40 MET 62 41 GLU 63 42 THR 64 43 ASP 65 44 LEU 66 45 GLN 67 46 ALA 68 47 LYS 69 48 MET 70 49 LYS 71 50 LYS 72 51 LEU 73 52 GLN 74 53 SER 75 54 MET 76 55 LYS 77 56 ALA 78 57 GLY 79 58 SER 80 59 ASP 81 60 ARG 82 61 THR 83 62 LYS 84 63 LEU 85 64 GLU 86 65 LYS 87 66 ASP 88 67 VAL 89 68 MET 90 69 ALA 91 70 GLN 92 71 ARG 93 72 GLN 94 73 THR 95 74 PHE 96 75 ALA 97 76 GLN 98 77 LYS 99 78 ALA 100 79 GLN 101 80 ALA 102 81 PHE 103 82 GLU 104 83 GLN 105 84 ASP 106 85 ARG 107 86 ALA 108 87 ARG 109 88 ARG 110 89 SER 111 90 ASN 112 91 GLU 113 92 GLU 114 93 ARG 115 94 GLY 116 95 LYS 117 96 LEU 118 97 VAL 119 98 THR 120 99 ARG 121 100 ILE 122 101 GLN 123 102 THR 124 103 ALA 125 104 VAL 126 105 LYS 127 106 SER 128 107 VAL 129 108 LEU 130 109 ASN 131 110 SER 132 111 GLN 133 112 ASP 134 113 ILE 135 114 ASP 136 115 LEU 137 116 VAL 138 117 VAL 139 118 ASP 140 119 ALA 141 120 ASN 142 121 ALA 143 122 VAL 144 123 ALA 145 124 TYR 146 125 ASN 147 126 SER 148 127 SER 149 128 ASP 150 129 VAL 151 130 LYS 152 131 ASP 153 132 ILE 154 133 THR 155 134 ALA 156 135 ASP 157 136 VAL 158 137 LEU 159 138 LYS 160 139 GLN 161 140 VAL 162 141 LYS 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 'E. coli' 562 Bacteria . Escherichia coli 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' . . . . plasmid 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 $entity_1 1 mM '[U-99% 13C; U-99% 15N]' MES 25 mM 'natural abundance' NaCl 150 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _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' 0.150 . M pH 6.5 . pH pressure 1 . atm temperature 310 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' 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 Skp_A108L _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 22 ALA H H 8.22 0.02 1 2 1 22 ALA CA C 49.79 0.3 1 3 1 22 ALA CB C 15.99 0.3 1 4 1 22 ALA N N 127.20 0.3 1 5 2 23 ASP H H 8.14257 0.02 1 6 2 23 ASP CA C 51.7 0.3 1 7 2 23 ASP CB C 38.05 0.3 1 8 2 23 ASP N N 119.36625 0.3 1 9 4 25 ILE H H 7.97063 0.02 1 10 4 25 ILE CA C 58.234 0.3 1 11 4 25 ILE CB C 35.333 0.3 1 12 4 25 ILE N N 122.13113 0.3 1 13 5 26 ALA H H 8.15483 0.02 1 14 5 26 ALA CA C 49.71 0.3 1 15 5 26 ALA CB C 16.05 0.3 1 16 5 26 ALA N N 127.64625 0.3 1 17 6 27 ILE H H 7.95167 0.02 1 18 6 27 ILE CA C 58.49 0.3 1 19 6 27 ILE CB C 35.15 0.3 1 20 6 27 ILE N N 120.60755 0.3 1 21 7 28 VAL H H 8.00271 0.02 1 22 7 28 VAL CA C 59.76 0.3 1 23 7 28 VAL CB C 29.35 0.3 1 24 7 28 VAL N N 123.50819 0.3 1 25 10 31 GLY H H 8.341 0.02 1 26 10 31 GLY CA C 44.8 0.3 1 27 10 31 GLY N N 109.487 0.3 1 28 11 32 SER H H 8.27501 0.02 1 29 11 32 SER CA C 57.063 0.3 1 30 11 32 SER CB C 60.845 0.3 1 31 11 32 SER N N 117.88355 0.3 1 32 12 33 LEU H H 8.24128 0.02 1 33 12 33 LEU CA C 52.576 0.3 1 34 12 33 LEU CB C 38.149 0.3 1 35 12 33 LEU N N 122.75637 0.3 1 36 13 34 PHE H H 7.93559 0.02 1 37 13 34 PHE CA C 56.846 0.3 1 38 13 34 PHE CB C 38.243 0.3 1 39 13 34 PHE N N 122.72431 0.3 1 40 14 35 GLN H H 7.97155 0.02 1 41 14 35 GLN CA C 56.846 0.3 1 42 14 35 GLN CB C 29.306 0.3 1 43 14 35 GLN N N 122.62303 0.3 1 44 15 36 GLN H H 8.18992 0.02 1 45 15 36 GLN CA C 53.329 0.3 1 46 15 36 GLN CB C 27.695 0.3 1 47 15 36 GLN N N 123.8724 0.3 1 48 20 41 THR H H 8.08688 0.02 1 49 20 41 THR CA C 59.23 0.3 1 50 20 41 THR CB C 67.07 0.3 1 51 20 41 THR N N 115.11703 0.3 1 52 21 42 GLY H H 8.30537 0.02 1 53 21 42 GLY CA C 44.6 0.3 1 54 21 42 GLY N N 110.91139 0.3 1 55 22 43 VAL H H 7.928 0.02 1 56 22 43 VAL CA C 59.85 0.3 1 57 22 43 VAL CB C 29.01 0.3 1 58 22 43 VAL N N 119.434 0.3 1 59 25 46 THR H H 8.0929 0.02 1 60 25 46 THR CA C 59.616 0.3 1 61 25 46 THR CB C 66.879 0.3 1 62 25 46 THR N N 114.84014 0.3 1 63 26 47 LEU H H 8.18338 0.02 1 64 26 47 LEU CA C 53.703 0.3 1 65 26 47 LEU CB C 38.69 0.3 1 66 26 47 LEU N N 124.26808 0.3 1 67 27 48 GLU H H 7.8661 0.02 1 68 27 48 GLU CA C 58.512 0.3 1 69 27 48 GLU CB C 29.094 0.3 1 70 27 48 GLU N N 119.9036 0.3 1 71 28 49 ASN H H 8.0745 0.02 1 72 28 49 ASN CA C 53.285 0.3 1 73 28 49 ASN CB C 35.28 0.3 1 74 28 49 ASN N N 121.93485 0.3 1 75 29 50 GLU H H 7.97072 0.02 1 76 29 50 GLU CA C 56.283 0.3 1 77 29 50 GLU CB C 29.22 0.3 1 78 29 50 GLU N N 122.45874 0.3 1 79 31 52 LYS H H 8.46908 0.02 1 80 31 52 LYS CA C 55.06 0.3 1 81 31 52 LYS CB C 28.74 0.3 1 82 31 52 LYS N N 121.35137 0.3 1 83 32 53 GLY H H 7.98043 0.02 1 84 32 53 GLY CA C 44.89 0.3 1 85 32 53 GLY N N 109.29505 0.3 1 86 33 54 ARG H H 8.08626 0.02 1 87 33 54 ARG CA C 54.11 0.3 1 88 33 54 ARG CB C 26.05 0.3 1 89 33 54 ARG N N 121.5667 0.3 1 90 34 55 ALA H H 8.3585 0.02 1 91 34 55 ALA CA C 50.95 0.3 1 92 34 55 ALA CB C 15.53 0.3 1 93 34 55 ALA N N 124.6623 0.3 1 94 35 56 SER H H 8.19665 0.02 1 95 35 56 SER CA C 56.67 0.3 1 96 35 56 SER CB C 60.39 0.3 1 97 35 56 SER N N 115.13726 0.3 1 98 36 57 GLU H H 8.21552 0.02 1 99 36 57 GLU CA C 54.9 0.3 1 100 36 57 GLU CB C 26.83 0.3 1 101 36 57 GLU N N 115.51158 0.3 1 102 37 58 LEU H H 8.21136 0.02 1 103 37 58 LEU CA C 51.31 0.3 1 104 37 58 LEU CB C 38.15 0.3 1 105 37 58 LEU N N 118.95005 0.3 1 106 38 59 GLN H H 8.29589 0.02 1 107 38 59 GLN CA C 54.77 0.3 1 108 38 59 GLN CB C 26.71 0.3 1 109 38 59 GLN N N 121.54213 0.3 1 110 39 60 ARG H H 8.18226 0.02 1 111 39 60 ARG CA C 55.64 0.3 1 112 39 60 ARG CB C 27.715 0.3 1 113 39 60 ARG N N 120.515 0.3 1 114 40 61 MET H H 8.07091 0.02 1 115 40 61 MET CA C 54.72 0.3 1 116 40 61 MET CB C 29.31 0.3 1 117 40 61 MET N N 122.90086 0.3 1 118 41 62 GLU H H 8.246 0.02 1 119 41 62 GLU CA C 54.55 0.3 1 120 41 62 GLU CB C 25.78 0.3 1 121 41 62 GLU N N 119.473 0.3 1 122 42 63 THR H H 8.07213 0.02 1 123 42 63 THR CA C 60.849 0.3 1 124 42 63 THR CB C 67.092 0.3 1 125 42 63 THR N N 116.15118 0.3 1 126 45 66 GLN H H 8.18287 0.02 1 127 45 66 GLN CA C 54.59 0.3 1 128 45 66 GLN CB C 26.69 0.3 1 129 45 66 GLN N N 121.50278 0.3 1 130 46 67 ALA H H 8.04478 0.02 1 131 46 67 ALA CA C 50.47 0.3 1 132 46 67 ALA CB C 15.53 0.3 1 133 46 67 ALA N N 123.33627 0.3 1 134 47 68 LYS H H 7.939 0.02 1 135 47 68 LYS CA C 54.28 0.3 1 136 47 68 LYS CB C 29.578 0.3 1 137 47 68 LYS N N 119.579 0.3 1 138 48 69 MET H H 8.27972 0.02 1 139 48 69 MET CA C 53.28 0.3 1 140 48 69 MET CB C 29.52 0.3 1 141 48 69 MET N N 122.91837 0.3 1 142 49 70 LYS H H 7.841 0.02 1 143 49 70 LYS CA C 55.11 0.3 1 144 49 70 LYS CB C 29.05 0.3 1 145 49 70 LYS N N 121.36 0.3 1 146 51 72 LEU H H 8.22709 0.02 1 147 51 72 LEU CA C 51.698 0.3 1 148 51 72 LEU CB C 38.103 0.3 1 149 51 72 LEU N N 123.11536 0.3 1 150 52 73 GLN H H 8.044 0.02 1 151 52 73 GLN CA C 53.341 0.3 1 152 52 73 GLN CB C 26.125 0.3 1 153 52 73 GLN N N 121.103 0.3 1 154 53 74 SER H H 8.20817 0.02 1 155 53 74 SER CA C 55.36 0.3 1 156 53 74 SER CB C 60.95 0.3 1 157 53 74 SER N N 117.37899 0.3 1 158 54 75 MET H H 8.19812 0.02 1 159 54 75 MET CA C 54.03 0.3 1 160 54 75 MET CB C 29.46 0.3 1 161 54 75 MET N N 123.13081 0.3 1 162 56 77 ALA H H 8.23037 0.02 1 163 56 77 ALA CA C 49.87 0.3 1 164 56 77 ALA CB C 16.13 0.3 1 165 56 77 ALA N N 124.98972 0.3 1 166 57 78 GLY H H 8.31726 0.02 1 167 57 78 GLY CA C 45.34 0.3 1 168 57 78 GLY N N 109.10001 0.3 1 169 58 79 SER H H 8.122 0.02 1 170 58 79 SER CA C 60 0.3 1 171 58 79 SER CB C 63.8 0.3 1 172 58 79 SER N N 116.168 0.3 1 173 60 81 ARG H H 8.3701 0.02 1 174 60 81 ARG CA C 55.05 0.3 1 175 60 81 ARG CB C 26.61 0.3 1 176 60 81 ARG N N 121.86405 0.3 1 177 61 82 THR H H 8.1262 0.02 1 178 61 82 THR CA C 61.43 0.3 1 179 61 82 THR CB C 66.78 0.3 1 180 61 82 THR N N 115.38113 0.3 1 181 63 84 LEU H H 8.08661 0.02 1 182 63 84 LEU CA C 53.08 0.3 1 183 63 84 LEU CB C 38.66 0.3 1 184 63 84 LEU N N 123.81308 0.3 1 185 64 85 GLU H H 8.234 0.02 1 186 64 85 GLU CA C 54.5 0.3 1 187 64 85 GLU CB C 26.9 0.3 1 188 64 85 GLU N N 121.095 0.3 1 189 65 86 LYS H H 8.039 0.02 1 190 65 86 LYS CA C 54.96 0.3 1 191 65 86 LYS CB C 29.29 0.3 1 192 65 86 LYS N N 120.596 0.3 1 193 66 87 ASP H H 8.15035 0.02 1 194 66 87 ASP CA C 53.22 0.3 1 195 66 87 ASP CB C 38.01 0.3 1 196 66 87 ASP N N 121.8421 0.3 1 197 69 90 ALA H H 7.9505 0.02 1 198 69 90 ALA CA C 51.64 0.3 1 199 69 90 ALA CB C 14.98 0.3 1 200 69 90 ALA N N 122.99347 0.3 1 201 70 91 GLN H H 8.02702 0.02 1 202 70 91 GLN CA C 55.949 0.3 1 203 70 91 GLN CB C 29.224 0.3 1 204 70 91 GLN N N 119.8674 0.3 1 205 71 92 ARG H H 8.21435 0.02 1 206 71 92 ARG CA C 54.649 0.3 1 207 71 92 ARG CB C 25.984 0.3 1 208 71 92 ARG N N 120.74301 0.3 1 209 72 93 GLN H H 8.36633 0.02 1 210 72 93 GLN CA C 55.417 0.3 1 211 72 93 GLN CB C 26.84 0.3 1 212 72 93 GLN N N 122.266 0.3 1 213 73 94 THR H H 8.084 0.02 1 214 73 94 THR CA C 62.03 0.3 1 215 73 94 THR CB C 66.87 0.3 1 216 73 94 THR N N 116.238 0.3 1 217 75 96 ALA H H 8.19534 0.02 1 218 75 96 ALA CA C 51.875 0.3 1 219 75 96 ALA CB C 16.035 0.3 1 220 75 96 ALA N N 124.79329 0.3 1 221 76 97 GLN H H 8.422 0.02 1 222 76 97 GLN CA C 55.172 0.3 1 223 76 97 GLN CB C 26.73 0.3 1 224 76 97 GLN N N 124.829 0.3 1 225 77 98 LYS H H 8.24785 0.02 1 226 77 98 LYS CA C 55.246 0.3 1 227 77 98 LYS CB C 29.573 0.3 1 228 77 98 LYS N N 122.95313 0.3 1 229 78 99 ALA H H 8.16043 0.02 1 230 78 99 ALA CA C 51.014 0.3 1 231 78 99 ALA CB C 15.588 0.3 1 232 78 99 ALA N N 123.74546 0.3 1 233 79 100 GLN H H 8.2296 0.02 1 234 79 100 GLN CA C 54.555 0.3 1 235 79 100 GLN CB C 25.72 0.3 1 236 79 100 GLN N N 119.4662 0.3 1 237 80 101 ALA H H 7.9546 0.02 1 238 80 101 ALA CA C 51.018 0.3 1 239 80 101 ALA CB C 15.366 0.3 1 240 80 101 ALA N N 123.62031 0.3 1 241 81 102 PHE H H 8.25606 0.02 1 242 81 102 PHE CA C 58.543 0.3 1 243 81 102 PHE CB C 38.09 0.3 1 244 81 102 PHE N N 123.57885 0.3 1 245 82 103 GLU H H 8.248 0.02 1 246 82 103 GLU CA C 54.52 0.3 1 247 82 103 GLU CB C 26.87 0.3 1 248 82 103 GLU N N 121.373 0.3 1 249 83 104 GLN H H 8.25788 0.02 1 250 83 104 GLN CA C 54.43 0.3 1 251 83 104 GLN CB C 26.75 0.3 1 252 83 104 GLN N N 121.66604 0.3 1 253 84 105 ASP H H 8.01897 0.02 1 254 84 105 ASP CA C 54.048 0.3 1 255 84 105 ASP CB C 38.119 0.3 1 256 84 105 ASP N N 119.27302 0.3 1 257 85 106 ARG H H 8.10736 0.02 1 258 85 106 ARG CA C 55.221 0.3 1 259 85 106 ARG CB C 27.611 0.3 1 260 85 106 ARG N N 122.5244 0.3 1 261 86 107 ALA H H 8.408 0.02 1 262 86 107 ALA CA C 50.71 0.3 1 263 86 107 ALA CB C 15.42 0.3 1 264 86 107 ALA N N 124.819 0.3 1 265 87 108 ARG H H 8.08766 0.02 1 266 87 108 ARG CA C 54.02 0.3 1 267 87 108 ARG CB C 25.85 0.3 1 268 87 108 ARG N N 119.45908 0.3 1 269 89 110 SER H H 8.08976 0.02 1 270 89 110 SER CA C 59.935 0.3 1 271 89 110 SER CB C 63.396 0.3 1 272 89 110 SER N N 117.30577 0.3 1 273 90 111 ASN H H 8.13927 0.02 1 274 90 111 ASN CA C 54.836 0.3 1 275 90 111 ASN CB C 38.303 0.3 1 276 90 111 ASN N N 122.25899 0.3 1 277 91 112 GLU H H 8.055 0.02 1 278 91 112 GLU CA C 54.669 0.3 1 279 91 112 GLU CB C 25.686 0.3 1 280 91 112 GLU N N 120.164 0.3 1 281 93 114 ARG H H 8.19581 0.02 1 282 93 114 ARG CA C 54.43 0.3 1 283 93 114 ARG CB C 26.79 0.3 1 284 93 114 ARG N N 121.73933 0.3 1 285 94 115 GLY H H 8.29124 0.02 1 286 94 115 GLY CA C 44.71 0.3 1 287 94 115 GLY N N 109.31521 0.3 1 288 95 116 LYS H H 7.918 0.02 1 289 95 116 LYS CA C 53.5 0.3 1 290 95 116 LYS CB C 29.2 0.3 1 291 95 116 LYS N N 120.925 0.3 1 292 96 117 LEU H H 8.08016 0.02 1 293 96 117 LEU CA C 52.77 0.3 1 294 96 117 LEU CB C 38.9 0.3 1 295 96 117 LEU N N 123.2657 0.3 1 296 103 124 ALA H H 8.20413 0.02 1 297 103 124 ALA CA C 50.676 0.3 1 298 103 124 ALA CB C 16.131 0.3 1 299 103 124 ALA N N 126.72174 0.3 1 300 104 125 VAL H H 8.009 0.02 1 301 104 125 VAL CA C 59.672 0.3 1 302 104 125 VAL CB C 29.32 0.3 1 303 104 125 VAL N N 119.867 0.3 1 304 107 128 VAL H H 7.916 0.02 1 305 107 128 VAL CA C 58.931 0.3 1 306 107 128 VAL CB C 28.586 0.3 1 307 107 128 VAL N N 121.353 0.3 1 308 110 131 SER H H 8.1848 0.02 1 309 110 131 SER CA C 56.36 0.3 1 310 110 131 SER CB C 60.78 0.3 1 311 110 131 SER N N 116.5963 0.3 1 312 111 132 GLN H H 8.34123 0.02 1 313 111 132 GLN CA C 53.35 0.3 1 314 111 132 GLN CB C 26.35 0.3 1 315 111 132 GLN N N 121.82105 0.3 1 316 112 133 ASP H H 8.20532 0.02 1 317 112 133 ASP CA C 51.64 0.3 1 318 112 133 ASP CB C 38.05 0.3 1 319 112 133 ASP N N 121.58393 0.3 1 320 113 134 ILE H H 7.85243 0.02 1 321 113 134 ILE CA C 58.49 0.3 1 322 113 134 ILE CB C 35.77 0.3 1 323 113 134 ILE N N 120.23634 0.3 1 324 114 135 ASP H H 8.24713 0.02 1 325 114 135 ASP CA C 51.6 0.3 1 326 114 135 ASP CB C 38.09 0.3 1 327 114 135 ASP N N 123.74264 0.3 1 328 115 136 LEU H H 8.15865 0.02 1 329 115 136 LEU CA C 52.541 0.3 1 330 115 136 LEU CB C 39.029 0.3 1 331 115 136 LEU N N 124.93098 0.3 1 332 116 137 VAL H H 7.89851 0.02 1 333 116 137 VAL CA C 59.76 0.3 1 334 116 137 VAL CB C 29.19 0.3 1 335 116 137 VAL N N 120.53803 0.3 1 336 117 138 VAL H H 8.08224 0.02 1 337 117 138 VAL CA C 59.64 0.3 1 338 117 138 VAL CB C 29.32 0.3 1 339 117 138 VAL N N 124.11174 0.3 1 340 118 139 ASP H H 8.23339 0.02 1 341 118 139 ASP CA C 51.37 0.3 1 342 118 139 ASP CB C 38.31 0.3 1 343 118 139 ASP N N 124.42332 0.3 1 344 119 140 ALA H H 8.29441 0.02 1 345 119 140 ALA CA C 50.48 0.3 1 346 119 140 ALA CB C 15.91 0.3 1 347 119 140 ALA N N 125.89441 0.3 1 348 120 141 ASN H H 8.34447 0.02 1 349 120 141 ASN CA C 50.63 0.3 1 350 120 141 ASN CB C 36.01 0.3 1 351 120 141 ASN N N 116.72016 0.3 1 352 121 142 ALA H H 7.864 0.02 1 353 121 142 ALA CA C 49.96 0.3 1 354 121 142 ALA CB C 16.04 0.3 1 355 121 142 ALA N N 124.012 0.3 1 356 122 143 VAL H H 7.817 0.02 1 357 122 143 VAL CA C 59.68 0.3 1 358 122 143 VAL CB C 29.22 0.3 1 359 122 143 VAL N N 118.768 0.3 1 360 123 144 ALA H H 8.07137 0.02 1 361 123 144 ALA CA C 49.58 0.3 1 362 123 144 ALA CB C 15.99 0.3 1 363 123 144 ALA N N 126.90284 0.3 1 364 124 145 TYR H H 7.992 0.02 1 365 124 145 TYR CA C 55.01 0.3 1 366 124 145 TYR CB C 35.82 0.3 1 367 124 145 TYR N N 119.935 0.3 1 368 130 151 LYS H H 8.48871 0.02 1 369 130 151 LYS CA C 53.8 0.3 1 370 130 151 LYS CB C 29.95 0.3 1 371 130 151 LYS N N 124.73571 0.3 1 372 131 152 ASP H H 7.933 0.02 1 373 131 152 ASP CA C 53.567 0.3 1 374 131 152 ASP CB C 38.303 0.3 1 375 131 152 ASP N N 121.495 0.3 1 376 132 153 ILE H H 8.06 0.02 1 377 132 153 ILE CA C 59.72 0.3 1 378 132 153 ILE CB C 35.225 0.3 1 379 132 153 ILE N N 121.366 0.3 1 380 133 154 THR H H 8.106 0.02 1 381 133 154 THR CA C 59.515 0.3 1 382 133 154 THR CB C 66.879 0.3 1 383 133 154 THR N N 117.431 0.3 1 384 134 155 ALA H H 8.07982 0.02 1 385 134 155 ALA CA C 49.943 0.3 1 386 134 155 ALA CB C 16.083 0.3 1 387 134 155 ALA N N 125.87811 0.3 1 388 135 156 ASP H H 8.239 0.02 1 389 135 156 ASP CA C 53.28 0.3 1 390 135 156 ASP CB C 38.21 0.3 1 391 135 156 ASP N N 123.528 0.3 1 392 136 157 VAL H H 8.05 0.02 1 393 136 157 VAL CA C 59.74 0.3 1 394 136 157 VAL CB C 29.43 0.3 1 395 136 157 VAL N N 121.496 0.3 1 396 137 158 LEU H H 8.04967 0.02 1 397 137 158 LEU CA C 52.79 0.3 1 398 137 158 LEU CB C 38.6 0.3 1 399 137 158 LEU N N 123.82035 0.3 1 400 138 159 LYS H H 7.95035 0.02 1 401 138 159 LYS CA C 53.33 0.3 1 402 138 159 LYS CB C 29.36 0.3 1 403 138 159 LYS N N 121.57076 0.3 1 404 140 161 VAL H H 8.0639 0.02 1 405 140 161 VAL CA C 59.78 0.3 1 406 140 161 VAL CB C 29.29 0.3 1 407 140 161 VAL N N 122.26909 0.3 1 408 141 162 LYS H H 7.84445 0.02 1 409 141 162 LYS CA C 54.91 0.3 1 410 141 162 LYS CB C 30.49 0.3 1 411 141 162 LYS N N 130.40038 0.3 1 stop_ save_