data_50211 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solid state NMR assignments of a human l-III immunoglobulin light chain amyloid fibrils ; _BMRB_accession_number 50211 _BMRB_flat_file_name bmr50211.str _Entry_type original _Submission_date 2020-03-17 _Accession_date 2020-03-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'S3706 VL monomer' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pradhan Tejaswini . . 2 Annamalai Karthikeyan . . 3 Sarkar Riddhiman . . 4 Hegenbart Ute . . 5 Schonland Stefan . . 6 Fandrich Marcus . . 7 Reif Bernd . . 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" 177 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-09-18 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 50192 'S3706 VL fibrils' stop_ _Original_release_date 2020-03-20 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solid state NMR assignments of a human l-III immunoglobulin light chain amyloid fibrils ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32946005 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pradhan Tejaswini . . 2 Annamalai Karthikeyan . . 3 Sarkar Riddhiman . . 4 Hegenbart Ute . . 5 Schonland Stefan . . 6 Fandrich Marcus . . 7 Reif Bernd . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _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 2020 _Details . loop_ _Keyword 'AL amyloidosis, variable light chain fibrils, solid state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name S3706_VL_monomer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Immunoglobulin light chain' $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 disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; GSSELTQDPAVSVALGQTVR ITCQGDSLRSYSASWYQQKP GQAPVLVIFRKSNRPSGIPD RFSGSSSGNTASLTITGAQA EDEADYYCNSRDSSANHQVF GGGTKLTVLG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 GLY 2 1 SER 3 2 SER 4 3 GLU 5 4 LEU 6 5 THR 7 6 GLN 8 7 ASP 9 8 PRO 10 9 ALA 11 10 VAL 12 11 SER 13 12 VAL 14 13 ALA 15 14 LEU 16 15 GLY 17 16 GLN 18 17 THR 19 18 VAL 20 19 ARG 21 20 ILE 22 21 THR 23 22 CYS 24 23 GLN 25 24 GLY 26 25 ASP 27 26 SER 28 27 LEU 29 28 ARG 30 29 SER 31 30 TYR 32 31 SER 33 32 ALA 34 33 SER 35 34 TRP 36 35 TYR 37 36 GLN 38 37 GLN 39 38 LYS 40 39 PRO 41 40 GLY 42 41 GLN 43 42 ALA 44 43 PRO 45 44 VAL 46 45 LEU 47 46 VAL 48 47 ILE 49 48 PHE 50 49 ARG 51 50 LYS 52 51 SER 53 52 ASN 54 53 ARG 55 54 PRO 56 55 SER 57 56 GLY 58 57 ILE 59 58 PRO 60 59 ASP 61 60 ARG 62 61 PHE 63 62 SER 64 63 GLY 65 64 SER 66 65 SER 67 66 SER 68 67 GLY 69 68 ASN 70 69 THR 71 70 ALA 72 71 SER 73 72 LEU 74 73 THR 75 74 ILE 76 75 THR 77 76 GLY 78 77 ALA 79 78 GLN 80 79 ALA 81 80 GLU 82 81 ASP 83 82 GLU 84 83 ALA 85 84 ASP 86 85 TYR 87 86 TYR 88 87 CYS 89 88 ASN 90 89 SER 91 90 ARG 92 91 ASP 93 92 SER 94 93 SER 95 94 ALA 96 95 ASN 97 96 HIS 98 97 GLN 99 98 VAL 100 99 PHE 101 100 GLY 102 101 GLY 103 102 GLY 104 103 THR 105 104 LYS 106 105 LEU 107 106 THR 108 107 VAL 109 108 LEU 110 109 GLY 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 _Details $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens 'Human patient associated with AL amyloidosis' 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 BL21(DE3) plasmid 'pET 28(b+)' 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-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version V2 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 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '50 mM' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 1 . mM pH 6.5 . 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 TMS C 13 'methyl protons' ppm 0 external indirect . . . 0.2514502001 TMS H 1 'methyl protons' ppm 0 external direct . . . 1 TMS N 15 'methyl protons' ppm 0 external indirect . . . 0.101329120 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 '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCA' 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 'Immunoglobulin light chain' _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 2 3 SER H H 8.117 0.012 1 2 2 3 SER CA C 55.959 0.527 1 3 2 3 SER CB C 61.432 0.000 1 4 2 3 SER N N 117.548 0.134 1 5 3 4 GLU H H 8.277 0.015 1 6 3 4 GLU CA C 54.372 0.000 1 7 3 4 GLU CB C 28.332 0.067 1 8 3 4 GLU N N 121.562 0.167 1 9 4 5 LEU H H 8.215 0.017 1 10 4 5 LEU CA C 50.924 0.092 1 11 4 5 LEU CB C 41.328 0.000 1 12 4 5 LEU N N 122.603 0.047 1 13 5 6 THR H H 9.131 0.001 1 14 5 6 THR CA C 58.916 0.022 1 15 5 6 THR CB C 68.215 0.000 1 16 5 6 THR N N 117.107 0.005 1 17 6 7 GLN H H 8.710 0.001 1 18 6 7 GLN CA C 51.414 0.000 1 19 6 7 GLN CB C 31.269 0.087 1 20 6 7 GLN N N 122.085 0.006 1 21 7 8 ASP H H 8.846 0.019 1 22 7 8 ASP CA C 50.520 0.000 1 23 7 8 ASP CB C 37.901 0.000 1 24 7 8 ASP N N 124.328 0.125 1 25 9 10 ALA H H 7.665 0.017 1 26 9 10 ALA CA C 49.754 0.000 1 27 9 10 ALA CB C 18.465 0.091 1 28 9 10 ALA N N 119.186 0.152 1 29 10 11 VAL H H 8.538 0.021 1 30 10 11 VAL CA C 58.238 0.000 1 31 10 11 VAL CB C 33.149 0.008 1 32 10 11 VAL N N 120.533 0.170 1 33 11 12 SER H H 8.293 0.019 1 34 11 12 SER CA C 53.407 0.070 1 35 11 12 SER CB C 63.431 0.071 1 36 11 12 SER N N 119.567 0.180 1 37 12 13 VAL H H 8.576 0.001 1 38 12 13 VAL CA C 56.287 0.002 1 39 12 13 VAL CB C 32.925 0.097 1 40 12 13 VAL N N 120.233 0.004 1 41 13 14 ALA H H 8.270 0.003 1 42 13 14 ALA CA C 48.545 0.063 1 43 13 14 ALA CB C 16.519 0.000 1 44 13 14 ALA N N 128.290 0.262 1 45 14 15 LEU H H 7.918 0.019 1 46 14 15 LEU CA C 54.085 0.039 1 47 14 15 LEU CB C 40.002 0.000 1 48 14 15 LEU N N 121.258 0.250 1 49 15 16 GLY H H 9.708 0.003 1 50 15 16 GLY CA C 42.319 0.007 1 51 15 16 GLY N N 113.991 0.006 1 52 16 17 GLN H H 8.156 0.026 1 53 16 17 GLN CA C 51.958 0.118 1 54 16 17 GLN CB C 25.951 0.079 1 55 16 17 GLN N N 120.787 0.130 1 56 17 18 THR H H 8.310 0.003 1 57 17 18 THR CA C 59.235 0.003 1 58 17 18 THR CB C 67.731 0.000 1 59 17 18 THR N N 117.459 0.122 1 60 18 19 VAL H H 8.694 0.001 1 61 18 19 VAL CA C 56.116 0.001 1 62 18 19 VAL CB C 32.432 0.000 1 63 18 19 VAL N N 126.863 0.016 1 64 19 20 ARG H H 7.996 0.002 1 65 19 20 ARG CA C 51.564 0.000 1 66 19 20 ARG CB C 30.124 0.097 1 67 19 20 ARG N N 126.600 0.053 1 68 20 21 ILE H H 9.178 0.001 1 69 20 21 ILE CA C 57.957 0.000 1 70 20 21 ILE CB C 37.440 0.097 1 71 20 21 ILE N N 127.219 0.006 1 72 21 22 THR H H 8.435 0.000 1 73 21 22 THR CA C 59.221 0.000 1 74 21 22 THR CB C 68.908 0.085 1 75 21 22 THR N N 118.709 0.006 1 76 22 23 CYS H H 9.257 0.002 1 77 22 23 CYS CA C 51.101 0.011 1 78 22 23 CYS CB C 44.012 0.000 1 79 22 23 CYS N N 123.420 0.005 1 80 23 24 GLN H H 8.860 0.001 1 81 23 24 GLN CA C 51.417 0.084 1 82 23 24 GLN CB C 30.556 0.017 1 83 23 24 GLN N N 123.172 0.007 1 84 24 25 GLY H H 8.487 0.005 1 85 24 25 GLY CA C 43.578 0.007 1 86 24 25 GLY N N 110.712 0.128 1 87 25 26 ASP H H 9.053 0.001 1 88 25 26 ASP CA C 55.346 0.081 1 89 25 26 ASP CB C 37.968 0.085 1 90 25 26 ASP N N 123.343 0.015 1 91 26 27 SER H H 9.045 0.001 1 92 26 27 SER CA C 58.705 0.082 1 93 26 27 SER CB C 59.801 0.082 1 94 26 27 SER N N 115.754 0.007 1 95 27 28 LEU H H 7.338 0.002 1 96 27 28 LEU CA C 53.016 0.000 1 97 27 28 LEU CB C 37.328 0.000 1 98 27 28 LEU N N 119.387 0.013 1 99 28 29 ARG H H 7.435 0.001 1 100 28 29 ARG CA C 55.469 0.087 1 101 28 29 ARG CB C 27.520 0.000 1 102 28 29 ARG N N 115.078 0.011 1 103 29 30 SER H H 7.299 0.003 1 104 29 30 SER CA C 56.313 0.000 1 105 29 30 SER CB C 62.063 0.080 1 106 29 30 SER N N 110.796 0.179 1 107 30 31 TYR H H 7.961 0.023 1 108 30 31 TYR CA C 54.351 0.039 1 109 30 31 TYR CB C 37.397 0.000 1 110 30 31 TYR N N 121.729 0.179 1 111 31 32 SER H H 8.215 0.006 1 112 31 32 SER CA C 55.528 0.089 1 113 31 32 SER CB C 61.742 0.067 1 114 31 32 SER N N 115.859 0.013 1 115 32 33 ALA H H 8.338 0.017 1 116 32 33 ALA CA C 49.521 0.001 1 117 32 33 ALA CB C 17.323 0.000 1 118 32 33 ALA N N 126.769 0.137 1 119 33 34 SER H H 8.462 0.001 1 120 33 34 SER CA C 54.761 0.000 1 121 33 34 SER CB C 63.801 0.047 1 122 33 34 SER N N 114.666 0.020 1 123 34 35 TRP H H 9.106 0.000 1 124 34 35 TRP CA C 53.205 0.093 1 125 34 35 TRP CB C 30.832 0.093 1 126 34 35 TRP N N 118.941 0.009 1 127 35 36 TYR H H 9.408 0.001 1 128 35 36 TYR CA C 53.768 0.008 1 129 35 36 TYR CB C 39.813 0.086 1 130 35 36 TYR N N 120.004 0.007 1 131 36 37 GLN H H 9.672 0.001 1 132 36 37 GLN CA C 51.248 0.000 1 133 36 37 GLN CB C 31.789 0.069 1 134 36 37 GLN N N 123.193 0.012 1 135 37 38 GLN H H 9.628 0.001 1 136 37 38 GLN CA C 52.222 0.072 1 137 37 38 GLN CB C 29.452 0.095 1 138 37 38 GLN N N 128.849 0.005 1 139 38 39 LYS H H 8.899 0.002 1 140 38 39 LYS CA C 51.854 0.000 1 141 38 39 LYS CB C 29.673 0.000 1 142 38 39 LYS N N 131.052 0.010 1 143 40 41 GLY H H 8.744 0.001 1 144 40 41 GLY CA C 42.942 0.079 1 145 40 41 GLY N N 112.225 0.005 1 146 41 42 GLN H H 7.692 0.003 1 147 41 42 GLN CA C 50.802 0.003 1 148 41 42 GLN CB C 29.158 0.019 1 149 41 42 GLN N N 117.784 0.037 1 150 42 43 ALA H H 8.322 0.026 1 151 42 43 ALA CA C 47.907 0.000 1 152 42 43 ALA CB C 14.609 0.000 1 153 42 43 ALA N N 124.006 0.248 1 154 44 45 VAL H H 9.139 0.001 1 155 44 45 VAL CA C 58.309 0.077 1 156 44 45 VAL CB C 32.796 0.000 1 157 44 45 VAL N N 123.289 0.016 1 158 45 46 LEU H H 8.510 0.003 1 159 45 46 LEU CA C 52.365 0.021 1 160 45 46 LEU CB C 39.858 0.000 1 161 45 46 LEU N N 130.222 0.011 1 162 46 47 VAL H H 8.569 0.002 1 163 46 47 VAL CA C 59.444 0.026 1 164 46 47 VAL CB C 30.494 0.001 1 165 46 47 VAL N N 121.264 0.023 1 166 47 48 ILE H H 7.059 0.002 1 167 47 48 ILE CA C 53.928 0.022 1 168 47 48 ILE N N 115.778 0.003 1 169 48 49 PHE H H 9.353 0.004 1 170 48 49 PHE CA C 51.634 0.019 1 171 48 49 PHE CB C 39.823 0.057 1 172 48 49 PHE N N 123.159 0.006 1 173 49 50 ARG H H 8.641 0.001 1 174 49 50 ARG CA C 54.789 0.000 1 175 49 50 ARG CB C 26.215 0.091 1 176 49 50 ARG N N 121.720 0.009 1 177 50 51 LYS H H 8.871 0.001 1 178 50 51 LYS N N 114.138 0.017 1 179 51 52 SER H H 8.270 0.001 1 180 51 52 SER CA C 55.090 0.048 1 181 51 52 SER CB C 63.361 0.049 1 182 51 52 SER N N 109.881 0.010 1 183 52 53 ASN H H 8.320 0.015 1 184 52 53 ASN CA C 50.753 0.078 1 185 52 53 ASN CB C 36.295 0.000 1 186 52 53 ASN N N 122.450 0.154 1 187 53 54 ARG H H 8.720 0.023 1 188 53 54 ARG CA C 50.615 0.000 1 189 53 54 ARG CB C 30.427 0.000 1 190 53 54 ARG N N 124.353 0.115 1 191 55 56 SER H H 8.458 0.006 1 192 55 56 SER CA C 57.325 0.037 1 193 55 56 SER CB C 60.460 0.000 1 194 55 56 SER N N 116.112 0.034 1 195 56 57 GLY H H 8.678 0.004 1 196 56 57 GLY CA C 42.253 0.019 1 197 56 57 GLY N N 112.804 0.020 1 198 57 58 ILE H H 7.327 0.001 1 199 57 58 ILE CA C 52.557 0.000 1 200 57 58 ILE CB C 33.976 0.000 1 201 57 58 ILE N N 123.297 0.006 1 202 59 60 ASP H H 8.415 0.007 1 203 59 60 ASP CA C 52.625 0.000 1 204 59 60 ASP CB C 36.942 0.003 1 205 59 60 ASP N N 119.372 0.214 1 206 60 61 ARG H H 6.920 0.001 1 207 60 61 ARG CA C 54.296 0.000 1 208 60 61 ARG CB C 26.427 0.080 1 209 60 61 ARG N N 114.204 0.050 1 210 61 62 PHE H H 7.616 0.001 1 211 61 62 PHE CA C 55.214 0.075 1 212 61 62 PHE CB C 37.539 0.087 1 213 61 62 PHE N N 120.551 0.008 1 214 62 63 SER H H 8.895 0.002 1 215 62 63 SER CA C 54.840 0.474 1 216 62 63 SER CB C 62.683 0.635 1 217 62 63 SER N N 114.865 0.005 1 218 63 64 GLY H H 8.648 0.002 1 219 63 64 GLY CA C 41.632 0.076 1 220 63 64 GLY N N 107.698 0.010 1 221 64 65 SER H H 8.504 0.000 1 222 64 65 SER CA C 54.470 0.000 1 223 64 65 SER CB C 63.199 0.000 1 224 64 65 SER N N 112.835 0.006 1 225 68 69 ASN H H 8.498 0.015 1 226 68 69 ASN CA C 49.528 0.000 1 227 68 69 ASN CB C 35.123 0.114 1 228 68 69 ASN N N 124.602 0.151 1 229 69 70 THR H H 8.059 0.012 1 230 69 70 THR CA C 58.199 0.027 1 231 69 70 THR CB C 70.245 0.000 1 232 69 70 THR N N 110.070 0.111 1 233 70 71 ALA H H 9.323 0.002 1 234 70 71 ALA CA C 48.631 0.085 1 235 70 71 ALA CB C 19.842 0.094 1 236 70 71 ALA N N 127.566 0.007 1 237 71 72 SER H H 8.984 0.001 1 238 71 72 SER CA C 54.825 0.000 1 239 71 72 SER CB C 63.606 0.052 1 240 71 72 SER N N 114.455 0.008 1 241 72 73 LEU H H 8.591 0.001 1 242 72 73 LEU CA C 49.920 0.000 1 243 72 73 LEU CB C 39.130 0.089 1 244 72 73 LEU N N 128.986 0.009 1 245 73 74 THR H H 8.943 0.000 1 246 73 74 THR CA C 58.699 0.065 1 247 73 74 THR CB C 67.007 0.089 1 248 73 74 THR N N 123.557 0.089 1 249 74 75 ILE H H 8.571 0.014 1 250 74 75 ILE CA C 57.446 0.000 1 251 74 75 ILE CB C 36.476 0.000 1 252 74 75 ILE N N 126.742 0.044 1 253 75 76 THR H H 8.451 0.020 1 254 75 76 THR CA C 58.335 0.018 1 255 75 76 THR CB C 66.403 0.000 1 256 75 76 THR N N 122.587 0.076 1 257 76 77 GLY H H 7.228 0.001 1 258 76 77 GLY CA C 43.745 0.093 1 259 76 77 GLY N N 113.311 0.007 1 260 77 78 ALA H H 8.151 0.026 1 261 77 78 ALA CA C 51.049 0.000 1 262 77 78 ALA CB C 16.225 0.086 1 263 77 78 ALA N N 120.925 0.240 1 264 78 79 GLN H H 9.020 0.000 1 265 78 79 GLN CA C 50.289 0.000 1 266 78 79 GLN CB C 29.339 0.068 1 267 78 79 GLN N N 121.229 0.005 1 268 79 80 ALA H H 8.811 0.001 1 269 79 80 ALA CA C 53.414 0.086 1 270 79 80 ALA CB C 14.916 0.087 1 271 79 80 ALA N N 125.234 0.044 1 272 80 81 GLU H H 8.786 0.003 1 273 80 81 GLU CA C 54.814 0.000 1 274 80 81 GLU CB C 25.912 0.072 1 275 80 81 GLU N N 113.446 0.049 1 276 81 82 ASP H H 8.031 0.016 1 277 81 82 ASP CA C 51.765 0.078 1 278 81 82 ASP CB C 37.658 0.081 1 279 81 82 ASP N N 119.362 0.145 1 280 82 83 GLU H H 7.391 0.001 1 281 82 83 GLU CA C 56.402 0.000 1 282 82 83 GLU CB C 27.053 0.099 1 283 82 83 GLU N N 122.368 0.008 1 284 83 84 ALA H H 7.998 0.002 1 285 83 84 ALA CA C 48.692 0.093 1 286 83 84 ALA CB C 18.167 0.088 1 287 83 84 ALA N N 127.615 0.120 1 288 84 85 ASP H H 7.853 0.001 1 289 84 85 ASP CA C 51.053 0.000 1 290 84 85 ASP CB C 40.397 0.089 1 291 84 85 ASP N N 117.794 0.005 1 292 85 86 TYR H H 9.008 0.001 1 293 85 86 TYR CA C 54.337 0.000 1 294 85 86 TYR CB C 39.274 0.037 1 295 85 86 TYR N N 118.774 0.007 1 296 86 87 TYR H H 9.686 0.001 1 297 86 87 TYR CA C 54.547 0.000 1 298 86 87 TYR CB C 39.502 0.053 1 299 86 87 TYR N N 121.804 0.005 1 300 87 88 CYS H H 7.811 0.001 1 301 87 88 CYS CA C 50.288 0.091 1 302 87 88 CYS CB C 41.173 0.027 1 303 87 88 CYS N N 119.358 0.015 1 304 88 89 ASN H H 8.380 0.002 1 305 88 89 ASN CA C 49.017 0.090 1 306 88 89 ASN CB C 40.620 0.004 1 307 88 89 ASN N N 121.486 0.010 1 308 89 90 SER H H 8.223 0.001 1 309 89 90 SER CA C 54.266 0.000 1 310 89 90 SER CB C 62.697 0.098 1 311 89 90 SER N N 117.057 0.013 1 312 90 91 ARG H H 7.923 0.004 1 313 90 91 ARG CA C 52.717 0.031 1 314 90 91 ARG CB C 29.126 0.025 1 315 90 91 ARG N N 120.434 0.114 1 316 91 92 ASP H H 8.037 0.017 1 317 91 92 ASP CA C 50.623 0.000 1 318 91 92 ASP CB C 39.322 0.000 1 319 91 92 ASP N N 120.867 0.130 1 320 94 95 ALA H H 8.028 0.001 1 321 94 95 ALA CA C 49.887 0.000 1 322 94 95 ALA CB C 16.162 0.087 1 323 94 95 ALA N N 123.148 0.006 1 324 95 96 ASN H H 8.131 0.014 1 325 95 96 ASN CA C 51.015 0.000 1 326 95 96 ASN CB C 35.633 0.000 1 327 95 96 ASN N N 115.868 0.142 1 328 99 100 PHE H H 8.676 0.003 1 329 99 100 PHE CA C 54.288 0.000 1 330 99 100 PHE CB C 39.809 0.072 1 331 99 100 PHE N N 122.572 0.014 1 332 100 101 GLY H H 8.650 0.005 1 333 100 101 GLY CA C 42.025 0.000 1 334 100 101 GLY N N 108.674 0.014 1 335 101 102 GLY H H 8.101 0.000 1 336 101 102 GLY CA C 43.5112 0.000 1 337 101 102 GLY N N 104.349 0.000 1 338 102 103 GLY H H 7.123 0.005 1 339 102 103 GLY CA C 42.064 0.099 1 340 102 103 GLY N N 106.476 0.019 1 341 103 104 THR H H 8.278 0.003 1 342 103 104 THR CA C 58.463 0.062 1 343 103 104 THR CB C 70.184 0.000 1 344 103 104 THR N N 119.002 0.037 1 345 104 105 LYS H H 8.473 0.001 1 346 104 105 LYS CA C 53.510 0.014 1 347 104 105 LYS CB C 29.249 0.092 1 348 104 105 LYS N N 129.100 0.010 1 349 105 106 LEU H H 9.071 0.002 1 350 105 106 LEU CA C 50.998 0.027 1 351 105 106 LEU CB C 42.004 0.030 1 352 105 106 LEU N N 133.520 0.040 1 353 106 107 THR H H 8.581 0.011 1 354 106 107 THR CA C 59.220 0.026 1 355 106 107 THR CB C 67.967 0.041 1 356 106 107 THR N N 123.789 0.152 1 357 107 108 VAL H H 8.956 0.002 1 358 107 108 VAL CA C 57.982 0.084 1 359 107 108 VAL CB C 29.714 0.000 1 360 107 108 VAL N N 126.950 0.004 1 361 108 109 LEU H H 8.965 0.001 1 362 108 109 LEU CA C 51.749 0.010 1 363 108 109 LEU CB C 39.812 0.086 1 364 108 109 LEU N N 129.248 0.193 1 365 109 110 GLY H H 8.145 0.020 1 366 109 110 GLY CA C 43.246 0.000 1 367 109 110 GLY N N 118.384 0.217 1 stop_ save_