data_27885 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the N-terminal domain of Sfr1 ; _BMRB_accession_number 27885 _BMRB_flat_file_name bmr27885.str _Entry_type original _Submission_date 2019-04-27 _Accession_date 2019-04-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The N-terminal domain of Schizosaccharomyces pombe Swi five-dependent recombination repair protein (sfr1).' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sakakura Masayoshi . . 2 Kurihara Misato . . 3 Ito Kentaro . . 4 Maki Takahisa . . 5 Argunhan Bilge . . 6 Iwasaki Hiroshi . . 7 Takahashi Hideo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 157 "13C chemical shifts" 515 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-03-18 original BMRB . stop_ _Original_release_date 2019-04-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Rad51 Interaction Analysis Reveals a Novel Interplay Among Recombination Auxiliary Factors ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Argunhan Bilge . . 2 Sakakura Masayoshi . . 3 Afshar Negar . . 4 Kurihara Misato . . 5 Ito Kentaro . . 6 Maki Takahisa . . 7 Kanamaru Shuji . . 8 Murayama Yasuto . . 9 Tsubouchi Hideo . . 10 Takahashi Hideo . . 11 Iwasaki Hiroshi . . stop_ _Journal_abbreviation eLIFE _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 _Saveframe_category molecular_system _Mol_system_name Sfr1N _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Sfr1N $Sfr1N stop_ _System_molecular_weight 19421.66 _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sfr1N _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Sfr1N _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 176 _Mol_residue_sequence ; MSQTINSELNENATSQCKED LKVSLSESDLRDSQGQLGIE NPPKCNNSGNHSDNLGFIEQ SETVHPENEKALTPDLRDTK IHTSLPITTPFSKKRAREAK NILLKPFKSPLRQTASPQVA DTNLKPSLAVTNLNSDETNT SSEPVTSPLRTTPNSIKRQK RLFKSPISNCLNPKSD ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLN 4 THR 5 ILE 6 ASN 7 SER 8 GLU 9 LEU 10 ASN 11 GLU 12 ASN 13 ALA 14 THR 15 SER 16 GLN 17 CYS 18 LYS 19 GLU 20 ASP 21 LEU 22 LYS 23 VAL 24 SER 25 LEU 26 SER 27 GLU 28 SER 29 ASP 30 LEU 31 ARG 32 ASP 33 SER 34 GLN 35 GLY 36 GLN 37 LEU 38 GLY 39 ILE 40 GLU 41 ASN 42 PRO 43 PRO 44 LYS 45 CYS 46 ASN 47 ASN 48 SER 49 GLY 50 ASN 51 HIS 52 SER 53 ASP 54 ASN 55 LEU 56 GLY 57 PHE 58 ILE 59 GLU 60 GLN 61 SER 62 GLU 63 THR 64 VAL 65 HIS 66 PRO 67 GLU 68 ASN 69 GLU 70 LYS 71 ALA 72 LEU 73 THR 74 PRO 75 ASP 76 LEU 77 ARG 78 ASP 79 THR 80 LYS 81 ILE 82 HIS 83 THR 84 SER 85 LEU 86 PRO 87 ILE 88 THR 89 THR 90 PRO 91 PHE 92 SER 93 LYS 94 LYS 95 ARG 96 ALA 97 ARG 98 GLU 99 ALA 100 LYS 101 ASN 102 ILE 103 LEU 104 LEU 105 LYS 106 PRO 107 PHE 108 LYS 109 SER 110 PRO 111 LEU 112 ARG 113 GLN 114 THR 115 ALA 116 SER 117 PRO 118 GLN 119 VAL 120 ALA 121 ASP 122 THR 123 ASN 124 LEU 125 LYS 126 PRO 127 SER 128 LEU 129 ALA 130 VAL 131 THR 132 ASN 133 LEU 134 ASN 135 SER 136 ASP 137 GLU 138 THR 139 ASN 140 THR 141 SER 142 SER 143 GLU 144 PRO 145 VAL 146 THR 147 SER 148 PRO 149 LEU 150 ARG 151 THR 152 THR 153 PRO 154 ASN 155 SER 156 ILE 157 LYS 158 ARG 159 GLN 160 LYS 161 ARG 162 LEU 163 PHE 164 LYS 165 SER 166 PRO 167 ILE 168 SER 169 ASN 170 CYS 171 LEU 172 ASN 173 PRO 174 LYS 175 SER 176 ASP 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 $Sfr1N 'fission yeast' 4896 Eukaryota Fungi Schizosaccharomyces pombe 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 $Sfr1N 'recombinant technology' . Escherichia coli BL21(DE3)RIPL pBKN220 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sfr1N 0.175 mM 0.15 0.20 '[U-13C; U-15N]' 'sodium phosphate' 20 mM . . 'natural abundance' 'sodium chloride' 25 mM . . 'natural abundance' DTT 1 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2012.090.12.09 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.134 loop_ _Vendor _Address _Electronic_address Goddard . . 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 800 _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_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0.05 . M pH 6 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . 'separate tube (no insert) not similar to the experimental sample tube' . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . 'separate tube (no insert) not similar to the experimental sample tube' . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . 'separate tube (no insert) not similar to the experimental sample tube' . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HN(CO)CACB' '3D HNCO' '3D HN(CA)CO' 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 Sfr1N _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 3 3 GLN C C 175.923 0.188 1 2 3 3 GLN CA C 55.951 0.188 1 3 3 3 GLN CB C 29.548 0.234 1 4 4 4 THR H H 8.391 0.003 1 5 4 4 THR C C 174.534 0.188 1 6 4 4 THR CA C 62.066 0.188 1 7 4 4 THR CB C 69.926 0.234 1 8 4 4 THR N N 117.210 0.047 1 9 5 5 ILE H H 8.291 0.003 1 10 5 5 ILE C C 175.793 0.188 1 11 5 5 ILE CA C 61.087 0.188 1 12 5 5 ILE CB C 38.841 0.234 1 13 5 5 ILE N N 123.665 0.047 1 14 6 6 ASN H H 8.561 0.003 1 15 6 6 ASN C C 175.363 0.188 1 16 6 6 ASN CA C 53.366 0.188 1 17 6 6 ASN CB C 38.829 0.234 1 18 6 6 ASN N N 123.171 0.047 1 19 7 7 SER H H 8.354 0.003 1 20 7 7 SER C C 174.621 0.188 1 21 7 7 SER CA C 58.872 0.188 1 22 7 7 SER CB C 63.895 0.234 1 23 7 7 SER N N 117.061 0.047 1 24 8 8 GLU H H 8.478 0.003 1 25 8 8 GLU C C 176.531 0.188 1 26 8 8 GLU CA C 56.863 0.188 1 27 8 8 GLU CB C 29.922 0.234 1 28 8 8 GLU N N 122.494 0.047 1 29 9 9 LEU H H 8.088 0.003 1 30 9 9 LEU C C 177.026 0.188 1 31 9 9 LEU CA C 55.306 0.188 1 32 9 9 LEU CB C 42.257 0.234 1 33 9 9 LEU N N 121.994 0.047 1 34 10 10 ASN H H 8.333 0.003 1 35 10 10 ASN C C 175.427 0.188 1 36 10 10 ASN CA C 53.271 0.188 1 37 10 10 ASN CB C 38.951 0.234 1 38 10 10 ASN N N 119.492 0.047 1 39 11 11 GLU H H 8.501 0.003 1 40 11 11 GLU C C 176.419 0.188 1 41 11 11 GLU CA C 57.171 0.188 1 42 11 11 GLU CB C 30.028 0.234 1 43 11 11 GLU N N 121.650 0.047 1 44 12 12 ASN H H 8.423 0.003 1 45 12 12 ASN C C 175.210 0.188 1 46 12 12 ASN CA C 53.442 0.188 1 47 12 12 ASN CB C 38.865 0.234 1 48 12 12 ASN N N 118.892 0.047 1 49 13 13 ALA H H 8.170 0.003 1 50 13 13 ALA C C 178.208 0.188 1 51 13 13 ALA CA C 53.108 0.188 1 52 13 13 ALA CB C 19.201 0.234 1 53 13 13 ALA N N 124.021 0.047 1 54 14 14 THR H H 8.118 0.003 1 55 14 14 THR C C 174.919 0.188 1 56 14 14 THR CA C 62.091 0.188 1 57 14 14 THR CB C 69.821 0.234 1 58 14 14 THR N N 112.378 0.047 1 59 15 15 SER H H 8.228 0.003 1 60 15 15 SER C C 174.607 0.188 1 61 15 15 SER CA C 58.618 0.188 1 62 15 15 SER CB C 63.872 0.234 1 63 15 15 SER N N 117.664 0.047 1 64 16 16 GLN H H 8.375 0.003 1 65 16 16 GLN C C 175.891 0.188 1 66 16 16 GLN CA C 55.992 0.188 1 67 16 16 GLN CB C 29.428 0.234 1 68 16 16 GLN N N 122.022 0.047 1 69 17 17 CYS H H 8.390 0.003 1 70 17 17 CYS C C 174.752 0.188 1 71 17 17 CYS CA C 58.620 0.188 1 72 17 17 CYS CB C 27.853 0.234 1 73 17 17 CYS N N 120.622 0.047 1 74 18 18 LYS H H 8.476 0.003 1 75 18 18 LYS C C 176.712 0.188 1 76 18 18 LYS CA C 56.749 0.188 1 77 18 18 LYS CB C 32.898 0.234 1 78 18 18 LYS N N 124.377 0.047 1 79 19 19 GLU H H 8.436 0.003 1 80 19 19 GLU C C 176.175 0.188 1 81 19 19 GLU CA C 56.944 0.188 1 82 19 19 GLU CB C 30.211 0.234 1 83 19 19 GLU N N 121.842 0.047 1 84 20 20 ASP H H 8.317 0.003 1 85 20 20 ASP C C 176.217 0.188 1 86 20 20 ASP CA C 54.418 0.188 1 87 20 20 ASP CB C 41.041 0.234 1 88 20 20 ASP N N 121.445 0.047 1 89 21 21 LEU H H 8.071 0.003 1 90 21 21 LEU C C 177.361 0.188 1 91 21 21 LEU CA C 55.334 0.188 1 92 21 21 LEU CB C 42.222 0.234 1 93 21 21 LEU N N 122.611 0.047 1 94 22 22 LYS H H 8.254 0.003 1 95 22 22 LYS C C 176.666 0.188 1 96 22 22 LYS CA C 56.451 0.188 1 97 22 22 LYS CB C 32.668 0.234 1 98 22 22 LYS N N 122.144 0.047 1 99 23 23 VAL H H 8.034 0.003 1 100 23 23 VAL C C 176.223 0.188 1 101 23 23 VAL CA C 62.312 0.188 1 102 23 23 VAL CB C 32.953 0.234 1 103 23 23 VAL N N 120.865 0.047 1 104 24 24 SER H H 8.380 0.003 1 105 24 24 SER C C 174.496 0.188 1 106 24 24 SER CA C 58.126 0.188 1 107 24 24 SER CB C 63.918 0.234 1 108 24 24 SER N N 119.581 0.047 1 109 25 25 LEU H H 8.351 0.003 1 110 25 25 LEU C C 177.482 0.188 1 111 25 25 LEU CA C 55.287 0.188 1 112 25 25 LEU CB C 42.505 0.234 1 113 25 25 LEU N N 124.790 0.047 1 114 26 26 SER H H 8.455 0.003 1 115 26 26 SER C C 174.873 0.188 1 116 26 26 SER CA C 58.297 0.188 1 117 26 26 SER CB C 64.138 0.234 1 118 26 26 SER N N 116.751 0.047 1 119 27 27 GLU H H 8.526 0.003 1 120 27 27 GLU C C 177.229 0.188 1 121 27 27 GLU CA C 57.593 0.188 1 122 27 27 GLU CB C 29.958 0.234 1 123 27 27 GLU N N 122.644 0.047 1 124 28 28 SER H H 8.233 0.003 1 125 28 28 SER C C 174.690 0.188 1 126 28 28 SER CA C 59.310 0.188 1 127 28 28 SER CB C 63.693 0.234 1 128 28 28 SER N N 115.380 0.047 1 129 29 29 ASP H H 8.185 0.003 1 130 29 29 ASP C C 176.745 0.188 1 131 29 29 ASP CA C 54.977 0.188 1 132 29 29 ASP CB C 41.141 0.234 1 133 29 29 ASP N N 122.358 0.047 1 134 30 30 LEU H H 8.077 0.003 1 135 30 30 LEU C C 177.901 0.188 1 136 30 30 LEU CA C 55.740 0.188 1 137 30 30 LEU CB C 41.971 0.234 1 138 30 30 LEU N N 122.052 0.047 1 139 31 31 ARG H H 8.148 0.003 1 140 31 31 ARG C C 176.767 0.188 1 141 31 31 ARG CA C 56.905 0.188 1 142 31 31 ARG CB C 30.608 0.234 1 143 31 31 ARG N N 120.818 0.047 1 144 32 32 ASP H H 8.292 0.003 1 145 32 32 ASP C C 176.836 0.188 1 146 32 32 ASP CA C 54.702 0.188 1 147 32 32 ASP CB C 41.079 0.234 1 148 32 32 ASP N N 120.408 0.047 1 149 33 33 SER H H 8.208 0.003 1 150 33 33 SER C C 175.149 0.188 1 151 33 33 SER CA C 59.138 0.188 1 152 33 33 SER CB C 63.821 0.234 1 153 33 33 SER N N 115.873 0.047 1 154 34 34 GLN H H 8.340 0.003 1 155 34 34 GLN C C 176.799 0.188 1 156 34 34 GLN CA C 56.384 0.188 1 157 34 34 GLN CB C 29.081 0.234 1 158 34 34 GLN N N 121.285 0.047 1 159 35 35 GLY H H 8.317 0.003 1 160 35 35 GLY C C 174.300 0.188 1 161 35 35 GLY CA C 45.594 0.188 1 162 35 35 GLY N N 109.083 0.047 1 163 36 36 GLN H H 8.227 0.003 1 164 36 36 GLN C C 176.147 0.188 1 165 36 36 GLN CA C 55.838 0.188 1 166 36 36 GLN CB C 29.328 0.234 1 167 36 36 GLN N N 119.723 0.047 1 168 37 37 LEU H H 8.300 0.003 1 169 37 37 LEU C C 177.952 0.188 1 170 37 37 LEU CA C 55.480 0.188 1 171 37 37 LEU CB C 42.425 0.234 1 172 37 37 LEU N N 122.866 0.047 1 173 38 38 GLY H H 8.408 0.003 1 174 38 38 GLY C C 174.076 0.188 1 175 38 38 GLY CA C 45.475 0.188 1 176 38 38 GLY N N 109.650 0.047 1 177 39 39 ILE H H 7.827 0.003 1 178 39 39 ILE C C 176.150 0.188 1 179 39 39 ILE CA C 61.031 0.188 1 180 39 39 ILE CB C 38.847 0.234 1 181 39 39 ILE N N 119.259 0.047 1 182 40 40 GLU H H 8.483 0.003 1 183 40 40 GLU C C 175.877 0.188 1 184 40 40 GLU CA C 56.522 0.188 1 185 40 40 GLU CB C 30.308 0.234 1 186 40 40 GLU N N 124.379 0.047 1 187 41 41 ASN H H 8.469 0.003 1 188 41 41 ASN C C 172.295 0.188 1 189 41 41 ASN CA C 51.460 0.188 1 190 41 41 ASN CB C 38.806 0.234 1 191 41 41 ASN N N 120.581 0.047 1 192 43 43 PRO C C 176.971 0.188 1 193 43 43 PRO CA C 62.919 0.188 1 194 43 43 PRO CB C 32.028 0.234 1 195 44 44 LYS H H 8.429 0.003 1 196 44 44 LYS C C 176.611 0.188 1 197 44 44 LYS CA C 56.294 0.188 1 198 44 44 LYS CB C 33.003 0.234 1 199 44 44 LYS N N 121.547 0.047 1 200 45 45 CYS H H 8.394 0.003 1 201 45 45 CYS C C 174.252 0.188 1 202 45 45 CYS CA C 58.236 0.188 1 203 45 45 CYS CB C 28.122 0.234 1 204 45 45 CYS N N 120.321 0.047 1 205 46 46 ASN H H 8.604 0.003 1 206 46 46 ASN C C 174.991 0.188 1 207 46 46 ASN CA C 53.310 0.188 1 208 46 46 ASN CB C 38.837 0.234 1 209 46 46 ASN N N 121.775 0.047 1 210 47 47 ASN H H 8.450 0.003 1 211 47 47 ASN C C 175.410 0.188 1 212 47 47 ASN CA C 53.336 0.188 1 213 47 47 ASN CB C 38.867 0.234 1 214 47 47 ASN N N 119.818 0.047 1 215 48 48 SER H H 8.354 0.003 1 216 48 48 SER C C 175.075 0.188 1 217 48 48 SER CA C 58.903 0.188 1 218 48 48 SER CB C 63.924 0.234 1 219 48 48 SER N N 116.211 0.047 1 220 49 49 GLY H H 8.417 0.003 1 221 49 49 GLY C C 173.799 0.188 1 222 49 49 GLY CA C 45.347 0.188 1 223 49 49 GLY N N 110.394 0.047 1 224 50 50 ASN H H 8.228 0.003 1 225 50 50 ASN C C 175.160 0.188 1 226 50 50 ASN CA C 53.131 0.188 1 227 50 50 ASN CB C 38.830 0.234 1 228 50 50 ASN N N 118.463 0.047 1 229 51 51 HIS C C 174.932 0.188 1 230 51 51 HIS CA C 55.796 0.188 1 231 51 51 HIS CB C 29.426 0.234 1 232 52 52 SER H H 8.311 0.003 1 233 52 52 SER C C 174.220 0.188 1 234 52 52 SER CA C 58.608 0.188 1 235 52 52 SER CB C 63.989 0.234 1 236 52 52 SER N N 116.787 0.047 1 237 53 53 ASP H H 8.428 0.003 1 238 53 53 ASP C C 176.004 0.188 1 239 53 53 ASP CA C 54.492 0.188 1 240 53 53 ASP CB C 41.142 0.234 1 241 53 53 ASP N N 122.125 0.047 1 242 54 54 ASN H H 8.329 0.003 1 243 54 54 ASN C C 175.346 0.188 1 244 54 54 ASN CA C 53.379 0.188 1 245 54 54 ASN CB C 38.676 0.234 1 246 54 54 ASN N N 118.377 0.047 1 247 55 55 LEU H H 8.241 0.003 1 248 55 55 LEU C C 177.866 0.188 1 249 55 55 LEU CA C 55.648 0.188 1 250 55 55 LEU CB C 42.007 0.234 1 251 55 55 LEU N N 122.035 0.047 1 252 56 56 GLY H H 8.314 0.003 1 253 56 56 GLY C C 173.739 0.188 1 254 56 56 GLY CA C 45.300 0.188 1 255 56 56 GLY N N 108.589 0.047 1 256 57 57 PHE H H 7.961 0.003 1 257 57 57 PHE C C 175.491 0.188 1 258 57 57 PHE CA C 57.849 0.188 1 259 57 57 PHE CB C 39.610 0.234 1 260 57 57 PHE N N 120.055 0.047 1 261 58 58 ILE H H 7.988 0.003 1 262 58 58 ILE C C 175.686 0.188 1 263 58 58 ILE CA C 60.846 0.188 1 264 58 58 ILE CB C 38.951 0.234 1 265 58 58 ILE N N 123.539 0.047 1 266 59 59 GLU H H 8.430 0.003 1 267 59 59 GLU C C 176.422 0.188 1 268 59 59 GLU CA C 56.740 0.188 1 269 59 59 GLU CB C 30.210 0.234 1 270 59 59 GLU N N 125.421 0.047 1 271 60 60 GLN H H 8.463 0.003 1 272 60 60 GLN C C 175.919 0.188 1 273 60 60 GLN CA C 55.930 0.188 1 274 60 60 GLN CB C 29.509 0.234 1 275 60 60 GLN N N 122.135 0.047 1 276 61 61 SER H H 8.384 0.003 1 277 61 61 SER C C 174.625 0.188 1 278 61 61 SER CA C 58.697 0.188 1 279 61 61 SER CB C 63.907 0.234 1 280 61 61 SER N N 117.298 0.047 1 281 62 62 GLU H H 8.489 0.003 1 282 62 62 GLU C C 176.525 0.188 1 283 62 62 GLU CA C 56.703 0.188 1 284 62 62 GLU CB C 30.269 0.234 1 285 62 62 GLU N N 122.641 0.047 1 286 63 63 THR H H 8.186 0.003 1 287 63 63 THR C C 174.194 0.188 1 288 63 63 THR CA C 62.069 0.188 1 289 63 63 THR CB C 69.858 0.234 1 290 63 63 THR N N 115.839 0.047 1 291 64 64 VAL H H 8.074 0.003 1 292 64 64 VAL C C 175.478 0.188 1 293 64 64 VAL CA C 62.218 0.188 1 294 64 64 VAL CB C 32.679 0.234 1 295 64 64 VAL N N 122.977 0.047 1 296 65 65 HIS H H 8.603 0.003 1 297 65 65 HIS C C 172.845 0.188 1 298 65 65 HIS CA C 53.304 0.188 1 299 65 65 HIS CB C 28.994 0.234 1 300 65 65 HIS N N 123.705 0.047 1 301 66 66 PRO C C 177.226 0.188 1 302 66 66 PRO CA C 63.471 0.188 1 303 66 66 PRO CB C 32.117 0.234 1 304 67 67 GLU H H 8.923 0.003 1 305 67 67 GLU C C 176.600 0.188 1 306 67 67 GLU CA C 57.183 0.188 1 307 67 67 GLU CB C 29.771 0.234 1 308 67 67 GLU N N 121.128 0.047 1 309 68 68 ASN H H 8.364 0.003 1 310 68 68 ASN C C 175.386 0.188 1 311 68 68 ASN CA C 53.397 0.188 1 312 68 68 ASN CB C 38.741 0.234 1 313 68 68 ASN N N 118.622 0.047 1 314 69 69 GLU H H 8.262 0.003 1 315 69 69 GLU C C 176.639 0.188 1 316 69 69 GLU CA C 57.102 0.188 1 317 69 69 GLU CB C 30.144 0.234 1 318 69 69 GLU N N 121.199 0.047 1 319 70 70 LYS H H 8.222 0.003 1 320 70 70 LYS C C 176.281 0.188 1 321 70 70 LYS CA C 56.372 0.188 1 322 70 70 LYS CB C 32.851 0.234 1 323 70 70 LYS N N 121.798 0.047 1 324 71 71 ALA H H 8.154 0.003 1 325 71 71 ALA C C 177.549 0.188 1 326 71 71 ALA CA C 52.379 0.188 1 327 71 71 ALA CB C 19.177 0.234 1 328 71 71 ALA N N 124.547 0.047 1 329 72 72 LEU H H 8.181 0.003 1 330 72 72 LEU C C 177.333 0.188 1 331 72 72 LEU CA C 55.070 0.188 1 332 72 72 LEU CB C 42.435 0.234 1 333 72 72 LEU N N 121.361 0.047 1 334 73 73 THR H H 7.999 0.003 1 335 73 73 THR C C 173.088 0.188 1 336 73 73 THR CA C 59.565 0.188 1 337 73 73 THR CB C 69.587 0.234 1 338 73 73 THR N N 116.265 0.047 1 339 74 74 PRO C C 176.500 0.188 1 340 74 74 PRO CA C 63.677 0.188 1 341 74 74 PRO CB C 32.079 0.234 1 342 75 75 ASP H H 8.435 0.003 1 343 75 75 ASP C C 176.509 0.188 1 344 75 75 ASP CA C 54.283 0.188 1 345 75 75 ASP CB C 40.984 0.234 1 346 75 75 ASP N N 119.677 0.047 1 347 76 76 LEU H H 8.163 0.003 1 348 76 76 LEU C C 177.653 0.188 1 349 76 76 LEU CA C 55.343 0.188 1 350 76 76 LEU CB C 41.961 0.234 1 351 76 76 LEU N N 123.205 0.047 1 352 77 77 ARG H H 8.225 0.003 1 353 77 77 ARG C C 176.306 0.188 1 354 77 77 ARG CA C 56.790 0.188 1 355 77 77 ARG CB C 30.570 0.234 1 356 77 77 ARG N N 120.651 0.047 1 357 78 78 ASP H H 8.260 0.003 1 358 78 78 ASP C C 176.659 0.188 1 359 78 78 ASP CA C 54.423 0.188 1 360 78 78 ASP CB C 41.184 0.234 1 361 78 78 ASP N N 120.535 0.047 1 362 79 79 THR H H 8.058 0.003 1 363 79 79 THR C C 174.921 0.188 1 364 79 79 THR CA C 62.289 0.188 1 365 79 79 THR CB C 69.598 0.234 1 366 79 79 THR N N 114.603 0.047 1 367 80 80 LYS H H 8.257 0.003 1 368 80 80 LYS C C 176.499 0.188 1 369 80 80 LYS CA C 56.555 0.188 1 370 80 80 LYS CB C 32.615 0.234 1 371 80 80 LYS N N 122.916 0.047 1 372 81 81 ILE H H 7.928 0.003 1 373 81 81 ILE C C 176.087 0.188 1 374 81 81 ILE CA C 61.134 0.188 1 375 81 81 ILE CB C 38.552 0.234 1 376 81 81 ILE N N 120.631 0.047 1 377 82 82 HIS H H 8.482 0.003 1 378 82 82 HIS C C 175.035 0.188 1 379 82 82 HIS CA C 55.632 0.188 1 380 82 82 HIS CB C 29.969 0.234 1 381 82 82 HIS N N 123.391 0.047 1 382 83 83 THR H H 8.135 0.003 1 383 83 83 THR C C 174.211 0.188 1 384 83 83 THR CA C 61.803 0.188 1 385 83 83 THR CB C 69.909 0.234 1 386 83 83 THR N N 115.862 0.047 1 387 84 84 SER H H 8.369 0.003 1 388 84 84 SER C C 173.966 0.188 1 389 84 84 SER CA C 58.166 0.188 1 390 84 84 SER CB C 63.983 0.234 1 391 84 84 SER N N 118.444 0.047 1 392 85 85 LEU H H 8.243 0.003 1 393 85 85 LEU C C 175.201 0.188 1 394 85 85 LEU CA C 53.149 0.188 1 395 85 85 LEU CB C 41.800 0.234 1 396 85 85 LEU N N 125.337 0.047 1 397 86 86 PRO C C 176.684 0.188 1 398 86 86 PRO CA C 63.040 0.188 1 399 86 86 PRO CB C 31.907 0.234 1 400 87 87 ILE H H 8.271 0.003 1 401 87 87 ILE C C 176.642 0.188 1 402 87 87 ILE CA C 61.232 0.188 1 403 87 87 ILE CB C 38.786 0.234 1 404 87 87 ILE N N 121.180 0.047 1 405 88 88 THR H H 8.218 0.003 1 406 88 88 THR C C 174.363 0.188 1 407 88 88 THR CA C 61.569 0.188 1 408 88 88 THR CB C 69.915 0.234 1 409 88 88 THR N N 118.233 0.047 1 410 89 89 THR H H 8.235 0.003 1 411 89 89 THR C C 173.101 0.188 1 412 89 89 THR CA C 59.802 0.188 1 413 89 89 THR CB C 69.881 0.234 1 414 89 89 THR N N 118.403 0.047 1 415 90 90 PRO C C 176.849 0.188 1 416 90 90 PRO CA C 63.483 0.188 1 417 90 90 PRO CB C 31.896 0.234 1 418 91 91 PHE H H 8.184 0.003 1 419 91 91 PHE C C 175.973 0.188 1 420 91 91 PHE CA C 58.081 0.188 1 421 91 91 PHE CB C 39.302 0.234 1 422 91 91 PHE N N 119.732 0.047 1 423 92 92 SER H H 8.056 0.003 1 424 92 92 SER C C 174.608 0.188 1 425 92 92 SER CA C 58.441 0.188 1 426 92 92 SER CB C 64.043 0.234 1 427 92 92 SER N N 117.151 0.047 1 428 93 93 LYS H H 8.291 0.003 1 429 93 93 LYS C C 176.726 0.188 1 430 93 93 LYS CA C 56.816 0.188 1 431 93 93 LYS CB C 32.853 0.234 1 432 93 93 LYS N N 123.665 0.047 1 433 94 94 LYS H H 8.187 0.003 1 434 94 94 LYS C C 177.280 0.188 1 435 94 94 LYS CA C 56.832 0.188 1 436 94 94 LYS CB C 32.927 0.234 1 437 94 94 LYS N N 122.092 0.047 1 438 95 95 ARG H H 8.280 0.003 1 439 95 95 ARG C C 176.232 0.188 1 440 95 95 ARG CA C 56.322 0.188 1 441 95 95 ARG CB C 30.575 0.234 1 442 95 95 ARG N N 122.220 0.047 1 443 96 96 ALA H H 8.293 0.003 1 444 96 96 ALA C C 178.010 0.188 1 445 96 96 ALA CA C 52.856 0.188 1 446 96 96 ALA CB C 19.187 0.234 1 447 96 96 ALA N N 125.318 0.047 1 448 97 97 ARG H H 8.283 0.003 1 449 97 97 ARG C C 176.650 0.188 1 450 97 97 ARG CA C 56.549 0.188 1 451 97 97 ARG CB C 30.705 0.234 1 452 97 97 ARG N N 120.146 0.047 1 453 98 98 GLU H H 8.362 0.003 1 454 98 98 GLU C C 176.314 0.188 1 455 98 98 GLU CA C 56.564 0.188 1 456 98 98 GLU CB C 30.362 0.234 1 457 98 98 GLU N N 121.899 0.047 1 458 99 99 ALA H H 8.294 0.003 1 459 99 99 ALA C C 177.744 0.188 1 460 99 99 ALA CA C 52.674 0.188 1 461 99 99 ALA CB C 19.154 0.234 1 462 99 99 ALA N N 125.383 0.047 1 463 100 100 LYS H H 8.227 0.003 1 464 100 100 LYS C C 176.236 0.188 1 465 100 100 LYS CA C 56.439 0.188 1 466 100 100 LYS CB C 33.025 0.234 1 467 100 100 LYS N N 120.002 0.047 1 468 101 101 ASN H H 8.376 0.003 1 469 101 101 ASN C C 175.200 0.188 1 470 101 101 ASN CA C 53.315 0.188 1 471 101 101 ASN CB C 38.695 0.234 1 472 101 101 ASN N N 119.582 0.047 1 473 102 102 ILE H H 8.028 0.003 1 474 102 102 ILE C C 175.932 0.188 1 475 102 102 ILE CA C 61.408 0.188 1 476 102 102 ILE CB C 38.666 0.234 1 477 102 102 ILE N N 121.081 0.047 1 478 103 103 LEU H H 8.195 0.003 1 479 103 103 LEU C C 176.867 0.188 1 480 103 103 LEU CA C 55.032 0.188 1 481 103 103 LEU CB C 42.209 0.234 1 482 103 103 LEU N N 125.490 0.047 1 483 104 104 LEU H H 8.076 0.003 1 484 104 104 LEU C C 176.814 0.188 1 485 104 104 LEU CA C 54.913 0.188 1 486 104 104 LEU CB C 42.365 0.234 1 487 104 104 LEU N N 123.354 0.047 1 488 105 105 LYS H H 8.180 0.003 1 489 105 105 LYS C C 174.289 0.188 1 490 105 105 LYS CA C 54.107 0.188 1 491 105 105 LYS CB C 32.487 0.234 1 492 105 105 LYS N N 123.253 0.047 1 493 106 106 PRO C C 176.578 0.188 1 494 106 106 PRO CA C 63.070 0.188 1 495 106 106 PRO CB C 31.867 0.234 1 496 107 107 PHE H H 8.264 0.003 1 497 107 107 PHE C C 175.370 0.188 1 498 107 107 PHE CA C 57.743 0.188 1 499 107 107 PHE CB C 39.767 0.234 1 500 107 107 PHE N N 120.986 0.047 1 501 108 108 LYS H H 8.105 0.003 1 502 108 108 LYS C C 175.485 0.188 1 503 108 108 LYS CA C 55.631 0.188 1 504 108 108 LYS CB C 33.362 0.234 1 505 108 108 LYS N N 124.192 0.047 1 506 109 109 SER H H 8.294 0.003 1 507 109 109 SER C C 173.006 0.188 1 508 109 109 SER CA C 56.473 0.188 1 509 109 109 SER CB C 64.096 0.234 1 510 109 109 SER N N 119.172 0.047 1 511 110 110 PRO C C 176.722 0.188 1 512 110 110 PRO CA C 63.201 0.188 1 513 110 110 PRO CB C 32.077 0.234 1 514 111 111 LEU H H 8.194 0.003 1 515 111 111 LEU C C 177.295 0.188 1 516 111 111 LEU CA C 55.283 0.188 1 517 111 111 LEU CB C 42.260 0.234 1 518 111 111 LEU N N 122.023 0.047 1 519 112 112 ARG H H 8.298 0.003 1 520 112 112 ARG C C 176.041 0.188 1 521 112 112 ARG CA C 55.910 0.188 1 522 112 112 ARG CB C 30.778 0.234 1 523 112 112 ARG N N 122.118 0.047 1 524 113 113 GLN H H 8.463 0.003 1 525 113 113 GLN C C 176.001 0.188 1 526 113 113 GLN CA C 55.840 0.188 1 527 113 113 GLN CB C 29.646 0.234 1 528 113 113 GLN N N 122.135 0.047 1 529 114 114 THR H H 8.220 0.003 1 530 114 114 THR C C 174.044 0.188 1 531 114 114 THR CA C 61.789 0.188 1 532 114 114 THR CB C 69.976 0.234 1 533 114 114 THR N N 115.997 0.047 1 534 115 115 ALA H H 8.365 0.003 1 535 115 115 ALA C C 177.390 0.188 1 536 115 115 ALA CA C 52.337 0.188 1 537 115 115 ALA CB C 19.398 0.234 1 538 115 115 ALA N N 126.604 0.047 1 539 116 116 SER H H 8.333 0.003 1 540 116 116 SER C C 172.739 0.188 1 541 116 116 SER CA C 56.437 0.188 1 542 116 116 SER CB C 63.359 0.234 1 543 116 116 SER N N 116.987 0.047 1 544 117 117 PRO C C 176.786 0.188 1 545 117 117 PRO CA C 63.340 0.188 1 546 117 117 PRO CB C 32.032 0.234 1 547 118 118 GLN H H 8.447 0.003 1 548 118 118 GLN C C 176.002 0.188 1 549 118 118 GLN CA C 55.828 0.188 1 550 118 118 GLN CB C 29.417 0.234 1 551 118 118 GLN N N 120.813 0.047 1 552 119 119 VAL H H 8.159 0.003 1 553 119 119 VAL C C 175.755 0.188 1 554 119 119 VAL CA C 62.179 0.188 1 555 119 119 VAL CB C 32.848 0.234 1 556 119 119 VAL N N 121.764 0.047 1 557 120 120 ALA H H 8.378 0.003 1 558 120 120 ALA C C 177.344 0.188 1 559 120 120 ALA CA C 52.472 0.188 1 560 120 120 ALA CB C 19.327 0.234 1 561 120 120 ALA N N 127.631 0.047 1 562 121 121 ASP H H 8.293 0.003 1 563 121 121 ASP C C 176.846 0.188 1 564 121 121 ASP CA C 54.358 0.188 1 565 121 121 ASP CB C 41.232 0.234 1 566 121 121 ASP N N 120.203 0.047 1 567 122 122 THR H H 8.118 0.003 1 568 122 122 THR C C 174.635 0.188 1 569 122 122 THR CA C 62.225 0.188 1 570 122 122 THR CB C 69.517 0.234 1 571 122 122 THR N N 114.459 0.047 1 572 123 123 ASN H H 8.465 0.003 1 573 123 123 ASN C C 175.001 0.188 1 574 123 123 ASN CA C 53.548 0.188 1 575 123 123 ASN CB C 38.783 0.234 1 576 123 123 ASN N N 120.578 0.047 1 577 124 124 LEU H H 8.002 0.003 1 578 124 124 LEU C C 176.986 0.188 1 579 124 124 LEU CA C 55.136 0.188 1 580 124 124 LEU CB C 42.358 0.234 1 581 124 124 LEU N N 122.026 0.047 1 582 125 125 LYS H H 8.230 0.003 1 583 125 125 LYS C C 174.402 0.188 1 584 125 125 LYS CA C 54.128 0.188 1 585 125 125 LYS CB C 32.351 0.234 1 586 125 125 LYS N N 123.427 0.047 1 587 126 126 PRO C C 177.012 0.188 1 588 126 126 PRO CA C 63.270 0.188 1 589 126 126 PRO CB C 32.082 0.234 1 590 127 127 SER H H 8.391 0.003 1 591 127 127 SER C C 174.605 0.188 1 592 127 127 SER CA C 58.268 0.188 1 593 127 127 SER CB C 63.849 0.234 1 594 127 127 SER N N 116.118 0.047 1 595 128 128 LEU H H 8.235 0.003 1 596 128 128 LEU C C 176.920 0.188 1 597 128 128 LEU CA C 55.059 0.188 1 598 128 128 LEU CB C 42.459 0.234 1 599 128 128 LEU N N 124.339 0.047 1 600 129 129 ALA H H 8.207 0.003 1 601 129 129 ALA C C 177.637 0.188 1 602 129 129 ALA CA C 52.457 0.188 1 603 129 129 ALA CB C 19.142 0.234 1 604 129 129 ALA N N 124.849 0.047 1 605 130 130 VAL H H 8.084 0.003 1 606 130 130 VAL C C 176.419 0.188 1 607 130 130 VAL CA C 62.292 0.188 1 608 130 130 VAL CB C 32.745 0.234 1 609 130 130 VAL N N 119.330 0.047 1 610 131 131 THR H H 8.192 0.003 1 611 131 131 THR C C 174.073 0.188 1 612 131 131 THR CA C 61.817 0.188 1 613 131 131 THR CB C 69.890 0.234 1 614 131 131 THR N N 117.559 0.047 1 615 132 132 ASN H H 8.429 0.003 1 616 132 132 ASN C C 174.954 0.188 1 617 132 132 ASN CA C 53.173 0.188 1 618 132 132 ASN CB C 38.855 0.234 1 619 132 132 ASN N N 121.252 0.047 1 620 133 133 LEU H H 8.267 0.003 1 621 133 133 LEU C C 177.135 0.188 1 622 133 133 LEU CA C 55.426 0.188 1 623 133 133 LEU CB C 42.340 0.234 1 624 133 133 LEU N N 122.784 0.047 1 625 134 134 ASN H H 8.452 0.003 1 626 134 134 ASN C C 175.309 0.188 1 627 134 134 ASN CA C 53.261 0.188 1 628 134 134 ASN CB C 38.927 0.234 1 629 134 134 ASN N N 119.306 0.047 1 630 135 135 SER H H 8.261 0.003 1 631 135 135 SER C C 174.367 0.188 1 632 135 135 SER CA C 58.608 0.188 1 633 135 135 SER CB C 63.971 0.234 1 634 135 135 SER N N 116.335 0.047 1 635 136 136 ASP H H 8.399 0.003 1 636 136 136 ASP C C 176.549 0.188 1 637 136 136 ASP CA C 54.600 0.188 1 638 136 136 ASP CB C 41.095 0.234 1 639 136 136 ASP N N 122.205 0.047 1 640 137 137 GLU H H 8.371 0.003 1 641 137 137 GLU C C 176.886 0.188 1 642 137 137 GLU CA C 56.944 0.188 1 643 137 137 GLU CB C 30.092 0.234 1 644 137 137 GLU N N 121.009 0.047 1 645 138 138 THR H H 8.197 0.003 1 646 138 138 THR C C 174.567 0.188 1 647 138 138 THR CA C 62.370 0.188 1 648 138 138 THR CB C 69.876 0.234 1 649 138 138 THR N N 114.214 0.047 1 650 139 139 ASN H H 8.411 0.003 1 651 139 139 ASN C C 175.518 0.188 1 652 139 139 ASN CA C 53.376 0.188 1 653 139 139 ASN CB C 38.880 0.234 1 654 139 139 ASN N N 121.164 0.047 1 655 140 140 THR H H 8.178 0.003 1 656 140 140 THR C C 174.800 0.188 1 657 140 140 THR CA C 62.005 0.188 1 658 140 140 THR CB C 69.751 0.234 1 659 140 140 THR N N 114.374 0.047 1 660 141 141 SER H H 8.341 0.003 1 661 141 141 SER C C 174.521 0.188 1 662 141 141 SER CA C 58.414 0.188 1 663 141 141 SER CB C 63.957 0.234 1 664 141 141 SER N N 117.957 0.047 1 665 142 142 SER H H 8.354 0.003 1 666 142 142 SER C C 174.152 0.188 1 667 142 142 SER CA C 58.312 0.188 1 668 142 142 SER CB C 63.960 0.234 1 669 142 142 SER N N 117.939 0.047 1 670 143 143 GLU H H 8.263 0.003 1 671 143 143 GLU C C 174.447 0.188 1 672 143 143 GLU CA C 54.477 0.188 1 673 143 143 GLU CB C 29.683 0.234 1 674 143 143 GLU N N 123.685 0.047 1 675 144 144 PRO C C 177.054 0.188 1 676 144 144 PRO CA C 63.120 0.188 1 677 144 144 PRO CB C 32.060 0.234 1 678 145 145 VAL H H 8.320 0.003 1 679 145 145 VAL C C 176.574 0.188 1 680 145 145 VAL CA C 62.587 0.188 1 681 145 145 VAL CB C 32.621 0.234 1 682 145 145 VAL N N 120.471 0.047 1 683 146 146 THR H H 8.154 0.003 1 684 146 146 THR C C 174.261 0.188 1 685 146 146 THR CA C 61.617 0.188 1 686 146 146 THR CB C 69.869 0.234 1 687 146 146 THR N N 117.083 0.047 1 688 147 147 SER H H 8.240 0.003 1 689 147 147 SER C C 173.107 0.188 1 690 147 147 SER CA C 56.258 0.188 1 691 147 147 SER CB C 63.799 0.234 1 692 147 147 SER N N 119.200 0.047 1 693 148 148 PRO C C 176.846 0.188 1 694 148 148 PRO CA C 63.430 0.188 1 695 148 148 PRO CB C 32.028 0.234 1 696 149 149 LEU H H 8.166 0.003 1 697 149 149 LEU C C 177.445 0.188 1 698 149 149 LEU CA C 55.328 0.188 1 699 149 149 LEU CB C 42.163 0.234 1 700 149 149 LEU N N 121.145 0.047 1 701 150 150 ARG H H 8.232 0.003 1 702 150 150 ARG C C 176.277 0.188 1 703 150 150 ARG CA C 55.957 0.188 1 704 150 150 ARG CB C 30.749 0.234 1 705 150 150 ARG N N 121.512 0.047 1 706 151 151 THR H H 8.118 0.003 1 707 151 151 THR C C 174.317 0.188 1 708 151 151 THR CA C 61.585 0.188 1 709 151 151 THR CB C 69.954 0.234 1 710 151 151 THR N N 115.122 0.047 1 711 152 152 THR H H 8.194 0.003 1 712 152 152 THR C C 172.990 0.188 1 713 152 152 THR CA C 59.775 0.188 1 714 152 152 THR CB C 69.820 0.234 1 715 152 152 THR N N 118.618 0.047 1 716 153 153 PRO C C 176.976 0.188 1 717 153 153 PRO CA C 63.653 0.188 1 718 153 153 PRO CB C 32.070 0.234 1 719 154 154 ASN H H 8.512 0.003 1 720 154 154 ASN C C 175.551 0.188 1 721 154 154 ASN CA C 53.690 0.188 1 722 154 154 ASN CB C 38.689 0.234 1 723 154 154 ASN N N 118.264 0.047 1 724 155 155 SER H H 8.193 0.003 1 725 155 155 SER C C 174.811 0.188 1 726 155 155 SER CA C 58.787 0.188 1 727 155 155 SER CB C 63.789 0.234 1 728 155 155 SER N N 116.010 0.047 1 729 156 156 ILE H H 8.035 0.003 1 730 156 156 ILE C C 176.466 0.188 1 731 156 156 ILE CA C 61.624 0.188 1 732 156 156 ILE CB C 38.458 0.234 1 733 156 156 ILE N N 122.537 0.047 1 734 157 157 LYS H H 8.249 0.003 1 735 157 157 LYS C C 176.663 0.188 1 736 157 157 LYS CA C 56.616 0.188 1 737 157 157 LYS CB C 32.773 0.234 1 738 157 157 LYS N N 124.790 0.047 1 739 158 158 ARG H H 8.267 0.003 1 740 158 158 ARG C C 176.417 0.188 1 741 158 158 ARG CA C 56.216 0.188 1 742 158 158 ARG CB C 30.689 0.234 1 743 158 158 ARG N N 122.165 0.047 1 744 159 159 GLN H H 8.354 0.003 1 745 159 159 GLN C C 175.986 0.188 1 746 159 159 GLN CA C 55.966 0.188 1 747 159 159 GLN CB C 29.574 0.234 1 748 159 159 GLN N N 121.733 0.047 1 749 160 160 LYS H H 8.377 0.003 1 750 160 160 LYS C C 176.399 0.188 1 751 160 160 LYS CA C 56.594 0.188 1 752 160 160 LYS CB C 33.007 0.234 1 753 160 160 LYS N N 123.142 0.047 1 754 161 161 ARG H H 8.323 0.003 1 755 161 161 ARG C C 175.740 0.188 1 756 161 161 ARG CA C 56.060 0.188 1 757 161 161 ARG CB C 30.778 0.234 1 758 161 161 ARG N N 122.542 0.047 1 759 162 162 LEU H H 8.230 0.003 1 760 162 162 LEU C C 176.679 0.188 1 761 162 162 LEU CA C 54.892 0.188 1 762 162 162 LEU CB C 42.552 0.234 1 763 162 162 LEU N N 123.678 0.047 1 764 163 163 PHE H H 8.222 0.003 1 765 163 163 PHE C C 175.205 0.188 1 766 163 163 PHE CA C 57.533 0.188 1 767 163 163 PHE CB C 39.927 0.234 1 768 163 163 PHE N N 121.508 0.047 1 769 164 164 LYS H H 8.211 0.003 1 770 164 164 LYS C C 175.738 0.188 1 771 164 164 LYS CA C 55.791 0.188 1 772 164 164 LYS CB C 33.301 0.234 1 773 164 164 LYS N N 123.616 0.047 1 774 165 165 SER H H 8.321 0.003 1 775 165 165 SER C C 172.964 0.188 1 776 165 165 SER CA C 56.470 0.188 1 777 165 165 SER CB C 63.556 0.234 1 778 165 165 SER N N 119.103 0.047 1 779 166 166 PRO C C 176.870 0.188 1 780 166 166 PRO CA C 63.335 0.188 1 781 166 166 PRO CB C 32.049 0.234 1 782 167 167 ILE H H 8.113 0.003 1 783 167 167 ILE C C 176.333 0.188 1 784 167 167 ILE CA C 61.229 0.188 1 785 167 167 ILE CB C 38.712 0.234 1 786 167 167 ILE N N 120.214 0.047 1 787 168 168 SER H H 8.275 0.003 1 788 168 168 SER C C 174.253 0.188 1 789 168 168 SER CA C 58.234 0.188 1 790 168 168 SER CB C 63.994 0.234 1 791 168 168 SER N N 119.330 0.047 1 792 169 169 ASN H H 8.465 0.003 1 793 169 169 ASN C C 175.025 0.188 1 794 169 169 ASN CA C 53.305 0.188 1 795 169 169 ASN CB C 38.767 0.234 1 796 169 169 ASN N N 121.085 0.047 1 797 170 170 CYS H H 8.247 0.003 1 798 170 170 CYS C C 174.319 0.188 1 799 170 170 CYS CA C 58.561 0.188 1 800 170 170 CYS CB C 27.858 0.234 1 801 170 170 CYS N N 119.099 0.047 1 802 171 171 LEU H H 8.311 0.003 1 803 171 171 LEU C C 176.715 0.188 1 804 171 171 LEU CA C 55.358 0.188 1 805 171 171 LEU CB C 42.285 0.234 1 806 171 171 LEU N N 124.192 0.047 1 807 172 172 ASN H H 8.319 0.003 1 808 172 172 ASN C C 172.925 0.188 1 809 172 172 ASN CA C 51.293 0.188 1 810 172 172 ASN CB C 38.901 0.234 1 811 172 172 ASN N N 119.788 0.047 1 812 173 173 PRO C C 176.738 0.188 1 813 173 173 PRO CA C 63.339 0.188 1 814 173 173 PRO CB C 32.130 0.234 1 815 174 174 LYS H H 8.326 0.003 1 816 174 174 LYS C C 176.486 0.188 1 817 174 174 LYS CA C 56.210 0.188 1 818 174 174 LYS CB C 33.136 0.234 1 819 174 174 LYS N N 121.445 0.047 1 820 175 175 SER H H 8.373 0.003 1 821 175 175 SER C C 173.341 0.188 1 822 175 175 SER CA C 58.219 0.188 1 823 175 175 SER CB C 64.238 0.234 1 824 175 175 SER N N 118.103 0.047 1 825 176 176 ASP H H 8.031 0.003 1 826 176 176 ASP C C 180.790 0.188 1 827 176 176 ASP CA C 55.795 0.188 1 828 176 176 ASP CB C 42.137 0.234 1 829 176 176 ASP N N 127.957 0.047 1 stop_ save_