data_26300 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata ; _BMRB_accession_number 26300 _BMRB_flat_file_name bmr26300.str _Entry_type original _Submission_date 2020-10-01 _Accession_date 2020-10-05 _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 Kamata Kenichi . . 2 Mizutani Kenji . . 3 Takahashi Katsuya . . 4 Marchetti Roberta . . 5 Silipo Alba . . 6 Addy Christine . . 7 Park Sam-Yong . . 8 Fujii Yuki . . 9 Fujita Hideaki . . 10 Konuma Tsuyoshi . . 11 Ikegami Takahisa . . 12 Ozeki Yasuhiro . . 13 Tame Jeremy R.H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 114 "13C chemical shifts" 351 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-22 original BMRB . stop_ _Original_release_date 2020-10-05 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 33328520 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kamata Kenichi . . 2 Mizutani Kenji . . 3 Takahashi Katsuya . . 4 Marchetti Roberta . . 5 Silipo Alba . . 6 Addy Christine . . 7 Park Sam-Yong . . 8 Fujii Yuki . . 9 Fujita Hideaki . . 10 Konuma Tsuyoshi . . 11 Ikegami Takahisa . . 12 Ozeki Yasuhiro . . 13 Tame Jeremy R.H. . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_name_full 'Scientific reports' _Journal_volume 10 _Journal_issue 1 _Journal_ISSN 2045-2322 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22102 _Page_last 22102 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'SeviL dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $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 132 _Mol_residue_sequence ; GSHMSSVTIGKCYIQNRENG GRAFYNLGRKDLGIFTGKMY DDQIWSFQKSDTPGYYTIGR ESKFLQYNGEQVIMSDIEQD TTLWSLEEVPEDKGFYRLLN KVHKAYLDYNGGDLVANKHQ TESEKWILFKAY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . SER 3 . HIS 4 . MET 5 . SER 6 3 SER 7 4 VAL 8 5 THR 9 6 ILE 10 7 GLY 11 8 LYS 12 9 CYS 13 10 TYR 14 11 ILE 15 12 GLN 16 13 ASN 17 14 ARG 18 15 GLU 19 16 ASN 20 17 GLY 21 18 GLY 22 19 ARG 23 20 ALA 24 21 PHE 25 22 TYR 26 23 ASN 27 24 LEU 28 25 GLY 29 26 ARG 30 27 LYS 31 28 ASP 32 29 LEU 33 30 GLY 34 31 ILE 35 32 PHE 36 33 THR 37 34 GLY 38 35 LYS 39 36 MET 40 37 TYR 41 38 ASP 42 39 ASP 43 40 GLN 44 41 ILE 45 42 TRP 46 43 SER 47 44 PHE 48 45 GLN 49 46 LYS 50 47 SER 51 48 ASP 52 49 THR 53 50 PRO 54 51 GLY 55 52 TYR 56 53 TYR 57 54 THR 58 55 ILE 59 56 GLY 60 57 ARG 61 58 GLU 62 59 SER 63 60 LYS 64 61 PHE 65 62 LEU 66 63 GLN 67 64 TYR 68 65 ASN 69 66 GLY 70 67 GLU 71 68 GLN 72 69 VAL 73 70 ILE 74 71 MET 75 72 SER 76 73 ASP 77 74 ILE 78 75 GLU 79 76 GLN 80 77 ASP 81 78 THR 82 79 THR 83 80 LEU 84 81 TRP 85 82 SER 86 83 LEU 87 84 GLU 88 85 GLU 89 86 VAL 90 87 PRO 91 88 GLU 92 89 ASP 93 90 LYS 94 91 GLY 95 92 PHE 96 93 TYR 97 94 ARG 98 95 LEU 99 96 LEU 100 97 ASN 101 98 LYS 102 99 VAL 103 100 HIS 104 101 LYS 105 102 ALA 106 103 TYR 107 104 LEU 108 105 ASP 109 106 TYR 110 107 ASN 111 108 GLY 112 109 GLY 113 110 ASP 114 111 LEU 115 112 VAL 116 113 ALA 117 114 ASN 118 115 LYS 119 116 HIS 120 117 GLN 121 118 THR 122 119 GLU 123 120 SER 124 121 GLU 125 122 LYS 126 123 TRP 127 124 ILE 128 125 LEU 129 126 PHE 130 127 LYS 131 128 ALA 132 129 TYR 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 . 2547956 Eukaryota Metazoa Mytilisepta virgata 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 pET28 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The protein concentration, 0.36 mM, was estimated as a monomer (corresponding to 0.18 mM as a dimer).' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.36 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 20 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name MagRO _Version . loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AVANCE III' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB-trosy_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB-trosy' _Sample_label $sample_1 save_ save_3D_HNCOCACB-trosy_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCACB-trosy' _Sample_label $sample_1 save_ save_3D_HNCA-trosy_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA-trosy' _Sample_label $sample_1 save_ save_3D_HNCOCA-trosy_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCA-trosy' _Sample_label $sample_1 save_ save_3D_HNCO-trosy_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO-trosy' _Sample_label $sample_1 save_ save_3D_HNCACO-trosy_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO-trosy' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC-trosy_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC-trosy' _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' 0.07 . M pH 6.8 . 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 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 1.000000000 DSS N 15 'methyl protons' ppm 0 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 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_ _Software_label $software_1 stop_ loop_ _Experiment_label '3D HNCACB-trosy' '3D HNCOCACB-trosy' '3D HNCA-trosy' '3D HNCOCA-trosy' '3D HNCO-trosy' '3D HNCACO-trosy' '2D 1H-15N HSQC-trosy' 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 'subunit 1' _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 6 SER C C 174.266 0.100 1 2 3 6 SER CA C 58.146 0.300 1 3 3 6 SER CB C 63.491 0.300 1 4 4 7 VAL H H 7.722 0.020 1 5 4 7 VAL C C 175.719 0.100 1 6 4 7 VAL CA C 61.746 0.300 1 7 4 7 VAL CB C 32.162 0.300 1 8 4 7 VAL N N 122.678 0.150 1 9 5 8 THR H H 8.029 0.020 1 10 5 8 THR C C 172.560 0.100 1 11 5 8 THR CA C 62.475 0.300 1 12 5 8 THR CB C 69.228 0.300 1 13 5 8 THR N N 122.822 0.150 1 14 6 9 ILE H H 7.700 0.020 1 15 6 9 ILE C C 176.023 0.100 1 16 6 9 ILE CA C 59.454 0.300 1 17 6 9 ILE CB C 38.339 0.300 1 18 6 9 ILE N N 123.264 0.150 1 19 7 10 GLY H H 8.789 0.020 1 20 7 10 GLY C C 173.686 0.100 1 21 7 10 GLY CA C 44.206 0.300 1 22 7 10 GLY N N 114.042 0.150 1 23 8 11 LYS H H 8.194 0.020 1 24 8 11 LYS C C 177.890 0.100 1 25 8 11 LYS CA C 54.385 0.300 1 26 8 11 LYS CB C 31.208 0.300 1 27 8 11 LYS N N 123.711 0.150 1 28 9 12 CYS H H 9.602 0.020 1 29 9 12 CYS C C 172.617 0.100 1 30 9 12 CYS CA C 56.129 0.300 1 31 9 12 CYS CB C 31.930 0.300 1 32 9 12 CYS N N 122.249 0.150 1 33 10 13 TYR H H 8.118 0.020 1 34 10 13 TYR C C 174.684 0.100 1 35 10 13 TYR CA C 56.737 0.300 1 36 10 13 TYR CB C 39.646 0.300 1 37 10 13 TYR N N 119.502 0.150 1 38 11 14 ILE H H 9.964 0.020 1 39 11 14 ILE C C 173.957 0.100 1 40 11 14 ILE CA C 61.502 0.300 1 41 11 14 ILE CB C 37.787 0.300 1 42 11 14 ILE N N 122.314 0.150 1 43 12 15 GLN H H 9.031 0.020 1 44 12 15 GLN C C 173.900 0.100 1 45 12 15 GLN CA C 53.614 0.300 1 46 12 15 GLN CB C 33.066 0.300 1 47 12 15 GLN N N 126.526 0.150 1 48 13 16 ASN H H 9.660 0.020 1 49 13 16 ASN C C 175.842 0.100 1 50 13 16 ASN CA C 54.000 0.300 1 51 13 16 ASN CB C 41.755 0.300 1 52 13 16 ASN N N 128.973 0.150 1 53 14 17 ARG H H 8.648 0.020 1 54 14 17 ARG C C 176.509 0.100 1 55 14 17 ARG CA C 58.907 0.300 1 56 14 17 ARG CB C 30.454 0.300 1 57 14 17 ARG N N 127.599 0.150 1 58 15 18 GLU H H 8.573 0.020 1 59 15 18 GLU C C 177.365 0.100 1 60 15 18 GLU CA C 57.681 0.300 1 61 15 18 GLU CB C 28.680 0.300 1 62 15 18 GLU N N 115.876 0.150 1 63 20 23 ALA C C 178.509 0.100 1 64 20 23 ALA CA C 51.499 0.300 1 65 20 23 ALA CB C 16.552 0.300 1 66 21 24 PHE H H 9.545 0.020 1 67 21 24 PHE C C 172.023 0.100 1 68 21 24 PHE CA C 56.392 0.300 1 69 21 24 PHE CB C 43.613 0.300 1 70 21 24 PHE N N 124.208 0.150 1 71 22 25 TYR H H 7.449 0.020 1 72 22 25 TYR C C 173.226 0.100 1 73 22 25 TYR CA C 56.160 0.300 1 74 22 25 TYR CB C 40.449 0.300 1 75 22 25 TYR N N 116.357 0.150 1 76 23 26 ASN H H 8.987 0.020 1 77 23 26 ASN C C 173.745 0.100 1 78 23 26 ASN CA C 51.850 0.300 1 79 23 26 ASN CB C 40.574 0.300 1 80 23 26 ASN N N 130.634 0.150 1 81 24 27 LEU H H 8.856 0.020 1 82 24 27 LEU C C 179.045 0.100 1 83 24 27 LEU CA C 57.670 0.300 1 84 24 27 LEU CB C 41.504 0.300 1 85 24 27 LEU N N 129.865 0.150 1 86 25 28 GLY H H 8.113 0.020 1 87 25 28 GLY C C 175.554 0.100 1 88 25 28 GLY CA C 46.700 0.300 1 89 25 28 GLY N N 108.077 0.150 1 90 26 29 ARG H H 7.513 0.020 1 91 26 29 ARG C C 175.016 0.100 1 92 26 29 ARG CA C 55.399 0.300 1 93 26 29 ARG CB C 31.057 0.300 1 94 26 29 ARG N N 116.991 0.150 1 95 27 30 LYS H H 7.766 0.020 1 96 27 30 LYS C C 175.198 0.100 1 97 27 30 LYS CA C 56.818 0.300 1 98 27 30 LYS CB C 28.697 0.300 1 99 27 30 LYS N N 120.393 0.150 1 100 28 31 ASP H H 7.463 0.020 1 101 28 31 ASP C C 172.114 0.100 1 102 28 31 ASP CA C 52.925 0.300 1 103 28 31 ASP CB C 44.316 0.300 1 104 28 31 ASP N N 119.098 0.150 1 105 29 32 LEU H H 8.167 0.020 1 106 29 32 LEU C C 176.185 0.100 1 107 29 32 LEU CA C 52.641 0.300 1 108 29 32 LEU CB C 45.823 0.300 1 109 29 32 LEU N N 128.250 0.150 1 110 30 33 GLY H H 7.308 0.020 1 111 30 33 GLY C C 170.070 0.100 1 112 30 33 GLY CA C 46.720 0.300 1 113 30 33 GLY N N 113.864 0.150 1 114 31 34 ILE H H 8.215 0.020 1 115 31 34 ILE C C 172.874 0.100 1 116 31 34 ILE CA C 58.278 0.300 1 117 31 34 ILE CB C 40.901 0.300 1 118 31 34 ILE N N 120.117 0.150 1 119 32 35 PHE H H 9.155 0.020 1 120 32 35 PHE CA C 56.910 0.300 1 121 32 35 PHE CB C 42.634 0.300 1 122 32 35 PHE N N 130.518 0.150 1 123 34 37 GLY C C 171.719 0.100 1 124 34 37 GLY CA C 43.636 0.300 1 125 35 38 LYS H H 8.086 0.020 1 126 35 38 LYS C C 174.684 0.100 1 127 35 38 LYS CA C 56.494 0.300 1 128 35 38 LYS CB C 32.865 0.300 1 129 35 38 LYS N N 127.005 0.150 1 130 36 39 MET H H 8.127 0.020 1 131 36 39 MET C C 173.769 0.100 1 132 36 39 MET CA C 54.993 0.300 1 133 36 39 MET N N 122.376 0.150 1 134 37 40 TYR H H 6.669 0.020 1 135 37 40 TYR C C 176.936 0.100 1 136 37 40 TYR CA C 56.717 0.300 1 137 37 40 TYR CB C 41.353 0.300 1 138 37 40 TYR N N 120.032 0.150 1 139 38 41 ASP H H 8.450 0.020 1 140 38 41 ASP C C 177.216 0.100 1 141 38 41 ASP CA C 56.068 0.300 1 142 38 41 ASP CB C 39.897 0.300 1 143 38 41 ASP N N 119.305 0.150 1 144 39 42 ASP H H 7.192 0.020 1 145 39 42 ASP C C 175.208 0.100 1 146 39 42 ASP CA C 53.858 0.300 1 147 39 42 ASP CB C 37.938 0.300 1 148 39 42 ASP N N 118.813 0.150 1 149 40 43 GLN H H 7.451 0.020 1 150 40 43 GLN C C 175.041 0.100 1 151 40 43 GLN CA C 53.553 0.300 1 152 40 43 GLN CB C 26.888 0.300 1 153 40 43 GLN N N 114.815 0.150 1 154 41 44 ILE H H 6.991 0.020 1 155 41 44 ILE C C 176.210 0.100 1 156 41 44 ILE CA C 61.340 0.300 1 157 41 44 ILE CB C 37.084 0.300 1 158 41 44 ILE N N 119.776 0.150 1 159 42 45 TRP H H 9.666 0.020 1 160 42 45 TRP C C 175.124 0.100 1 161 42 45 TRP CA C 55.946 0.300 1 162 42 45 TRP CB C 30.705 0.300 1 163 42 45 TRP N N 133.098 0.150 1 164 43 46 SER H H 9.682 0.020 1 165 43 46 SER C C 173.817 0.100 1 166 43 46 SER CA C 57.163 0.300 1 167 43 46 SER CB C 63.050 0.300 1 168 43 46 SER N N 115.782 0.150 1 169 44 47 PHE H H 9.094 0.020 1 170 44 47 PHE C C 174.933 0.100 1 171 44 47 PHE CA C 56.930 0.300 1 172 44 47 PHE CB C 40.750 0.300 1 173 44 47 PHE N N 135.288 0.150 1 174 45 48 GLN H H 8.345 0.020 1 175 45 48 GLN C C 175.196 0.100 1 176 45 48 GLN CA C 53.310 0.300 1 177 45 48 GLN CB C 31.760 0.300 1 178 45 48 GLN N N 123.648 0.150 1 179 46 49 LYS H H 8.497 0.020 1 180 46 49 LYS C C 176.982 0.100 1 181 46 49 LYS CA C 57.548 0.300 1 182 46 49 LYS CB C 31.629 0.300 1 183 46 49 LYS N N 121.525 0.150 1 184 47 50 SER H H 8.057 0.020 1 185 47 50 SER C C 173.831 0.100 1 186 47 50 SER CA C 57.163 0.300 1 187 47 50 SER CB C 65.110 0.300 1 188 47 50 SER N N 120.540 0.150 1 189 48 51 ASP H H 8.600 0.020 1 190 48 51 ASP C C 176.691 0.100 1 191 48 51 ASP CA C 55.419 0.300 1 192 48 51 ASP CB C 40.048 0.300 1 193 48 51 ASP N N 120.887 0.150 1 194 49 52 THR H H 8.544 0.020 1 195 49 52 THR C C 172.004 0.100 1 196 49 52 THR CA C 59.832 0.300 1 197 49 52 THR CB C 69.236 0.300 1 198 49 52 THR N N 120.317 0.150 1 199 51 54 GLY C C 173.229 0.100 1 200 51 54 GLY CA C 44.325 0.300 1 201 52 55 TYR H H 7.333 0.020 1 202 52 55 TYR C C 175.336 0.100 1 203 52 55 TYR CA C 57.102 0.300 1 204 52 55 TYR CB C 42.056 0.300 1 205 52 55 TYR N N 116.282 0.150 1 206 53 56 TYR H H 9.763 0.020 1 207 53 56 TYR C C 175.184 0.100 1 208 53 56 TYR CA C 57.295 0.300 1 209 53 56 TYR CB C 42.283 0.300 1 210 53 56 TYR N N 124.801 0.150 1 211 54 57 THR H H 8.916 0.020 1 212 54 57 THR C C 173.231 0.100 1 213 54 57 THR CA C 59.576 0.300 1 214 54 57 THR CB C 71.237 0.300 1 215 54 57 THR N N 109.938 0.150 1 216 55 58 ILE H H 9.858 0.020 1 217 55 58 ILE C C 175.597 0.100 1 218 55 58 ILE CA C 61.158 0.300 1 219 55 58 ILE CB C 38.865 0.300 1 220 55 58 ILE N N 123.358 0.150 1 221 56 59 GLY H H 8.959 0.020 1 222 56 59 GLY C C 173.248 0.100 1 223 56 59 GLY CA C 45.139 0.300 1 224 56 59 GLY N N 112.946 0.150 1 225 57 60 ARG H H 7.605 0.020 1 226 57 60 ARG C C 175.525 0.100 1 227 57 60 ARG CA C 57.143 0.300 1 228 57 60 ARG CB C 34.573 0.300 1 229 57 60 ARG N N 119.213 0.150 1 230 58 61 GLU H H 8.966 0.020 1 231 58 61 GLU C C 175.458 0.100 1 232 58 61 GLU CA C 56.068 0.300 1 233 58 61 GLU CB C 25.332 0.300 1 234 58 61 GLU N N 116.335 0.150 1 235 59 62 SER H H 8.169 0.020 1 236 59 62 SER C C 172.530 0.100 1 237 59 62 SER CA C 59.596 0.300 1 238 59 62 SER CB C 61.694 0.300 1 239 59 62 SER N N 107.681 0.150 1 240 60 63 LYS H H 7.620 0.020 1 241 60 63 LYS C C 175.843 0.100 1 242 60 63 LYS CA C 53.858 0.300 1 243 60 63 LYS CB C 36.431 0.300 1 244 60 63 LYS N N 119.937 0.150 1 245 61 64 PHE H H 9.140 0.020 1 246 61 64 PHE C C 175.925 0.100 1 247 61 64 PHE CA C 56.940 0.300 1 248 61 64 PHE CB C 42.157 0.300 1 249 61 64 PHE N N 118.261 0.150 1 250 62 65 LEU H H 9.387 0.020 1 251 62 65 LEU C C 177.094 0.100 1 252 62 65 LEU CA C 57.041 0.300 1 253 62 65 LEU CB C 42.609 0.300 1 254 62 65 LEU N N 126.977 0.150 1 255 63 66 GLN H H 9.656 0.020 1 256 63 66 GLN C C 173.691 0.100 1 257 63 66 GLN CA C 53.858 0.300 1 258 63 66 GLN CB C 32.734 0.300 1 259 63 66 GLN N N 130.787 0.150 1 260 64 67 TYR H H 6.969 0.020 1 261 64 67 TYR C C 173.909 0.100 1 262 64 67 TYR CA C 55.946 0.300 1 263 64 67 TYR CB C 40.248 0.300 1 264 64 67 TYR N N 121.226 0.150 1 265 65 68 ASN H H 7.348 0.020 1 266 65 68 ASN C C 175.084 0.100 1 267 65 68 ASN CA C 51.147 0.300 1 268 65 68 ASN CB C 38.217 0.300 1 269 65 68 ASN N N 123.303 0.150 1 270 66 69 GLY C C 171.920 0.100 1 271 66 69 GLY CA C 44.042 0.300 1 272 67 70 GLU H H 7.512 0.020 1 273 67 70 GLU C C 175.324 0.100 1 274 67 70 GLU CA C 57.163 0.300 1 275 67 70 GLU CB C 31.961 0.300 1 276 67 70 GLU N N 118.374 0.150 1 277 68 71 GLN H H 8.666 0.020 1 278 68 71 GLN C C 174.231 0.100 1 279 68 71 GLN CA C 54.243 0.300 1 280 68 71 GLN CB C 32.734 0.300 1 281 68 71 GLN N N 119.242 0.150 1 282 69 72 VAL H H 8.674 0.020 1 283 69 72 VAL C C 174.784 0.100 1 284 69 72 VAL CA C 62.050 0.300 1 285 69 72 VAL CB C 30.203 0.300 1 286 69 72 VAL N N 124.924 0.150 1 287 70 73 ILE H H 8.543 0.020 1 288 70 73 ILE C C 173.802 0.100 1 289 70 73 ILE CA C 59.434 0.300 1 290 70 73 ILE CB C 42.458 0.300 1 291 70 73 ILE N N 123.642 0.150 1 292 71 74 MET H H 7.990 0.020 1 293 71 74 MET C C 176.868 0.100 1 294 71 74 MET CA C 52.215 0.300 1 295 71 74 MET CB C 31.660 0.300 1 296 71 74 MET N N 117.441 0.150 1 297 72 75 SER H H 9.433 0.020 1 298 72 75 SER C C 175.597 0.100 1 299 72 75 SER CA C 55.561 0.300 1 300 72 75 SER CB C 64.356 0.300 1 301 72 75 SER N N 118.108 0.150 1 302 73 76 ASP H H 8.953 0.020 1 303 73 76 ASP C C 175.164 0.100 1 304 73 76 ASP CA C 56.109 0.300 1 305 73 76 ASP CB C 40.951 0.300 1 306 73 76 ASP N N 126.841 0.150 1 307 74 77 ILE H H 7.587 0.020 1 308 74 77 ILE C C 175.742 0.100 1 309 74 77 ILE CA C 59.049 0.300 1 310 74 77 ILE CB C 40.976 0.300 1 311 74 77 ILE N N 112.763 0.150 1 312 75 78 GLU H H 8.507 0.020 1 313 75 78 GLU C C 175.215 0.100 1 314 75 78 GLU CA C 56.352 0.300 1 315 75 78 GLU CB C 28.194 0.300 1 316 75 78 GLU N N 127.657 0.150 1 317 76 79 GLN H H 7.554 0.020 1 318 76 79 GLN C C 176.738 0.100 1 319 76 79 GLN CA C 54.069 0.300 1 320 76 79 GLN CB C 31.190 0.300 1 321 76 79 GLN N N 121.596 0.150 1 322 77 80 ASP C C 178.221 0.100 1 323 77 80 ASP CA C 58.065 0.300 1 324 77 80 ASP CB C 38.664 0.300 1 325 78 81 THR H H 7.640 0.020 1 326 78 81 THR C C 176.125 0.100 1 327 78 81 THR CA C 63.307 0.300 1 328 78 81 THR CB C 68.475 0.300 1 329 78 81 THR N N 107.032 0.150 1 330 79 82 THR H H 8.044 0.020 1 331 79 82 THR C C 173.017 0.100 1 332 79 82 THR CA C 60.975 0.300 1 333 79 82 THR CB C 68.718 0.300 1 334 79 82 THR N N 112.974 0.150 1 335 80 83 LEU H H 6.842 0.020 1 336 80 83 LEU C C 176.581 0.100 1 337 80 83 LEU CA C 54.507 0.300 1 338 80 83 LEU CB C 41.780 0.300 1 339 80 83 LEU N N 122.832 0.150 1 340 81 84 TRP H H 9.360 0.020 1 341 81 84 TRP C C 175.682 0.100 1 342 81 84 TRP CA C 55.216 0.300 1 343 81 84 TRP CB C 31.358 0.300 1 344 81 84 TRP N N 123.312 0.150 1 345 82 85 SER H H 9.912 0.020 1 346 82 85 SER C C 173.438 0.100 1 347 82 85 SER CA C 56.007 0.300 1 348 82 85 SER CB C 64.707 0.300 1 349 82 85 SER N N 119.264 0.150 1 350 83 86 LEU H H 8.464 0.020 1 351 83 86 LEU C C 176.895 0.100 1 352 83 86 LEU CA C 53.716 0.300 1 353 83 86 LEU CB C 42.960 0.300 1 354 83 86 LEU N N 122.171 0.150 1 355 84 87 GLU H H 9.424 0.020 1 356 84 87 GLU C C 175.742 0.100 1 357 84 87 GLU CA C 54.284 0.300 1 358 84 87 GLU CB C 32.062 0.300 1 359 84 87 GLU N N 126.344 0.150 1 360 85 88 GLU H H 9.084 0.020 1 361 85 88 GLU C C 176.130 0.100 1 362 85 88 GLU CA C 57.548 0.300 1 363 85 88 GLU CB C 29.500 0.300 1 364 85 88 GLU N N 127.574 0.150 1 365 86 89 VAL H H 7.690 0.020 1 366 86 89 VAL C C 174.770 0.100 1 367 86 89 VAL CA C 59.142 0.300 1 368 86 89 VAL CB C 30.688 0.300 1 369 86 89 VAL N N 125.716 0.150 1 370 87 90 PRO C C 178.491 0.100 1 371 87 90 PRO CA C 65.076 0.300 1 372 87 90 PRO CB C 31.327 0.300 1 373 88 91 GLU H H 9.358 0.020 1 374 88 91 GLU C C 175.462 0.100 1 375 88 91 GLU CA C 57.589 0.300 1 376 88 91 GLU CB C 27.642 0.300 1 377 88 91 GLU N N 114.967 0.150 1 378 89 92 ASP H H 6.986 0.020 1 379 89 92 ASP C C 173.153 0.100 1 380 89 92 ASP CA C 52.763 0.300 1 381 89 92 ASP CB C 42.609 0.300 1 382 89 92 ASP N N 121.955 0.150 1 383 90 93 LYS H H 8.130 0.020 1 384 90 93 LYS C C 177.446 0.100 1 385 90 93 LYS CA C 57.974 0.300 1 386 90 93 LYS CB C 31.308 0.300 1 387 90 93 LYS N N 123.350 0.150 1 388 91 94 GLY H H 8.228 0.020 1 389 91 94 GLY C C 172.697 0.100 1 390 91 94 GLY CA C 44.773 0.300 1 391 91 94 GLY N N 111.771 0.150 1 392 92 95 PHE H H 7.579 0.020 1 393 92 95 PHE C C 174.977 0.100 1 394 92 95 PHE CA C 57.001 0.300 1 395 92 95 PHE CB C 40.449 0.300 1 396 92 95 PHE N N 115.758 0.150 1 397 93 96 TYR H H 9.965 0.020 1 398 93 96 TYR C C 176.068 0.100 1 399 93 96 TYR CA C 57.690 0.300 1 400 93 96 TYR CB C 43.413 0.300 1 401 93 96 TYR N N 118.572 0.150 1 402 94 97 ARG H H 9.222 0.020 1 403 94 97 ARG C C 175.782 0.100 1 404 94 97 ARG CA C 54.811 0.300 1 405 94 97 ARG CB C 32.564 0.300 1 406 94 97 ARG N N 117.765 0.150 1 407 95 98 LEU H H 10.040 0.020 1 408 95 98 LEU C C 175.198 0.100 1 409 95 98 LEU CA C 53.817 0.300 1 410 95 98 LEU CB C 43.161 0.300 1 411 95 98 LEU N N 125.732 0.150 1 412 96 99 LEU H H 9.238 0.020 1 413 96 99 LEU C C 176.424 0.100 1 414 96 99 LEU CA C 53.189 0.300 1 415 96 99 LEU CB C 43.489 0.300 1 416 96 99 LEU N N 127.144 0.150 1 417 97 100 ASN H H 9.021 0.020 1 418 97 100 ASN C C 175.206 0.100 1 419 97 100 ASN CA C 55.034 0.300 1 420 97 100 ASN CB C 41.454 0.300 1 421 97 100 ASN N N 129.470 0.150 1 422 98 101 LYS H H 8.054 0.020 1 423 98 101 LYS C C 176.891 0.100 1 424 98 101 LYS CA C 59.718 0.300 1 425 98 101 LYS CB C 33.217 0.300 1 426 98 101 LYS N N 128.686 0.150 1 427 99 102 VAL H H 7.440 0.020 1 428 99 102 VAL C C 177.539 0.100 1 429 99 102 VAL CA C 65.051 0.300 1 430 99 102 VAL CB C 32.262 0.300 1 431 99 102 VAL N N 116.414 0.150 1 432 100 103 HIS H H 7.781 0.020 1 433 100 103 HIS C C 174.657 0.100 1 434 100 103 HIS CA C 56.413 0.300 1 435 100 103 HIS CB C 31.830 0.300 1 436 100 103 HIS N N 114.859 0.150 1 437 101 104 LYS H H 7.783 0.020 1 438 101 104 LYS C C 172.877 0.100 1 439 101 104 LYS CA C 56.048 0.300 1 440 101 104 LYS CB C 27.893 0.300 1 441 101 104 LYS N N 117.443 0.150 1 442 102 105 ALA H H 6.044 0.020 1 443 102 105 ALA C C 174.897 0.100 1 444 102 105 ALA CA C 48.789 0.300 1 445 102 105 ALA CB C 22.569 0.300 1 446 102 105 ALA N N 117.532 0.150 1 447 103 106 TYR H H 8.931 0.020 1 448 103 106 TYR C C 177.294 0.100 1 449 103 106 TYR CA C 56.392 0.300 1 450 103 106 TYR CB C 38.691 0.300 1 451 103 106 TYR N N 123.603 0.150 1 452 104 107 LEU H H 8.854 0.020 1 453 104 107 LEU C C 175.782 0.100 1 454 104 107 LEU CA C 56.322 0.300 1 455 104 107 LEU CB C 41.755 0.300 1 456 104 107 LEU N N 123.604 0.150 1 457 105 108 ASP H H 9.483 0.020 1 458 105 108 ASP C C 173.829 0.100 1 459 105 108 ASP CA C 52.033 0.300 1 460 105 108 ASP CB C 44.919 0.300 1 461 105 108 ASP N N 135.226 0.150 1 462 106 109 TYR H H 9.465 0.020 1 463 106 109 TYR C C 174.119 0.100 1 464 106 109 TYR CA C 56.656 0.300 1 465 106 109 TYR CB C 42.056 0.300 1 466 106 109 TYR N N 117.335 0.150 1 467 107 110 ASN H H 8.849 0.020 1 468 107 110 ASN C C 175.435 0.100 1 469 107 110 ASN CA C 52.986 0.300 1 470 107 110 ASN CB C 40.499 0.300 1 471 107 110 ASN N N 120.296 0.150 1 472 108 111 GLY H H 9.173 0.020 1 473 108 111 GLY C C 174.285 0.100 1 474 108 111 GLY CA C 47.126 0.300 1 475 108 111 GLY N N 118.841 0.150 1 476 109 112 GLY H H 8.674 0.020 1 477 109 112 GLY C C 174.500 0.100 1 478 109 112 GLY CA C 45.382 0.300 1 479 109 112 GLY N N 115.434 0.150 1 480 110 113 ASP H H 8.153 0.020 1 481 110 113 ASP C C 176.729 0.100 1 482 110 113 ASP CA C 53.533 0.300 1 483 110 113 ASP CB C 42.006 0.300 1 484 110 113 ASP N N 121.304 0.150 1 485 111 114 LEU H H 9.045 0.020 1 486 111 114 LEU C C 176.552 0.100 1 487 111 114 LEU CA C 53.878 0.300 1 488 111 114 LEU CB C 41.554 0.300 1 489 111 114 LEU N N 120.208 0.150 1 490 112 115 VAL H H 8.214 0.020 1 491 112 115 VAL C C 172.875 0.100 1 492 112 115 VAL CA C 58.887 0.300 1 493 112 115 VAL CB C 34.824 0.300 1 494 112 115 VAL N N 116.317 0.150 1 495 113 116 ALA H H 7.903 0.020 1 496 113 116 ALA C C 175.788 0.100 1 497 113 116 ALA CA C 50.512 0.300 1 498 113 116 ALA CB C 18.802 0.300 1 499 113 116 ALA N N 120.750 0.150 1 500 114 117 ASN H H 8.659 0.020 1 501 114 117 ASN C C 175.587 0.100 1 502 114 117 ASN CA C 51.526 0.300 1 503 114 117 ASN CB C 42.056 0.300 1 504 114 117 ASN N N 120.206 0.150 1 505 115 118 LYS H H 9.119 0.020 1 506 115 118 LYS C C 176.906 0.100 1 507 115 118 LYS CA C 58.359 0.300 1 508 115 118 LYS CB C 32.062 0.300 1 509 115 118 LYS N N 123.795 0.150 1 510 116 119 HIS H H 7.866 0.020 1 511 116 119 HIS C C 174.801 0.100 1 512 116 119 HIS CA C 54.203 0.300 1 513 116 119 HIS CB C 30.705 0.300 1 514 116 119 HIS N N 116.712 0.150 1 515 117 120 GLN H H 8.770 0.020 1 516 117 120 GLN C C 176.179 0.100 1 517 117 120 GLN CA C 55.845 0.300 1 518 117 120 GLN CB C 27.993 0.300 1 519 117 120 GLN N N 121.275 0.150 1 520 118 121 THR H H 6.972 0.020 1 521 118 121 THR C C 176.455 0.100 1 522 118 121 THR CA C 59.110 0.300 1 523 118 121 THR CB C 71.689 0.300 1 524 118 121 THR N N 112.217 0.150 1 525 119 122 GLU H H 8.825 0.020 1 526 119 122 GLU C C 177.731 0.100 1 527 119 122 GLU CA C 57.832 0.300 1 528 119 122 GLU CB C 29.048 0.300 1 529 119 122 GLU N N 120.297 0.150 1 530 120 123 SER H H 7.456 0.020 1 531 120 123 SER C C 172.902 0.100 1 532 120 123 SER CA C 58.136 0.300 1 533 120 123 SER CB C 60.740 0.300 1 534 120 123 SER N N 110.465 0.150 1 535 121 124 GLU H H 6.125 0.020 1 536 121 124 GLU C C 174.676 0.100 1 537 121 124 GLU CA C 53.675 0.300 1 538 121 124 GLU CB C 29.149 0.300 1 539 121 124 GLU N N 117.449 0.150 1 540 122 125 LYS H H 6.776 0.020 1 541 122 125 LYS C C 173.088 0.100 1 542 122 125 LYS CA C 56.535 0.300 1 543 122 125 LYS CB C 32.765 0.300 1 544 122 125 LYS N N 120.172 0.150 1 545 123 126 TRP H H 9.405 0.020 1 546 123 126 TRP C C 174.784 0.100 1 547 123 126 TRP CA C 55.257 0.300 1 548 123 126 TRP CB C 41.228 0.300 1 549 123 126 TRP N N 124.683 0.150 1 550 124 127 ILE H H 10.209 0.020 1 551 124 127 ILE C C 172.591 0.100 1 552 124 127 ILE CA C 59.454 0.300 1 553 124 127 ILE CB C 40.172 0.300 1 554 124 127 ILE N N 122.562 0.150 1 555 125 128 LEU H H 7.901 0.020 1 556 125 128 LEU C C 176.909 0.100 1 557 125 128 LEU CA C 53.736 0.300 1 558 125 128 LEU CB C 41.253 0.300 1 559 125 128 LEU N N 128.653 0.150 1 560 126 129 PHE H H 7.838 0.020 1 561 126 129 PHE C C 173.726 0.100 1 562 126 129 PHE CA C 53.614 0.300 1 563 126 129 PHE CB C 41.454 0.300 1 564 126 129 PHE N N 117.661 0.150 1 565 127 130 LYS H H 8.487 0.020 1 566 127 130 LYS C C 175.861 0.100 1 567 127 130 LYS CA C 56.636 0.300 1 568 127 130 LYS CB C 32.363 0.300 1 569 127 130 LYS N N 122.882 0.150 1 570 128 131 ALA H H 8.050 0.020 1 571 128 131 ALA C C 176.122 0.100 1 572 128 131 ALA CA C 52.864 0.300 1 573 128 131 ALA CB C 19.706 0.300 1 574 128 131 ALA N N 127.469 0.150 1 575 129 132 TYR H H 7.107 0.020 1 576 129 132 TYR C C 179.760 0.100 1 577 129 132 TYR CA C 57.275 0.300 1 578 129 132 TYR CB C 37.112 0.300 1 579 129 132 TYR N N 116.390 0.150 1 stop_ save_