data_27574 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; human TGF-b2 ; _BMRB_accession_number 27574 _BMRB_flat_file_name bmr27574.str _Entry_type original _Submission_date 2018-08-11 _Accession_date 2018-08-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone and partial side chain assignments for human TGFb2' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Henen Morkos . . 2 Mahlawat Pardeep . . 3 Ilangovan Udayar . . 4 Hinck Andrew . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 403 "13C chemical shifts" 383 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-22 update BMRB 'update entry citation' 2019-01-02 original author 'original release' stop_ _Original_release_date 2018-08-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; TGF-b2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-b and Inhibin-a ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30598510 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Henen Morkos . . 2 Mahlawat Pardeep . . 3 Zwieb Christian . . 4 Kodali Ravi S. . 5 Hanna Ramsey . . 6 Krzysiak Troy C. . 7 Ilangovan Udayar . . 8 Cano Kristin E. . 9 Hinck Garrett . . 10 Vonberg Morkos . . 11 McCabe Megan . . 12 Hinck Andrew P. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 294 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3065 _Page_last 3080 _Year 2019 _Details . loop_ _Keyword 'ILV methyl labeling' 'cardiac development' 'cell signaling' 'cell surface receptor' endocrinology 'nuclear magnetic resonance (NMR)' 'transforming growth factor beta (TGF-b)' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TGF-b2 homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TGF-b2, chain 1' $TGF-b2 'TGF-b2, chain 2' $TGF-b2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Binds TGF-b receptors, TbRI and TbRII' 'Cell signaling' stop_ _Database_query_date . _Details ; TGF-b2 homodimer is formed by formation a single disulfide bond between Cys77 in each of the two component monomers. ; save_ ######################## # Monomeric polymers # ######################## save_TGF-b2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TGF-b2 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function Cytokine 'Growth Factor' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; ALDAAYCFRNVQDNCCLRPL YIDFKRDLGWKWIHEPKGYN ANFCAGACPYLWSSDTQHSK VLSLYNTINPEASASPCCVS QDLEPLTILYYIGKTPKIEQ LSNMIVKSCKCS ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LEU 3 ASP 4 ALA 5 ALA 6 TYR 7 CYS 8 PHE 9 ARG 10 ASN 11 VAL 12 GLN 13 ASP 14 ASN 15 CYS 16 CYS 17 LEU 18 ARG 19 PRO 20 LEU 21 TYR 22 ILE 23 ASP 24 PHE 25 LYS 26 ARG 27 ASP 28 LEU 29 GLY 30 TRP 31 LYS 32 TRP 33 ILE 34 HIS 35 GLU 36 PRO 37 LYS 38 GLY 39 TYR 40 ASN 41 ALA 42 ASN 43 PHE 44 CYS 45 ALA 46 GLY 47 ALA 48 CYS 49 PRO 50 TYR 51 LEU 52 TRP 53 SER 54 SER 55 ASP 56 THR 57 GLN 58 HIS 59 SER 60 LYS 61 VAL 62 LEU 63 SER 64 LEU 65 TYR 66 ASN 67 THR 68 ILE 69 ASN 70 PRO 71 GLU 72 ALA 73 SER 74 ALA 75 SER 76 PRO 77 CYS 78 CYS 79 VAL 80 SER 81 GLN 82 ASP 83 LEU 84 GLU 85 PRO 86 LEU 87 THR 88 ILE 89 LEU 90 TYR 91 TYR 92 ILE 93 GLY 94 LYS 95 THR 96 PRO 97 LYS 98 ILE 99 GLU 100 GLN 101 LEU 102 SER 103 ASN 104 MET 105 ILE 106 VAL 107 LYS 108 SER 109 CYS 110 LYS 111 CYS 112 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value NCBI NP_003229.1 'transforming growth factor beta-2 isoform 2 preproprotein [Homo sapiens]' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TGF-b2 Human 9606 Eukaryota Metazoa Homo sapiens 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 $TGF-b2 'recombinant technology' . Escherichia coli . pET32a 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 $TGF-b2 0.25 mM 0.2 0.3 '[U-98% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version J loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'Equipped with 5 mm TCI cryoprobe' 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_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_C(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _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 . M pH 2.7 . pH pressure 1 . atm temperature 310 . 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 . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView $NMRPipe stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HNCACO' '3D HNCA' '3D HN(CO)CA' '3D H(CCO)NH' '3D HCCH-TOCSY' '3D C(CO)NH' '2D 1H-13C HSQC aliphatic' 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 'TGF-b2, chain 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 1 1 ALA HA H 4.013 0.01 1 2 1 1 ALA HB H 1.446 0.01 1 3 1 1 ALA C C 173.406 0.2 1 4 1 1 ALA CA C 51.612 0.2 1 5 1 1 ALA CB C 19.410 0.2 1 6 2 2 LEU H H 8.605 0.01 1 7 2 2 LEU HA H 4.594 0.01 1 8 2 2 LEU HB2 H 1.955 0.01 2 9 2 2 LEU HB3 H 1.191 0.01 2 10 2 2 LEU HG H 1.533 0.01 1 11 2 2 LEU HD1 H 0.733 0.01 2 12 2 2 LEU HD2 H 0.803 0.01 2 13 2 2 LEU C C 175.279 0.2 1 14 2 2 LEU CA C 53.686 0.2 1 15 2 2 LEU CB C 40.322 0.2 1 16 2 2 LEU CG C 26.784 0.2 1 17 2 2 LEU CD1 C 24.765 0.2 2 18 2 2 LEU CD2 C 22.909 0.2 2 19 2 2 LEU N N 121.220 0.3 1 20 3 3 ASP H H 7.888 0.01 1 21 3 3 ASP HA H 4.814 0.01 1 22 3 3 ASP HB2 H 3.044 0.01 2 23 3 3 ASP HB3 H 2.516 0.01 2 24 3 3 ASP C C 175.773 0.2 1 25 3 3 ASP CA C 51.720 0.2 1 26 3 3 ASP CB C 41.924 0.2 1 27 3 3 ASP N N 121.201 0.3 1 28 4 4 ALA H H 8.418 0.01 1 29 4 4 ALA HA H 3.109 0.01 1 30 4 4 ALA HB H 0.879 0.01 1 31 4 4 ALA C C 178.554 0.2 1 32 4 4 ALA CA C 54.869 0.2 1 33 4 4 ALA CB C 18.800 0.2 1 34 4 4 ALA N N 123.358 0.3 1 35 5 5 ALA H H 7.714 0.01 1 36 5 5 ALA HA H 3.967 0.01 1 37 5 5 ALA HB H 1.348 0.01 1 38 5 5 ALA C C 178.709 0.2 1 39 5 5 ALA CA C 54.109 0.2 1 40 5 5 ALA CB C 18.268 0.2 1 41 5 5 ALA N N 119.903 0.3 1 42 6 6 TYR H H 7.603 0.01 1 43 6 6 TYR HA H 4.478 0.01 1 44 6 6 TYR HB2 H 3.249 0.01 2 45 6 6 TYR HB3 H 3.117 0.01 2 46 6 6 TYR HD1 H 7.144 0.01 3 47 6 6 TYR HD2 H 7.144 0.01 3 48 6 6 TYR HE1 H 6.700 0.01 3 49 6 6 TYR HE2 H 6.700 0.01 3 50 6 6 TYR C C 177.785 0.2 1 51 6 6 TYR CA C 59.624 0.2 1 52 6 6 TYR CB C 40.043 0.2 1 53 6 6 TYR N N 116.054 0.3 1 54 7 7 CYS H H 8.671 0.01 1 55 7 7 CYS HA H 4.342 0.01 1 56 7 7 CYS HB2 H 3.349 0.01 2 57 7 7 CYS HB3 H 2.886 0.01 2 58 7 7 CYS C C 175.919 0.2 1 59 7 7 CYS CA C 57.021 0.2 1 60 7 7 CYS CB C 40.632 0.2 1 61 7 7 CYS N N 115.700 0.3 1 62 8 8 PHE H H 8.323 0.01 1 63 8 8 PHE HA H 4.736 0.01 1 64 8 8 PHE HB2 H 3.249 0.01 2 65 8 8 PHE HB3 H 3.249 0.01 2 66 8 8 PHE C C 176.444 0.2 1 67 8 8 PHE CA C 56.813 0.2 1 68 8 8 PHE CB C 36.772 0.2 1 69 8 8 PHE N N 118.352 0.3 1 70 9 9 ARG H H 7.411 0.01 1 71 9 9 ARG HA H 4.299 0.01 1 72 9 9 ARG HB2 H 1.802 0.01 2 73 9 9 ARG HB3 H 1.802 0.01 2 74 9 9 ARG C C 175.317 0.2 1 75 9 9 ARG CA C 56.782 0.2 1 76 9 9 ARG CB C 30.868 0.2 1 77 9 9 ARG CG C 27.693 0.2 1 78 9 9 ARG CD C 43.466 0.2 1 79 9 9 ARG N N 117.529 0.3 1 80 10 10 ASN H H 7.621 0.01 1 81 10 10 ASN HA H 4.699 0.01 1 82 10 10 ASN HB2 H 2.611 0.01 2 83 10 10 ASN HB3 H 2.443 0.01 2 84 10 10 ASN C C 174.095 0.2 1 85 10 10 ASN CA C 52.900 0.2 1 86 10 10 ASN CB C 39.302 0.2 1 87 10 10 ASN N N 117.850 0.3 1 88 11 11 VAL H H 8.029 0.01 1 89 11 11 VAL HA H 4.067 0.01 1 90 11 11 VAL HB H 2.041 0.01 1 91 11 11 VAL HG1 H 0.860 0.01 2 92 11 11 VAL HG2 H 0.884 0.01 2 93 11 11 VAL C C 176.157 0.2 1 94 11 11 VAL CA C 63.377 0.2 1 95 11 11 VAL CB C 31.585 0.2 1 96 11 11 VAL CG1 C 21.216 0.2 2 97 11 11 VAL CG2 C 21.216 0.2 2 98 11 11 VAL N N 120.785 0.3 1 99 12 12 GLN H H 8.350 0.01 1 100 12 12 GLN HA H 4.581 0.01 1 101 12 12 GLN HB2 H 2.168 0.01 2 102 12 12 GLN HB3 H 2.168 0.01 2 103 12 12 GLN C C 175.769 0.2 1 104 12 12 GLN CA C 55.144 0.2 1 105 12 12 GLN CB C 30.322 0.2 1 106 12 12 GLN N N 123.236 0.3 1 107 13 13 ASP H H 8.527 0.01 1 108 13 13 ASP HA H 4.699 0.01 1 109 13 13 ASP HB2 H 2.790 0.01 2 110 13 13 ASP HB3 H 2.790 0.01 2 111 13 13 ASP C C 175.961 0.2 1 112 13 13 ASP CA C 54.135 0.2 1 113 13 13 ASP CB C 39.428 0.2 1 114 13 13 ASP N N 119.604 0.3 1 115 14 14 ASN H H 7.752 0.01 1 116 14 14 ASN HA H 4.618 0.01 1 117 14 14 ASN CA C 53.361 0.2 1 118 14 14 ASN CB C 38.729 0.2 1 119 14 14 ASN N N 117.975 0.3 1 120 15 15 CYS HA H 4.102 0.01 1 121 15 15 CYS HB2 H 2.880 0.01 2 122 15 15 CYS HB3 H 2.338 0.01 2 123 15 15 CYS C C 172.523 0.2 1 124 15 15 CYS CA C 55.378 0.2 1 125 15 15 CYS CB C 34.783 0.2 1 126 16 16 CYS H H 8.204 0.01 1 127 16 16 CYS C C 171.209 0.2 1 128 16 16 CYS CA C 58.343 0.2 1 129 16 16 CYS CB C 41.198 0.2 1 130 16 16 CYS N N 125.332 0.3 1 131 17 17 LEU H H 7.690 0.01 1 132 17 17 LEU HA H 4.270 0.01 1 133 17 17 LEU HB2 H 1.092 0.01 2 134 17 17 LEU HB3 H 1.290 0.01 2 135 17 17 LEU HD1 H 0.448 0.01 2 136 17 17 LEU HD2 H 0.609 0.01 2 137 17 17 LEU C C 174.697 0.2 1 138 17 17 LEU CA C 55.519 0.2 1 139 17 17 LEU CB C 43.988 0.2 1 140 17 17 LEU CD1 C 26.413 0.2 2 141 17 17 LEU CD2 C 25.425 0.2 2 142 17 17 LEU N N 124.975 0.3 1 143 18 18 ARG H H 9.043 0.01 1 144 18 18 ARG HA H 4.600 0.01 1 145 18 18 ARG CA C 51.033 0.2 1 146 18 18 ARG CB C 29.719 0.2 1 147 18 18 ARG N N 126.142 0.3 1 148 19 19 PRO HA H 4.615 0.01 1 149 19 19 PRO HB2 H 1.665 0.01 2 150 19 19 PRO HB3 H 1.665 0.01 2 151 19 19 PRO C C 176.541 0.2 1 152 19 19 PRO CA C 62.320 0.2 1 153 19 19 PRO CB C 31.835 0.2 1 154 19 19 PRO CG C 26.829 0.2 1 155 19 19 PRO CD C 50.141 0.2 1 156 20 20 LEU H H 7.686 0.01 1 157 20 20 LEU HA H 4.279 0.01 1 158 20 20 LEU HB2 H 1.359 0.01 2 159 20 20 LEU HB3 H 1.883 0.01 2 160 20 20 LEU HD1 H 0.448 0.01 2 161 20 20 LEU HD2 H 0.664 0.01 2 162 20 20 LEU CA C 56.948 0.2 1 163 20 20 LEU CB C 44.764 0.2 1 164 20 20 LEU CG C 27.606 0.2 1 165 20 20 LEU CD1 C 26.170 0.2 2 166 20 20 LEU CD2 C 23.072 0.2 2 167 20 20 LEU N N 119.702 0.3 1 168 21 21 TYR H H 8.589 0.01 1 169 21 21 TYR HA H 4.743 0.01 1 170 21 21 TYR HB2 H 2.750 0.01 2 171 21 21 TYR HB3 H 2.750 0.01 2 172 21 21 TYR C C 173.521 0.2 1 173 21 21 TYR CA C 57.035 0.2 1 174 21 21 TYR CB C 39.614 0.2 1 175 21 21 TYR N N 130.701 0.3 1 176 22 22 ILE H H 7.789 0.01 1 177 22 22 ILE HA H 3.826 0.01 1 178 22 22 ILE HB H 0.836 0.01 1 179 22 22 ILE HG12 H 0.586 0.01 2 180 22 22 ILE HG13 H 0.586 0.01 2 181 22 22 ILE HG2 H 0.260 0.01 1 182 22 22 ILE HD1 H 0.300 0.01 1 183 22 22 ILE C C 172.522 0.2 1 184 22 22 ILE CA C 58.422 0.2 1 185 22 22 ILE CB C 38.646 0.2 1 186 22 22 ILE CG1 C 26.925 0.2 1 187 22 22 ILE CG2 C 16.761 0.2 1 188 22 22 ILE CD1 C 11.263 0.2 1 189 22 22 ILE N N 128.483 0.3 1 190 23 23 ASP H H 8.848 0.01 1 191 23 23 ASP HA H 4.528 0.01 1 192 23 23 ASP HB2 H 2.678 0.01 2 193 23 23 ASP HB3 H 2.455 0.01 2 194 23 23 ASP C C 177.392 0.2 1 195 23 23 ASP CA C 52.627 0.2 1 196 23 23 ASP CB C 44.249 0.2 1 197 23 23 ASP N N 127.276 0.3 1 198 24 24 PHE H H 8.260 0.01 1 199 24 24 PHE HA H 3.947 0.01 1 200 24 24 PHE HB2 H 3.186 0.01 2 201 24 24 PHE HB3 H 2.908 0.01 2 202 24 24 PHE C C 177.871 0.2 1 203 24 24 PHE CA C 63.199 0.2 1 204 24 24 PHE CB C 38.402 0.2 1 205 24 24 PHE N N 125.428 0.3 1 206 25 25 LYS H H 8.658 0.01 1 207 25 25 LYS HA H 3.882 0.01 1 208 25 25 LYS HB2 H 1.897 0.01 2 209 25 25 LYS HB3 H 1.897 0.01 2 210 25 25 LYS C C 178.400 0.2 1 211 25 25 LYS CA C 60.572 0.2 1 212 25 25 LYS CB C 32.710 0.2 1 213 25 25 LYS CG C 26.004 0.2 1 214 25 25 LYS CD C 29.542 0.2 1 215 25 25 LYS CE C 42.220 0.2 1 216 25 25 LYS N N 119.569 0.3 1 217 26 26 ARG H H 8.810 0.01 1 218 26 26 ARG HA H 3.996 0.01 1 219 26 26 ARG HB2 H 1.700 0.01 2 220 26 26 ARG HB3 H 1.700 0.01 2 221 26 26 ARG C C 177.462 0.2 1 222 26 26 ARG CA C 58.900 0.2 1 223 26 26 ARG CB C 31.359 0.2 1 224 26 26 ARG CG C 27.130 0.2 1 225 26 26 ARG CD C 43.480 0.2 1 226 26 26 ARG N N 118.819 0.3 1 227 27 27 ASP H H 8.262 0.01 1 228 27 27 ASP HA H 4.777 0.01 1 229 27 27 ASP CA C 56.086 0.2 1 230 27 27 ASP CB C 41.283 0.2 1 231 27 27 ASP N N 113.587 0.3 1 232 28 28 LEU HA H 4.378 0.01 1 233 28 28 LEU HB2 H 1.363 0.01 2 234 28 28 LEU HB3 H 1.037 0.01 2 235 28 28 LEU HD1 H 0.020 0.01 2 236 28 28 LEU HD2 H 0.484 0.01 2 237 28 28 LEU C C 177.113 0.2 1 238 28 28 LEU CA C 54.620 0.2 1 239 28 28 LEU CB C 41.989 0.2 1 240 28 28 LEU CD1 C 24.996 0.2 2 241 28 28 LEU CD2 C 22.649 0.2 2 242 29 29 GLY H H 7.303 0.01 1 243 29 29 GLY HA2 H 4.184 0.01 2 244 29 29 GLY HA3 H 4.002 0.01 2 245 29 29 GLY C C 175.736 0.2 1 246 29 29 GLY CA C 46.167 0.2 1 247 29 29 GLY N N 106.539 0.3 1 248 30 30 TRP H H 7.898 0.01 1 249 30 30 TRP HA H 5.008 0.01 1 250 30 30 TRP HB2 H 2.908 0.01 2 251 30 30 TRP HB3 H 2.429 0.01 2 252 30 30 TRP C C 176.380 0.2 1 253 30 30 TRP CA C 54.321 0.2 1 254 30 30 TRP N N 122.764 0.3 1 255 31 31 LYS H H 8.484 0.01 1 256 31 31 LYS HA H 4.214 0.01 1 257 31 31 LYS HB2 H 2.019 0.01 2 258 31 31 LYS HB3 H 1.865 0.01 2 259 31 31 LYS C C 175.724 0.2 1 260 31 31 LYS CA C 57.586 0.2 1 261 31 31 LYS CB C 32.570 0.2 1 262 31 31 LYS CG C 25.418 0.2 1 263 31 31 LYS CD C 29.564 0.2 1 264 31 31 LYS CE C 42.183 0.2 1 265 31 31 LYS N N 121.056 0.3 1 266 32 32 TRP H H 7.165 0.01 1 267 32 32 TRP HA H 4.575 0.01 1 268 32 32 TRP HB2 H 3.610 0.01 2 269 32 32 TRP HB3 H 3.099 0.01 2 270 32 32 TRP C C 175.781 0.2 1 271 32 32 TRP CA C 55.642 0.2 1 272 32 32 TRP N N 114.996 0.3 1 273 33 33 ILE H H 6.660 0.01 1 274 33 33 ILE HA H 3.531 0.01 1 275 33 33 ILE HB H 1.006 0.01 1 276 33 33 ILE HG12 H -0.400 0.01 2 277 33 33 ILE HG13 H -0.400 0.01 2 278 33 33 ILE HG2 H 0.429 0.01 1 279 33 33 ILE HD1 H -0.457 0.01 1 280 33 33 ILE C C 175.775 0.2 1 281 33 33 ILE CA C 62.662 0.2 1 282 33 33 ILE CB C 38.021 0.2 1 283 33 33 ILE CG1 C 27.021 0.2 1 284 33 33 ILE CG2 C 18.224 0.2 1 285 33 33 ILE CD1 C 13.164 0.2 1 286 33 33 ILE N N 122.481 0.3 1 287 34 34 HIS H H 8.970 0.01 1 288 34 34 HIS HA H 4.748 0.01 1 289 34 34 HIS HB2 H 3.297 0.01 2 290 34 34 HIS HB3 H 3.297 0.01 2 291 34 34 HIS C C 174.274 0.2 1 292 34 34 HIS CA C 57.554 0.2 1 293 34 34 HIS CB C 30.021 0.2 1 294 34 34 HIS N N 125.916 0.3 1 295 35 35 GLU H H 8.036 0.01 1 296 35 35 GLU CA C 53.671 0.2 1 297 35 35 GLU CB C 32.470 0.2 1 298 35 35 GLU N N 117.134 0.3 1 299 36 36 PRO HA H 5.051 0.01 1 300 36 36 PRO HB2 H 2.770 0.01 2 301 36 36 PRO HB3 H 2.770 0.01 2 302 36 36 PRO C C 175.374 0.2 1 303 36 36 PRO CA C 62.868 0.2 1 304 36 36 PRO CB C 34.813 0.2 1 305 36 36 PRO CG C 24.926 0.2 1 306 36 36 PRO CD C 49.550 0.2 1 307 37 37 LYS H H 8.711 0.01 1 308 37 37 LYS HA H 4.369 0.01 1 309 37 37 LYS HB2 H 2.058 0.01 2 310 37 37 LYS HB3 H 1.892 0.01 2 311 37 37 LYS C C 177.047 0.2 1 312 37 37 LYS CA C 57.889 0.2 1 313 37 37 LYS CB C 32.711 0.2 1 314 37 37 LYS CG C 25.332 0.2 1 315 37 37 LYS CD C 29.174 0.2 1 316 37 37 LYS CE C 42.529 0.2 1 317 37 37 LYS N N 116.264 0.3 1 318 38 38 GLY H H 7.648 0.01 1 319 38 38 GLY HA2 H 4.065 0.01 2 320 38 38 GLY HA3 H 3.252 0.01 2 321 38 38 GLY C C 170.508 0.2 1 322 38 38 GLY CA C 45.886 0.2 1 323 38 38 GLY N N 106.070 0.3 1 324 39 39 TYR H H 8.193 0.01 1 325 39 39 TYR HA H 4.752 0.01 1 326 39 39 TYR HB2 H 2.913 0.01 2 327 39 39 TYR HB3 H 2.739 0.01 2 328 39 39 TYR C C 171.714 0.2 1 329 39 39 TYR CA C 55.630 0.2 1 330 39 39 TYR CB C 40.773 0.2 1 331 39 39 TYR N N 116.500 0.3 1 332 40 40 ASN H H 8.592 0.01 1 333 40 40 ASN HA H 4.964 0.01 1 334 40 40 ASN C C 172.425 0.2 1 335 40 40 ASN CA C 53.062 0.2 1 336 40 40 ASN CB C 38.321 0.2 1 337 40 40 ASN N N 120.608 0.3 1 338 41 41 ALA H H 7.209 0.01 1 339 41 41 ALA HA H 4.205 0.01 1 340 41 41 ALA HB H 1.215 0.01 1 341 41 41 ALA C C 177.642 0.2 1 342 41 41 ALA CA C 55.512 0.2 1 343 41 41 ALA CB C 21.308 0.2 1 344 41 41 ALA N N 129.739 0.3 1 345 42 42 ASN H H 7.618 0.01 1 346 42 42 ASN CA C 55.144 0.2 1 347 42 42 ASN CB C 40.652 0.2 1 348 42 42 ASN N N 103.348 0.3 1 349 43 43 PHE C C 172.851 0.2 1 350 43 43 PHE CA C 57.384 0.2 1 351 43 43 PHE CB C 40.103 0.2 1 352 44 44 CYS H H 8.673 0.01 1 353 44 44 CYS HA H 5.020 0.01 1 354 44 44 CYS HB2 H 2.937 0.01 2 355 44 44 CYS HB3 H 2.544 0.01 2 356 44 44 CYS C C 173.418 0.2 1 357 44 44 CYS CA C 54.520 0.2 1 358 44 44 CYS CB C 42.443 0.2 1 359 44 44 CYS N N 118.959 0.3 1 360 45 45 ALA H H 8.078 0.01 1 361 45 45 ALA HA H 4.581 0.01 1 362 45 45 ALA HB H 1.551 0.01 1 363 45 45 ALA C C 176.399 0.2 1 364 45 45 ALA CA C 52.787 0.2 1 365 45 45 ALA CB C 23.601 0.2 1 366 45 45 ALA N N 121.669 0.3 1 367 46 46 GLY H H 8.940 0.01 1 368 46 46 GLY CA C 43.713 0.2 1 369 46 46 GLY N N 111.052 0.3 1 370 47 47 ALA HA H 4.045 0.01 1 371 47 47 ALA HB H 1.392 0.01 1 372 47 47 ALA C C 174.338 0.2 1 373 47 47 ALA CA C 51.933 0.2 1 374 47 47 ALA CB C 19.381 0.2 1 375 48 48 CYS H H 8.342 0.01 1 376 48 48 CYS HA H 4.327 0.01 1 377 48 48 CYS CA C 56.696 0.2 1 378 48 48 CYS CB C 33.058 0.2 1 379 48 48 CYS N N 123.500 0.3 1 380 51 51 LEU HA H 4.215 0.01 1 381 51 51 LEU HB2 H 1.297 0.01 2 382 51 51 LEU HB3 H 1.297 0.01 2 383 51 51 LEU HD1 H 0.739 0.01 2 384 51 51 LEU HD2 H 0.670 0.01 2 385 51 51 LEU C C 176.063 0.2 1 386 51 51 LEU CA C 54.678 0.2 1 387 51 51 LEU CB C 42.678 0.2 1 388 51 51 LEU CD1 C 24.994 0.2 2 389 51 51 LEU CD2 C 23.715 0.2 2 390 52 52 TRP H H 7.637 0.01 1 391 52 52 TRP HA H 4.417 0.01 1 392 52 52 TRP HB2 H 3.136 0.01 2 393 52 52 TRP HB3 H 3.136 0.01 2 394 52 52 TRP C C 175.947 0.2 1 395 52 52 TRP CA C 57.577 0.2 1 396 52 52 TRP N N 121.748 0.3 1 397 53 53 SER H H 7.767 0.01 1 398 53 53 SER HA H 4.330 0.01 1 399 53 53 SER HB2 H 3.658 0.01 2 400 53 53 SER HB3 H 3.658 0.01 2 401 53 53 SER C C 174.368 0.2 1 402 53 53 SER CA C 58.070 0.2 1 403 53 53 SER CB C 64.132 0.2 1 404 53 53 SER N N 116.468 0.3 1 405 54 54 SER H H 8.090 0.01 1 406 54 54 SER HA H 4.366 0.01 1 407 54 54 SER HB2 H 3.842 0.01 2 408 54 54 SER HB3 H 3.842 0.01 2 409 54 54 SER C C 174.529 0.2 1 410 54 54 SER CA C 58.790 0.2 1 411 54 54 SER CB C 63.954 0.2 1 412 54 54 SER N N 117.188 0.3 1 413 55 55 ASP H H 8.254 0.01 1 414 55 55 ASP HA H 4.694 0.01 1 415 55 55 ASP HB2 H 2.802 0.01 2 416 55 55 ASP HB3 H 2.802 0.01 2 417 55 55 ASP C C 176.268 0.2 1 418 55 55 ASP CA C 53.917 0.2 1 419 55 55 ASP CB C 39.640 0.2 1 420 55 55 ASP N N 120.997 0.3 1 421 56 56 THR H H 7.937 0.01 1 422 56 56 THR HA H 4.205 0.01 1 423 56 56 THR HB H 4.217 0.01 1 424 56 56 THR HG2 H 1.133 0.01 1 425 56 56 THR C C 175.165 0.2 1 426 56 56 THR CA C 62.769 0.2 1 427 56 56 THR CB C 69.604 0.2 1 428 56 56 THR CG2 C 21.875 0.2 1 429 56 56 THR N N 113.301 0.3 1 430 57 57 GLN H H 8.100 0.01 1 431 57 57 GLN HA H 4.220 0.01 1 432 57 57 GLN HB2 H 1.952 0.01 2 433 57 57 GLN HB3 H 1.952 0.01 2 434 57 57 GLN C C 176.232 0.2 1 435 57 57 GLN CA C 56.696 0.2 1 436 57 57 GLN CB C 29.092 0.2 1 437 57 57 GLN N N 120.870 0.3 1 438 58 58 HIS H H 8.205 0.01 1 439 58 58 HIS HA H 4.628 0.01 1 440 58 58 HIS HB2 H 3.220 0.01 2 441 58 58 HIS HB3 H 3.220 0.01 2 442 58 58 HIS C C 174.627 0.2 1 443 58 58 HIS CA C 55.741 0.2 1 444 58 58 HIS CB C 28.398 0.2 1 445 58 58 HIS N N 117.632 0.3 1 446 59 59 SER H H 8.099 0.01 1 447 59 59 SER HA H 4.379 0.01 1 448 59 59 SER HB2 H 3.870 0.01 2 449 59 59 SER HB3 H 3.870 0.01 2 450 59 59 SER C C 174.565 0.2 1 451 59 59 SER CA C 59.006 0.2 1 452 59 59 SER CB C 63.903 0.2 1 453 59 59 SER N N 115.369 0.3 1 454 60 60 LYS H H 8.211 0.01 1 455 60 60 LYS HA H 4.311 0.01 1 456 60 60 LYS HB2 H 1.797 0.01 2 457 60 60 LYS HB3 H 1.797 0.01 2 458 60 60 LYS C C 176.669 0.2 1 459 60 60 LYS CA C 55.026 0.2 1 460 60 60 LYS CB C 32.813 0.2 1 461 60 60 LYS CG C 25.013 0.2 1 462 60 60 LYS CD C 29.243 0.2 1 463 60 60 LYS N N 122.533 0.3 1 464 61 61 VAL H H 7.858 0.01 1 465 61 61 VAL HA H 4.038 0.01 1 466 61 61 VAL HB H 2.013 0.01 1 467 61 61 VAL HG1 H 0.840 0.01 2 468 61 61 VAL HG2 H 0.900 0.01 2 469 61 61 VAL CA C 62.819 0.2 1 470 61 61 VAL CB C 32.311 0.2 1 471 61 61 VAL CG1 C 21.253 0.2 2 472 61 61 VAL CG2 C 21.253 0.2 2 473 61 61 VAL N N 119.447 0.3 1 474 62 62 LEU H H 7.977 0.01 1 475 62 62 LEU HA H 4.275 0.01 1 476 62 62 LEU HB2 H 1.558 0.01 2 477 62 62 LEU HB3 H 1.558 0.01 2 478 62 62 LEU HG H 1.510 0.01 1 479 62 62 LEU HD1 H 0.796 0.01 2 480 62 62 LEU HD2 H 0.744 0.01 2 481 62 62 LEU C C 177.249 0.2 1 482 62 62 LEU CA C 55.566 0.2 1 483 62 62 LEU CB C 42.312 0.2 1 484 62 62 LEU CG C 27.176 0.2 1 485 62 62 LEU CD1 C 25.046 0.2 2 486 62 62 LEU CD2 C 23.774 0.2 2 487 62 62 LEU N N 124.072 0.3 1 488 63 63 SER H H 7.980 0.01 1 489 63 63 SER HA H 4.379 0.01 1 490 63 63 SER HB2 H 3.817 0.01 2 491 63 63 SER HB3 H 3.817 0.01 2 492 63 63 SER C C 174.578 0.2 1 493 63 63 SER CA C 58.677 0.2 1 494 63 63 SER CB C 63.998 0.2 1 495 63 63 SER N N 115.415 0.3 1 496 64 64 LEU H H 7.854 0.01 1 497 64 64 LEU HA H 4.090 0.01 1 498 64 64 LEU HB2 H 1.336 0.01 2 499 64 64 LEU HB3 H 1.230 0.01 2 500 64 64 LEU CA C 55.905 0.2 1 501 64 64 LEU CB C 42.262 0.2 1 502 64 64 LEU CD1 C 24.530 0.2 2 503 64 64 LEU CD2 C 24.530 0.2 2 504 64 64 LEU N N 122.800 0.3 1 505 65 65 TYR HA H 4.328 0.01 1 506 65 65 TYR HB2 H 2.808 0.01 2 507 65 65 TYR HB3 H 2.993 0.01 2 508 65 65 TYR CA C 58.121 0.2 1 509 65 65 TYR CB C 38.412 0.2 1 510 66 66 ASN HA H 4.614 0.01 1 511 66 66 ASN HB2 H 2.728 0.01 2 512 66 66 ASN HB3 H 2.728 0.01 2 513 66 66 ASN C C 174.822 0.2 1 514 66 66 ASN CA C 53.580 0.2 1 515 66 66 ASN CB C 38.920 0.2 1 516 67 67 THR H H 7.780 0.01 1 517 67 67 THR HA H 4.302 0.01 1 518 67 67 THR HB H 4.217 0.01 1 519 67 67 THR HG2 H 1.100 0.01 1 520 67 67 THR C C 174.102 0.2 1 521 67 67 THR CA C 62.218 0.2 1 522 67 67 THR CB C 69.826 0.2 1 523 67 67 THR CG2 C 21.725 0.2 1 524 67 67 THR N N 112.681 0.3 1 525 68 68 ILE H H 7.820 0.01 1 526 68 68 ILE CB C 38.929 0.2 1 527 68 68 ILE N N 120.829 0.3 1 528 70 70 PRO HA H 4.423 0.01 1 529 70 70 PRO HB2 H 2.257 0.01 2 530 70 70 PRO HB3 H 1.953 0.01 2 531 70 70 PRO C C 177.048 0.2 1 532 70 70 PRO CA C 64.145 0.2 1 533 70 70 PRO CB C 32.191 0.2 1 534 70 70 PRO CG C 27.378 0.2 1 535 70 70 PRO CD C 50.748 0.2 1 536 71 71 GLU H H 8.018 0.01 1 537 71 71 GLU HA H 4.312 0.01 1 538 71 71 GLU HB2 H 2.124 0.01 2 539 71 71 GLU HB3 H 1.939 0.01 2 540 71 71 GLU C C 175.893 0.2 1 541 71 71 GLU CA C 55.746 0.2 1 542 71 71 GLU CB C 28.529 0.2 1 543 71 71 GLU N N 117.228 0.3 1 544 72 72 ALA H H 7.906 0.01 1 545 72 72 ALA HA H 4.289 0.01 1 546 72 72 ALA HB H 1.369 0.01 1 547 72 72 ALA C C 178.025 0.2 1 548 72 72 ALA CA C 52.792 0.2 1 549 72 72 ALA CB C 19.201 0.2 1 550 72 72 ALA N N 123.198 0.3 1 551 73 73 SER H H 8.062 0.01 1 552 73 73 SER HA H 4.422 0.01 1 553 73 73 SER HB2 H 3.862 0.01 2 554 73 73 SER HB3 H 3.862 0.01 2 555 73 73 SER C C 173.701 0.2 1 556 73 73 SER CA C 58.559 0.2 1 557 73 73 SER CB C 64.226 0.2 1 558 73 73 SER N N 114.332 0.3 1 559 74 74 ALA H H 7.952 0.01 1 560 74 74 ALA HB H 1.493 0.01 1 561 74 74 ALA C C 177.046 0.2 1 562 74 74 ALA CA C 51.844 0.2 1 563 74 74 ALA CB C 21.116 0.2 1 564 74 74 ALA N N 124.538 0.3 1 565 75 75 SER H H 8.374 0.01 1 566 75 75 SER CA C 57.235 0.2 1 567 75 75 SER CB C 63.725 0.2 1 568 75 75 SER N N 116.420 0.3 1 569 76 76 PRO C C 175.210 0.2 1 570 76 76 PRO CA C 63.161 0.2 1 571 76 76 PRO CB C 32.526 0.2 1 572 76 76 PRO CG C 27.236 0.2 1 573 76 76 PRO CD C 50.815 0.2 1 574 77 77 CYS H H 8.787 0.01 1 575 77 77 CYS C C 172.857 0.2 1 576 77 77 CYS CA C 53.461 0.2 1 577 77 77 CYS CB C 42.490 0.2 1 578 77 77 CYS N N 120.913 0.3 1 579 78 78 CYS H H 8.649 0.01 1 580 78 78 CYS HA H 4.978 0.01 1 581 78 78 CYS HB2 H 1.904 0.01 2 582 78 78 CYS HB3 H 1.904 0.01 2 583 78 78 CYS C C 173.197 0.2 1 584 78 78 CYS CA C 55.198 0.2 1 585 78 78 CYS CB C 36.682 0.2 1 586 78 78 CYS N N 125.733 0.3 1 587 79 79 VAL H H 9.207 0.01 1 588 79 79 VAL HA H 4.873 0.01 1 589 79 79 VAL HB H 2.344 0.01 1 590 79 79 VAL HG1 H 0.877 0.01 2 591 79 79 VAL HG2 H 0.805 0.01 2 592 79 79 VAL C C 174.695 0.2 1 593 79 79 VAL CA C 59.240 0.2 1 594 79 79 VAL CB C 36.302 0.2 1 595 79 79 VAL N N 122.918 0.3 1 596 80 80 SER H H 8.240 0.01 1 597 80 80 SER HA H 4.804 0.01 1 598 80 80 SER HB2 H 3.814 0.01 2 599 80 80 SER HB3 H 3.814 0.01 2 600 80 80 SER C C 173.742 0.2 1 601 80 80 SER CA C 59.226 0.2 1 602 80 80 SER CB C 64.791 0.2 1 603 80 80 SER N N 114.501 0.3 1 604 81 81 GLN H H 8.667 0.01 1 605 81 81 GLN HA H 4.502 0.01 1 606 81 81 GLN HB2 H 1.932 0.01 2 607 81 81 GLN HB3 H 1.399 0.01 2 608 81 81 GLN C C 173.715 0.2 1 609 81 81 GLN CA C 56.110 0.2 1 610 81 81 GLN CB C 29.477 0.2 1 611 81 81 GLN N N 122.226 0.3 1 612 82 82 ASP H H 7.355 0.01 1 613 82 82 ASP HA H 4.865 0.01 1 614 82 82 ASP HB2 H 2.678 0.01 2 615 82 82 ASP HB3 H 2.678 0.01 2 616 82 82 ASP C C 173.915 0.2 1 617 82 82 ASP CA C 53.835 0.2 1 618 82 82 ASP CB C 41.275 0.2 1 619 82 82 ASP N N 117.469 0.3 1 620 83 83 LEU H H 8.400 0.01 1 621 83 83 LEU HA H 5.512 0.01 1 622 83 83 LEU HB2 H 1.726 0.01 2 623 83 83 LEU HB3 H 1.206 0.01 2 624 83 83 LEU C C 176.594 0.2 1 625 83 83 LEU CA C 53.403 0.2 1 626 83 83 LEU CB C 46.101 0.2 1 627 83 83 LEU CD1 C 25.814 0.2 2 628 83 83 LEU CD2 C 25.814 0.2 2 629 83 83 LEU N N 124.422 0.3 1 630 84 84 GLU H H 9.520 0.01 1 631 84 84 GLU HA H 5.013 0.01 1 632 84 84 GLU HB2 H 1.754 0.01 2 633 84 84 GLU HB3 H 2.278 0.01 2 634 84 84 GLU CA C 52.761 0.2 1 635 84 84 GLU CB C 31.776 0.2 1 636 84 84 GLU N N 120.380 0.3 1 637 85 85 PRO HA H 5.108 0.01 1 638 85 85 PRO HB2 H 1.727 0.01 2 639 85 85 PRO HB3 H 1.727 0.01 2 640 85 85 PRO C C 174.619 0.2 1 641 85 85 PRO CA C 62.317 0.2 1 642 85 85 PRO CB C 34.169 0.2 1 643 85 85 PRO CG C 26.543 0.2 1 644 85 85 PRO CD C 50.970 0.2 1 645 86 86 LEU H H 8.419 0.01 1 646 86 86 LEU HA H 4.670 0.01 1 647 86 86 LEU HB2 H 1.525 0.01 2 648 86 86 LEU HB3 H 1.001 0.01 2 649 86 86 LEU HD1 H 0.185 0.01 2 650 86 86 LEU HD2 H 0.850 0.01 2 651 86 86 LEU C C 175.394 0.2 1 652 86 86 LEU CA C 53.511 0.2 1 653 86 86 LEU CB C 47.396 0.2 1 654 86 86 LEU CD1 C 26.663 0.2 2 655 86 86 LEU CD2 C 23.335 0.2 2 656 86 86 LEU N N 118.803 0.3 1 657 87 87 THR H H 8.485 0.01 1 658 87 87 THR HA H 4.888 0.01 1 659 87 87 THR HB H 3.970 0.01 1 660 87 87 THR HG2 H 1.093 0.01 1 661 87 87 THR C C 173.896 0.2 1 662 87 87 THR CA C 63.269 0.2 1 663 87 87 THR CB C 69.186 0.2 1 664 87 87 THR CG2 C 22.532 0.2 1 665 87 87 THR N N 124.605 0.3 1 666 88 88 ILE H H 8.985 0.01 1 667 88 88 ILE HA H 5.016 0.01 1 668 88 88 ILE HB H 1.840 0.01 1 669 88 88 ILE HG12 H 1.565 0.01 2 670 88 88 ILE HG13 H 1.000 0.01 2 671 88 88 ILE HG2 H 0.724 0.01 1 672 88 88 ILE HD1 H 0.756 0.01 1 673 88 88 ILE C C 173.115 0.2 1 674 88 88 ILE CA C 59.124 0.2 1 675 88 88 ILE CB C 42.402 0.2 1 676 88 88 ILE CG1 C 26.816 0.2 1 677 88 88 ILE CG2 C 19.455 0.2 1 678 88 88 ILE CD1 C 15.774 0.2 1 679 88 88 ILE N N 120.979 0.3 1 680 89 89 LEU H H 8.702 0.01 1 681 89 89 LEU HA H 5.464 0.01 1 682 89 89 LEU HB2 H 1.704 0.01 2 683 89 89 LEU HB3 H 1.591 0.01 2 684 89 89 LEU HD1 H 0.752 0.01 2 685 89 89 LEU HD2 H 0.715 0.01 2 686 89 89 LEU C C 175.955 0.2 1 687 89 89 LEU CA C 54.044 0.2 1 688 89 89 LEU CB C 45.960 0.2 1 689 89 89 LEU CG C 28.189 0.2 1 690 89 89 LEU CD1 C 25.991 0.2 2 691 89 89 LEU CD2 C 24.838 0.2 2 692 89 89 LEU N N 122.395 0.3 1 693 90 90 TYR H H 9.302 0.01 1 694 90 90 TYR HA H 5.004 0.01 1 695 90 90 TYR HB2 H 3.593 0.01 2 696 90 90 TYR HB3 H 3.047 0.01 2 697 90 90 TYR C C 170.779 0.2 1 698 90 90 TYR CA C 55.685 0.2 1 699 90 90 TYR CB C 41.316 0.2 1 700 90 90 TYR N N 126.149 0.3 1 701 91 91 TYR H H 8.904 0.01 1 702 91 91 TYR HA H 4.897 0.01 1 703 91 91 TYR HB2 H 2.813 0.01 2 704 91 91 TYR HB3 H 2.637 0.01 2 705 91 91 TYR C C 176.383 0.2 1 706 91 91 TYR CA C 57.397 0.2 1 707 91 91 TYR CB C 40.990 0.2 1 708 91 91 TYR N N 118.632 0.3 1 709 92 92 ILE H H 8.303 0.01 1 710 92 92 ILE HA H 4.254 0.01 1 711 92 92 ILE HB H 1.677 0.01 1 712 92 92 ILE HG12 H 1.375 0.01 2 713 92 92 ILE HG13 H 1.068 0.01 2 714 92 92 ILE HG2 H 0.848 0.01 1 715 92 92 ILE HD1 H 0.832 0.01 1 716 92 92 ILE C C 177.176 0.2 1 717 92 92 ILE CA C 60.643 0.2 1 718 92 92 ILE CB C 38.023 0.2 1 719 92 92 ILE CG1 C 27.288 0.2 1 720 92 92 ILE CG2 C 17.383 0.2 1 721 92 92 ILE CD1 C 13.211 0.2 1 722 92 92 ILE N N 122.610 0.3 1 723 93 93 GLY H H 8.796 0.01 1 724 93 93 GLY HA2 H 4.038 0.01 2 725 93 93 GLY HA3 H 3.647 0.01 2 726 93 93 GLY C C 174.878 0.2 1 727 93 93 GLY CA C 47.107 0.2 1 728 93 93 GLY N N 117.857 0.3 1 729 94 94 LYS H H 8.725 0.01 1 730 94 94 LYS HA H 4.359 0.01 1 731 94 94 LYS HB2 H 1.993 0.01 2 732 94 94 LYS HB3 H 1.774 0.01 2 733 94 94 LYS C C 176.485 0.2 1 734 94 94 LYS CA C 56.191 0.2 1 735 94 94 LYS CB C 32.653 0.2 1 736 94 94 LYS N N 125.950 0.3 1 737 95 95 THR H H 8.244 0.01 1 738 95 95 THR HA H 4.576 0.01 1 739 95 95 THR HB H 4.214 0.01 1 740 95 95 THR HG2 H 1.155 0.01 1 741 95 95 THR CA C 60.472 0.2 1 742 95 95 THR CB C 70.630 0.2 1 743 95 95 THR CG2 C 21.500 0.2 1 744 95 95 THR N N 119.419 0.3 1 745 96 96 PRO HA H 3.798 0.01 1 746 96 96 PRO HB2 H 1.539 0.01 2 747 96 96 PRO HB3 H 1.539 0.01 2 748 96 96 PRO C C 175.728 0.2 1 749 96 96 PRO CA C 61.837 0.2 1 750 96 96 PRO CB C 32.085 0.2 1 751 96 96 PRO CG C 26.711 0.2 1 752 96 96 PRO CD C 51.063 0.2 1 753 97 97 LYS H H 8.726 0.01 1 754 97 97 LYS HA H 4.254 0.01 1 755 97 97 LYS HB2 H 1.033 0.01 2 756 97 97 LYS HB3 H 0.546 0.01 2 757 97 97 LYS C C 173.489 0.2 1 758 97 97 LYS CA C 53.983 0.2 1 759 97 97 LYS CB C 34.274 0.2 1 760 97 97 LYS CG C 24.377 0.2 1 761 97 97 LYS CD C 28.570 0.2 1 762 97 97 LYS CE C 42.398 0.2 1 763 97 97 LYS N N 123.646 0.3 1 764 98 98 ILE H H 7.855 0.01 1 765 98 98 ILE HA H 5.143 0.01 1 766 98 98 ILE HB H 1.587 0.01 1 767 98 98 ILE HG12 H 1.417 0.01 2 768 98 98 ILE HG13 H 1.003 0.01 2 769 98 98 ILE HG2 H 0.778 0.01 1 770 98 98 ILE HD1 H 0.762 0.01 1 771 98 98 ILE C C 176.868 0.2 1 772 98 98 ILE CA C 59.373 0.2 1 773 98 98 ILE CB C 39.948 0.2 1 774 98 98 ILE CG1 C 28.152 0.2 1 775 98 98 ILE CG2 C 17.776 0.2 1 776 98 98 ILE CD1 C 13.126 0.2 1 777 98 98 ILE N N 121.796 0.3 1 778 99 99 GLU H H 8.836 0.01 1 779 99 99 GLU HA H 4.788 0.01 1 780 99 99 GLU HB2 H 2.267 0.01 2 781 99 99 GLU HB3 H 2.267 0.01 2 782 99 99 GLU C C 173.270 0.2 1 783 99 99 GLU CA C 54.138 0.2 1 784 99 99 GLU CB C 32.496 0.2 1 785 99 99 GLU N N 124.534 0.3 1 786 100 100 GLN H H 8.598 0.01 1 787 100 100 GLN HA H 5.002 0.01 1 788 100 100 GLN HB2 H 1.926 0.01 2 789 100 100 GLN HB3 H 1.806 0.01 2 790 100 100 GLN C C 175.350 0.2 1 791 100 100 GLN CA C 55.088 0.2 1 792 100 100 GLN CB C 30.398 0.2 1 793 100 100 GLN N N 121.603 0.3 1 794 101 101 LEU H H 9.094 0.01 1 795 101 101 LEU HA H 4.668 0.01 1 796 101 101 LEU HB2 H 1.815 0.01 2 797 101 101 LEU HB3 H 1.651 0.01 2 798 101 101 LEU HD1 H 0.932 0.01 2 799 101 101 LEU HD2 H 0.885 0.01 2 800 101 101 LEU C C 176.335 0.2 1 801 101 101 LEU CA C 53.476 0.2 1 802 101 101 LEU CB C 42.802 0.2 1 803 101 101 LEU CD1 C 26.080 0.2 2 804 101 101 LEU CD2 C 23.144 0.2 2 805 101 101 LEU N N 126.928 0.3 1 806 102 102 SER H H 8.498 0.01 1 807 102 102 SER HA H 4.079 0.01 1 808 102 102 SER HB2 H 3.793 0.01 2 809 102 102 SER HB3 H 3.793 0.01 2 810 102 102 SER C C 174.478 0.2 1 811 102 102 SER CA C 59.282 0.2 1 812 102 102 SER CB C 64.020 0.2 1 813 102 102 SER N N 118.761 0.3 1 814 103 103 ASN H H 8.726 0.01 1 815 103 103 ASN HA H 4.592 0.01 1 816 103 103 ASN CA C 51.763 0.2 1 817 103 103 ASN CB C 36.302 0.2 1 818 103 103 ASN N N 115.913 0.3 1 819 104 104 MET H H 7.251 0.01 1 820 104 104 MET N N 113.929 0.3 1 821 105 105 ILE HB H 1.629 0.01 1 822 105 105 ILE HG12 H 1.344 0.01 2 823 105 105 ILE HG13 H 1.442 0.01 2 824 105 105 ILE HG2 H 0.900 0.01 1 825 105 105 ILE HD1 H 0.953 0.01 1 826 105 105 ILE CG2 C 16.909 0.2 1 827 105 105 ILE CD1 C 14.399 0.2 1 828 106 106 VAL C C 174.878 0.2 1 829 106 106 VAL CA C 63.243 0.2 1 830 106 106 VAL CB C 31.662 0.2 1 831 107 107 LYS H H 8.754 0.01 1 832 107 107 LYS HA H 4.467 0.01 1 833 107 107 LYS HB2 H 1.767 0.01 2 834 107 107 LYS HB3 H 1.602 0.01 2 835 107 107 LYS C C 176.021 0.2 1 836 107 107 LYS CA C 55.694 0.2 1 837 107 107 LYS CB C 34.819 0.2 1 838 107 107 LYS CG C 24.993 0.2 1 839 107 107 LYS CD C 29.141 0.2 1 840 107 107 LYS CE C 42.062 0.2 1 841 107 107 LYS N N 125.755 0.3 1 842 108 108 SER H H 7.814 0.01 1 843 108 108 SER HA H 5.000 0.01 1 844 108 108 SER HB2 H 4.000 0.01 2 845 108 108 SER HB3 H 3.854 0.01 2 846 108 108 SER C C 173.540 0.2 1 847 108 108 SER CA C 57.470 0.2 1 848 108 108 SER CB C 65.561 0.2 1 849 108 108 SER N N 110.267 0.3 1 850 109 109 CYS H H 8.123 0.01 1 851 109 109 CYS HA H 5.444 0.01 1 852 109 109 CYS HB2 H 2.200 0.01 2 853 109 109 CYS HB3 H 2.893 0.01 2 854 109 109 CYS C C 172.279 0.2 1 855 109 109 CYS CA C 53.763 0.2 1 856 109 109 CYS CB C 44.112 0.2 1 857 109 109 CYS N N 118.004 0.3 1 858 110 110 LYS H H 9.381 0.01 1 859 110 110 LYS HA H 4.601 0.01 1 860 110 110 LYS C C 173.331 0.2 1 861 110 110 LYS CA C 55.330 0.2 1 862 110 110 LYS CB C 35.397 0.2 1 863 110 110 LYS CG C 24.000 0.2 1 864 110 110 LYS CD C 29.826 0.2 1 865 110 110 LYS CE C 42.464 0.2 1 866 110 110 LYS N N 117.671 0.3 1 867 111 111 CYS H H 8.310 0.01 1 868 111 111 CYS HA H 5.200 0.01 1 869 111 111 CYS HB2 H 2.924 0.01 2 870 111 111 CYS HB3 H 2.800 0.01 2 871 111 111 CYS C C 175.325 0.2 1 872 111 111 CYS CA C 56.281 0.2 1 873 111 111 CYS CB C 43.313 0.2 1 874 111 111 CYS N N 118.550 0.3 1 875 112 112 SER H H 9.206 0.01 1 876 112 112 SER HA H 4.312 0.01 1 877 112 112 SER CA C 59.286 0.2 1 878 112 112 SER CB C 65.441 0.2 1 stop_ save_