data_27510 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for hFABP1 triple-mutant (K57A,E77A,K96A)in complex with GW7647 ; _BMRB_accession_number 27510 _BMRB_flat_file_name bmr27510.str _Entry_type original _Submission_date 2018-06-06 _Accession_date 2018-06-06 _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 Chandrashekaran Indu R. . 2 Mohanty Biswaranjan . . 3 Scanlon Martin J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 122 "13C chemical shifts" 241 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-26 update BMRB 'update entry citation' 2018-12-19 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27509 'hFABP1 K57A, E77A, K96A mutant' stop_ _Original_release_date 2018-06-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor alpha agonists ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30598509 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Patil Rahul . . 2 Mohanty Biswaranjan . . 3 Liu Bonan . . 4 Chandrashekaran Indu R. . 5 Headey Stephen J. . 6 Williams Martin L. . 7 Clements Craig S. . 8 Ilyichova Olga . . 9 Doak Bradley C. . 10 Genissel Patrick . . 11 Weaver Richard J. . 12 Vuillard Laurent . . 13 Halls Michelle L. . 14 Porter Christopher . . 15 Scanlon Martin J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 294 _Journal_issue 10 _Journal_ISSN 1083-351X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3720 _Page_last 3734 _Year 2019 _Details . loop_ _Keyword FABP1 GW7647 NMR PPAR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'hFABP1 K57A, E77A, K96A mutant in complex with GW7647' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'holo hFABP1 K567A, E77A, K96A mutant' $Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Nuclear translocation' 'PPAR alpha activation' stop_ _Database_query_date . _Details 'The PubChem CID for GW7647 is 3392731; PPAR alpha agonist.' save_ ######################## # Monomeric polymers # ######################## save_Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant _Molecular_mass 14180.3 _Mol_thiol_state 'all free' loop_ _Biological_function 'Fatty acid binding and transport' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; GSMSFSGKYQLQSQENFEAF MKAIGLPEELIQKGKDIKGV SEIVQNGKHFKFTITAGSAV IQNEFTVGEECELETMTGAK VKTVVQLEGDNKLVTTFANI KSVTELNGDIITNTMTLGDI VFKRISKRI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 SER 3 1 MET 4 2 SER 5 3 PHE 6 4 SER 7 5 GLY 8 6 LYS 9 7 TYR 10 8 GLN 11 9 LEU 12 10 GLN 13 11 SER 14 12 GLN 15 13 GLU 16 14 ASN 17 15 PHE 18 16 GLU 19 17 ALA 20 18 PHE 21 19 MET 22 20 LYS 23 21 ALA 24 22 ILE 25 23 GLY 26 24 LEU 27 25 PRO 28 26 GLU 29 27 GLU 30 28 LEU 31 29 ILE 32 30 GLN 33 31 LYS 34 32 GLY 35 33 LYS 36 34 ASP 37 35 ILE 38 36 LYS 39 37 GLY 40 38 VAL 41 39 SER 42 40 GLU 43 41 ILE 44 42 VAL 45 43 GLN 46 44 ASN 47 45 GLY 48 46 LYS 49 47 HIS 50 48 PHE 51 49 LYS 52 50 PHE 53 51 THR 54 52 ILE 55 53 THR 56 54 ALA 57 55 GLY 58 56 SER 59 57 ALA 60 58 VAL 61 59 ILE 62 60 GLN 63 61 ASN 64 62 GLU 65 63 PHE 66 64 THR 67 65 VAL 68 66 GLY 69 67 GLU 70 68 GLU 71 69 CYS 72 70 GLU 73 71 LEU 74 72 GLU 75 73 THR 76 74 MET 77 75 THR 78 76 GLY 79 77 ALA 80 78 LYS 81 79 VAL 82 80 LYS 83 81 THR 84 82 VAL 85 83 VAL 86 84 GLN 87 85 LEU 88 86 GLU 89 87 GLY 90 88 ASP 91 89 ASN 92 90 LYS 93 91 LEU 94 92 VAL 95 93 THR 96 94 THR 97 95 PHE 98 96 ALA 99 97 ASN 100 98 ILE 101 99 LYS 102 100 SER 103 101 VAL 104 102 THR 105 103 GLU 106 104 LEU 107 105 ASN 108 106 GLY 109 107 ASP 110 108 ILE 111 109 ILE 112 110 THR 113 111 ASN 114 112 THR 115 113 MET 116 114 THR 117 115 LEU 118 116 GLY 119 117 ASP 120 118 ILE 121 119 VAL 122 120 PHE 123 121 LYS 124 122 ARG 125 123 ILE 126 124 SER 127 125 LYS 128 126 ARG 129 127 ILE 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 $Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant 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 $Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling GW7647 0.3 mM 'natural abundance' $Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant 0.25 mM '[U-99% 13C; U-99% 15N]' D2O 10 % '[U-100% 2H]' 'sodium chloride' 50 mM 'natural abundance' MES 20 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.5 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA_1.2 _Saveframe_category software _Name CARA_1.2 _Version 4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'chemical shift calculation' 'data analysis' 'peak picking' stop_ _Details . save_ save_MddNMR _Saveframe_category software _Name MddNMR _Version 2 loop_ _Vendor _Address _Electronic_address 'Orekhov, Jaravine, Mayzel and Kazimierczuk,Swedish NMR Center, University of Gothenburg' . . 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 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 5.5 . pH pressure 1 . atm temperature 308 . 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 'Reference offset for Nitrogen can be corrected by - 0.9 ppm.' loop_ _Software_label $TOPSPIN $CARA_1.2 $MddNMR stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D CBCA(CO)NH' 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 'holo hFABP1 K567A, E77A, K96A mutant' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 4 SER CA C 57.252 0.3 1 2 2 4 SER CB C 64.341 0.3 1 3 3 5 PHE H H 9.572 0.025 1 4 3 5 PHE CA C 59.98 0.3 1 5 3 5 PHE CB C 40.64 0.3 1 6 3 5 PHE N N 119.702 0.3 1 7 4 6 SER H H 8.354 0.025 1 8 4 6 SER CA C 60 0.3 1 9 4 6 SER CB C 63.81 0.3 1 10 4 6 SER N N 114.054 0.3 1 11 5 7 GLY H H 9.013 0.025 1 12 5 7 GLY CA C 44.954 0.3 1 13 5 7 GLY N N 108.974 0.3 1 14 6 8 LYS H H 8.227 0.025 1 15 6 8 LYS CA C 54.874 0.3 1 16 6 8 LYS CB C 34.711 0.3 1 17 6 8 LYS N N 117.419 0.3 1 18 7 9 TYR H H 9.135 0.025 1 19 7 9 TYR CA C 56.678 0.3 1 20 7 9 TYR CB C 42.264 0.3 1 21 7 9 TYR N N 117.274 0.3 1 22 8 10 GLN H H 9.078 0.025 1 23 8 10 GLN CA C 53.924 0.3 1 24 8 10 GLN CB C 32.011 0.3 1 25 8 10 GLN N N 119.63 0.3 1 26 9 11 LEU H H 8.435 0.025 1 27 9 11 LEU CA C 57.062 0.3 1 28 9 11 LEU CB C 42.117 0.3 1 29 9 11 LEU N N 130.531 0.3 1 30 10 12 GLN H H 10.026 0.025 1 31 10 12 GLN CA C 56.281 0.3 1 32 10 12 GLN CB C 31.427 0.3 1 33 10 12 GLN N N 123.433 0.3 1 34 11 13 SER H H 8.044 0.025 1 35 11 13 SER CA C 57.805 0.3 1 36 11 13 SER CB C 64.831 0.3 1 37 11 13 SER N N 108.248 0.3 1 38 12 14 GLN H H 8.451 0.025 1 39 12 14 GLN CA C 54.639 0.3 1 40 12 14 GLN CB C 33.153 0.3 1 41 12 14 GLN N N 115.157 0.3 1 42 13 15 GLU H H 9.258 0.025 1 43 13 15 GLU CA C 55.299 0.3 1 44 13 15 GLU CB C 33.131 0.3 1 45 13 15 GLU N N 120.109 0.3 1 46 14 16 ASN H H 9.276 0.025 1 47 14 16 ASN CA C 54.321 0.3 1 48 14 16 ASN CB C 36.692 0.3 1 49 14 16 ASN N N 115.762 0.3 1 50 15 17 PHE H H 8.321 0.025 1 51 15 17 PHE CA C 61.984 0.3 1 52 15 17 PHE CB C 39.707 0.3 1 53 15 17 PHE N N 115.942 0.3 1 54 16 18 GLU H H 9.297 0.025 1 55 16 18 GLU CA C 61.156 0.3 1 56 16 18 GLU CB C 28.713 0.3 1 57 16 18 GLU N N 115.938 0.3 1 58 17 19 ALA H H 8.233 0.025 1 59 17 19 ALA CA C 54.851 0.3 1 60 17 19 ALA CB C 18.354 0.3 1 61 17 19 ALA N N 117.371 0.3 1 62 18 20 PHE H H 7.781 0.025 1 63 18 20 PHE CA C 62.019 0.3 1 64 18 20 PHE CB C 40.13 0.3 1 65 18 20 PHE N N 116.12 0.3 1 66 19 21 MET H H 8.101 0.025 1 67 19 21 MET CA C 56.281 0.3 1 68 19 21 MET CB C 31.347 0.3 1 69 19 21 MET N N 112.181 0.3 1 70 20 22 LYS H H 8.218 0.025 1 71 20 22 LYS CA C 59.227 0.3 1 72 20 22 LYS CB C 31.901 0.3 1 73 20 22 LYS N N 116.842 0.3 1 74 21 23 ALA H H 7.466 0.025 1 75 21 23 ALA CA C 54.867 0.3 1 76 21 23 ALA CB C 17.853 0.3 1 77 21 23 ALA N N 120.6 0.3 1 78 22 24 ILE H H 7.244 0.025 1 79 22 24 ILE CA C 61.105 0.3 1 80 22 24 ILE CB C 37.234 0.3 1 81 22 24 ILE N N 108.784 0.3 1 82 23 25 GLY H H 7.466 0.025 1 83 23 25 GLY CA C 45.525 0.3 1 84 23 25 GLY N N 106.136 0.3 1 85 24 26 LEU H H 7.647 0.025 1 86 24 26 LEU CA C 53.535 0.3 1 87 24 26 LEU CB C 42.087 0.3 1 88 24 26 LEU N N 121.442 0.3 1 89 25 27 PRO CA C 62.878 0.3 1 90 25 27 PRO CB C 32.397 0.3 1 91 26 28 GLU H H 8.728 0.025 1 92 26 28 GLU CA C 59.982 0.3 1 93 26 28 GLU CB C 29.506 0.3 1 94 26 28 GLU N N 121.564 0.3 1 95 27 29 GLU H H 9.275 0.025 1 96 27 29 GLU CA C 59.589 0.3 1 97 27 29 GLU CB C 28.738 0.3 1 98 27 29 GLU N N 115.034 0.3 1 99 28 30 LEU H H 7.191 0.025 1 100 28 30 LEU CA C 56.855 0.3 1 101 28 30 LEU CB C 41.303 0.3 1 102 28 30 LEU N N 115.52 0.3 1 103 29 31 ILE H H 7.72 0.025 1 104 29 31 ILE CA C 65.862 0.3 1 105 29 31 ILE CB C 32.904 0.3 9 106 29 31 ILE N N 119.873 0.3 1 107 30 32 GLN H H 8.161 0.025 1 108 30 32 GLN CA C 58.457 0.3 1 109 30 32 GLN CB C 28.149 0.3 1 110 30 32 GLN N N 114.372 0.3 1 111 31 33 LYS H H 7.467 0.025 1 112 31 33 LYS CA C 58.337 0.3 1 113 31 33 LYS CB C 32.878 0.3 1 114 31 33 LYS N N 114.265 0.3 1 115 32 34 GLY H H 7.886 0.025 1 116 32 34 GLY CA C 45.988 0.3 1 117 32 34 GLY N N 103.045 0.3 1 118 33 35 LYS H H 7.436 0.025 1 119 33 35 LYS CA C 58.303 0.3 1 120 33 35 LYS CB C 32.224 0.3 1 121 33 35 LYS N N 116.396 0.3 1 122 34 36 ASP H H 7.662 0.025 1 123 34 36 ASP CA C 54.322 0.3 1 124 34 36 ASP CB C 41.185 0.3 1 125 34 36 ASP N N 115.817 0.3 1 126 35 37 ILE H H 7.336 0.025 1 127 35 37 ILE CA C 61.169 0.3 1 128 35 37 ILE CB C 37.496 0.3 1 129 35 37 ILE N N 117.923 0.3 1 130 36 38 LYS H H 8.306 0.025 1 131 36 38 LYS CA C 55.487 0.3 1 132 36 38 LYS CB C 32.887 0.3 1 133 36 38 LYS N N 124.621 0.3 1 134 37 39 GLY H H 7.996 0.025 1 135 37 39 GLY CA C 45.337 0.3 1 136 37 39 GLY N N 108.375 0.3 1 137 38 40 VAL H H 7.925 0.025 1 138 38 40 VAL CA C 60.963 0.3 1 139 38 40 VAL CB C 34.983 0.3 1 140 38 40 VAL N N 116.966 0.3 1 141 39 41 SER H H 9.118 0.025 1 142 39 41 SER CA C 56.897 0.3 1 143 39 41 SER CB C 66.761 0.3 1 144 39 41 SER N N 121.086 0.3 1 145 40 42 GLU H H 9.406 0.025 1 146 40 42 GLU CA C 55.094 0.3 1 147 40 42 GLU CB C 33.366 0.3 1 148 40 42 GLU N N 121.28 0.3 1 149 41 43 ILE H H 9.331 0.025 1 150 41 43 ILE CA C 59.993 0.3 1 151 41 43 ILE CB C 39.854 0.3 1 152 41 43 ILE N N 122.898 0.3 1 153 42 44 VAL H H 9.076 0.025 1 154 42 44 VAL CA C 62.417 0.3 1 155 42 44 VAL CB C 33.824 0.3 1 156 42 44 VAL N N 125.936 0.3 1 157 43 45 GLN H H 8.639 0.025 1 158 43 45 GLN CA C 53.787 0.3 1 159 43 45 GLN CB C 29.957 0.3 1 160 43 45 GLN N N 128.715 0.3 1 161 44 46 ASN H H 8.838 0.025 1 162 44 46 ASN CA C 52.226 0.3 1 163 44 46 ASN CB C 39.312 0.3 1 164 44 46 ASN N N 124.358 0.3 1 165 45 47 GLY H H 9.096 0.025 1 166 45 47 GLY CA C 47.484 0.3 1 167 45 47 GLY N N 113.721 0.3 1 168 46 48 LYS H H 8.719 0.025 1 169 46 48 LYS CA C 56.466 0.3 1 170 46 48 LYS CB C 33.379 0.3 1 171 46 48 LYS N N 123.504 0.3 1 172 47 49 HIS H H 8.096 0.025 1 173 47 49 HIS CA C 55.312 0.3 1 174 47 49 HIS CB C 30.143 0.3 1 175 47 49 HIS N N 117.162 0.3 1 176 48 50 PHE H H 8.689 0.025 1 177 48 50 PHE CA C 56.863 0.3 1 178 48 50 PHE CB C 43.978 0.3 1 179 48 50 PHE N N 122.317 0.3 1 180 49 51 LYS H H 8.398 0.025 1 181 49 51 LYS CA C 55.497 0.3 1 182 49 51 LYS CB C 35.777 0.3 1 183 49 51 LYS N N 116.845 0.3 1 184 50 52 PHE H H 9.437 0.025 1 185 50 52 PHE CA C 56.869 0.3 1 186 50 52 PHE CB C 43.502 0.3 1 187 50 52 PHE N N 124.116 0.3 1 188 51 53 THR H H 9.429 0.025 1 189 51 53 THR CA C 62.729 0.3 1 190 51 53 THR CB C 69.869 0.3 9 191 51 53 THR N N 119.388 0.3 1 192 52 54 ILE CA C 60.51 0.3 1 193 52 54 ILE CB C 42.29 0.3 9 194 53 55 THR H H 8.622 0.025 1 195 53 55 THR CA C 62.129 0.3 1 196 53 55 THR CB C 69.189 0.3 1 197 53 55 THR N N 119.752 0.3 1 198 54 56 ALA H H 8.655 0.025 1 199 54 56 ALA CA C 50.817 0.3 1 200 54 56 ALA CB C 19.607 0.3 1 201 54 56 ALA N N 127.996 0.3 1 202 55 57 GLY H H 8.802 0.025 1 203 55 57 GLY CA C 47.105 0.3 1 204 55 57 GLY N N 111.641 0.3 1 205 56 58 SER H H 8.696 0.025 1 206 56 58 SER CA C 58.632 0.3 1 207 56 58 SER CB C 63.299 0.3 1 208 56 58 SER N N 118.547 0.3 1 209 57 59 ALA H H 7.833 0.025 1 210 57 59 ALA CA C 51.605 0.3 1 211 57 59 ALA CB C 20.668 0.3 1 212 57 59 ALA N N 123.21 0.3 1 213 58 60 VAL H H 8.116 0.025 1 214 58 60 VAL CA C 61.576 0.3 1 215 58 60 VAL CB C 33.115 0.3 1 216 58 60 VAL N N 118.553 0.3 1 217 59 61 ILE H H 9.102 0.025 1 218 59 61 ILE CA C 60.335 0.3 1 219 59 61 ILE CB C 40.57 0.3 1 220 59 61 ILE N N 124.776 0.3 1 221 60 62 GLN H H 8.919 0.025 1 222 60 62 GLN CA C 54.506 0.3 1 223 60 62 GLN CB C 31.618 0.3 1 224 60 62 GLN N N 125.806 0.3 1 225 61 63 ASN H H 8.826 0.025 1 226 61 63 ASN CA C 52.954 0.3 1 227 61 63 ASN CB C 45.47 0.3 1 228 61 63 ASN N N 117.955 0.3 1 229 62 64 GLU H H 8.944 0.025 1 230 62 64 GLU CA C 55.13 0.3 1 231 62 64 GLU CB C 33.343 0.3 1 232 62 64 GLU N N 118.909 0.3 1 233 63 65 PHE H H 8.18 0.025 1 234 63 65 PHE CA C 56.514 0.3 1 235 63 65 PHE CB C 41.138 0.3 1 236 63 65 PHE N N 114.15 0.3 1 237 64 66 THR H H 9.176 0.025 1 238 64 66 THR CA C 61.069 0.3 1 239 64 66 THR CB C 70.414 0.3 1 240 64 66 THR N N 116.247 0.3 1 241 65 67 VAL H H 9.043 0.025 1 242 65 67 VAL CA C 64.285 0.3 1 243 65 67 VAL CB C 31.688 0.3 1 244 65 67 VAL N N 123.025 0.3 1 245 66 68 GLY H H 8.869 0.025 1 246 66 68 GLY CA C 45.523 0.3 1 247 66 68 GLY N N 107.641 0.3 1 248 67 69 GLU H H 7.722 0.025 1 249 67 69 GLU CA C 54.184 0.3 1 250 67 69 GLU CB C 31.679 0.3 1 251 67 69 GLU N N 116.9 0.3 1 252 68 70 GLU H H 8.923 0.025 1 253 68 70 GLU CA C 58.063 0.3 1 254 68 70 GLU CB C 29.792 0.3 1 255 68 70 GLU N N 123.63 0.3 1 256 69 71 CYS H H 9.127 0.025 1 257 69 71 CYS CA C 55.387 0.3 1 258 69 71 CYS CB C 31.767 0.3 1 259 69 71 CYS N N 119.028 0.3 1 260 70 72 GLU H H 8.345 0.025 1 261 70 72 GLU CA C 55.079 0.3 1 262 70 72 GLU CB C 31.544 0.3 1 263 70 72 GLU N N 117.699 0.3 1 264 71 73 LEU H H 8.884 0.025 1 265 71 73 LEU CA C 52.787 0.3 1 266 71 73 LEU CB C 44.033 0.3 1 267 71 73 LEU N N 123.509 0.3 1 268 72 74 GLU H H 9.535 0.025 1 269 72 74 GLU CA C 55.297 0.3 1 270 72 74 GLU CB C 30.441 0.3 1 271 72 74 GLU N N 121.436 0.3 1 272 73 75 THR H H 8.191 0.025 1 273 73 75 THR CA C 60.057 0.3 1 274 73 75 THR CB C 71.932 0.3 1 275 73 75 THR N N 109.948 0.3 1 276 74 76 MET H H 9.521 0.025 1 277 74 76 MET CA C 58.358 0.3 1 278 74 76 MET CB C 33.817 0.3 1 279 74 76 MET N N 114.016 0.3 1 280 75 77 THR H H 7.416 0.025 1 281 75 77 THR CA C 61.461 0.3 1 282 75 77 THR CB C 68.56 0.3 1 283 75 77 THR N N 102.08 0.3 1 284 76 78 GLY H H 7.816 0.025 1 285 76 78 GLY CA C 45.133 0.3 1 286 76 78 GLY N N 108.368 0.3 1 287 77 79 ALA H H 7.175 0.025 1 288 77 79 ALA CA C 51.429 0.3 1 289 77 79 ALA CB C 19.327 0.3 1 290 77 79 ALA N N 120.387 0.3 1 291 78 80 LYS H H 8.282 0.025 1 292 78 80 LYS CA C 54.861 0.3 1 293 78 80 LYS CB C 33.881 0.3 1 294 78 80 LYS N N 118.218 0.3 1 295 79 81 VAL H H 8.899 0.025 1 296 79 81 VAL CA C 59.891 0.3 1 297 79 81 VAL CB C 34.941 0.3 1 298 79 81 VAL N N 118.239 0.3 1 299 80 82 LYS H H 8.394 0.025 1 300 80 82 LYS CA C 55.291 0.3 1 301 80 82 LYS CB C 32.932 0.3 1 302 80 82 LYS N N 123.508 0.3 1 303 81 83 THR H H 8.711 0.025 1 304 81 83 THR CA C 59.252 0.3 1 305 81 83 THR CB C 68.878 0.3 1 306 81 83 THR N N 117.766 0.3 1 307 82 84 VAL H H 8.075 0.025 1 308 82 84 VAL CA C 61.38 0.3 1 309 82 84 VAL CB C 35.279 0.3 1 310 82 84 VAL N N 116.963 0.3 1 311 83 85 VAL H H 9.689 0.025 1 312 83 85 VAL CA C 61.295 0.3 1 313 83 85 VAL CB C 32.037 0.3 1 314 83 85 VAL N N 131.137 0.3 1 315 84 86 GLN H H 8.875 0.025 1 316 84 86 GLN CA C 53.831 0.3 1 317 84 86 GLN CB C 31.084 0.3 1 318 84 86 GLN N N 122.409 0.3 1 319 85 87 LEU H H 8.419 0.025 1 320 85 87 LEU CA C 54.114 0.3 1 321 85 87 LEU CB C 44.4 0.3 1 322 85 87 LEU N N 121.203 0.3 1 323 86 88 GLU H H 9.032 0.025 1 324 86 88 GLU CA C 55.365 0.3 1 325 86 88 GLU CB C 31.396 0.3 1 326 86 88 GLU N N 126.022 0.3 1 327 87 89 GLY H H 8.362 0.025 1 328 87 89 GLY CA C 45.937 0.3 1 329 87 89 GLY N N 110.303 0.3 1 330 88 90 ASP H H 8.454 0.025 1 331 88 90 ASP CA C 54.681 0.3 1 332 88 90 ASP CB C 41.584 0.3 1 333 88 90 ASP N N 115.516 0.3 1 334 89 91 ASN H H 8.18 0.025 1 335 89 91 ASN CA C 53.459 0.3 1 336 89 91 ASN CB C 39.617 0.3 1 337 89 91 ASN N N 112.065 0.3 1 338 90 92 LYS H H 7.456 0.025 1 339 90 92 LYS CA C 55.293 0.3 1 340 90 92 LYS CB C 35.79 0.3 1 341 90 92 LYS N N 116.197 0.3 1 342 91 93 LEU H H 9.033 0.025 1 343 91 93 LEU CA C 52.757 0.3 1 344 91 93 LEU CB C 43.979 0.3 1 345 91 93 LEU N N 121.692 0.3 1 346 92 94 VAL H H 9.215 0.025 1 347 92 94 VAL CA C 60.611 0.3 1 348 92 94 VAL CB C 35.291 0.3 1 349 92 94 VAL N N 120.131 0.3 1 350 93 95 THR H H 8.786 0.025 1 351 93 95 THR CA C 60.776 0.3 1 352 93 95 THR CB C 69.161 0.3 1 353 93 95 THR N N 118.056 0.3 1 354 94 96 THR H H 7.95 0.025 1 355 94 96 THR CA C 59.609 0.3 1 356 94 96 THR CB C 71.33 0.3 1 357 94 96 THR N N 112.481 0.3 1 358 95 97 PHE H H 8.68 0.025 1 359 95 97 PHE CA C 55.903 0.3 1 360 95 97 PHE CB C 40.096 0.3 9 361 95 97 PHE N N 119.748 0.3 1 362 96 98 ALA CA C 54.064 0.3 1 363 96 98 ALA CB C 16.552 0.3 1 364 97 99 ASN H H 8.451 0.025 1 365 97 99 ASN CA C 54.321 0.3 1 366 97 99 ASN CB C 37.673 0.3 1 367 97 99 ASN N N 113.402 0.3 1 368 98 100 ILE H H 8.285 0.025 1 369 98 100 ILE CA C 61.081 0.3 1 370 98 100 ILE CB C 39.405 0.3 1 371 98 100 ILE N N 119.653 0.3 1 372 99 101 LYS H H 8.199 0.025 1 373 99 101 LYS CA C 55.884 0.3 1 374 99 101 LYS CB C 33.66 0.3 1 375 99 101 LYS N N 125.689 0.3 1 376 100 102 SER H H 8.645 0.025 1 377 100 102 SER CA C 57.049 0.3 1 378 100 102 SER CB C 65.321 0.3 1 379 100 102 SER N N 117.421 0.3 1 380 101 103 VAL H H 8.741 0.025 1 381 101 103 VAL CA C 61.552 0.3 1 382 101 103 VAL CB C 34.8 0.3 1 383 101 103 VAL N N 126.411 0.3 1 384 102 104 THR H H 9.586 0.025 1 385 102 104 THR CA C 61.947 0.3 1 386 102 104 THR CB C 69.852 0.3 1 387 102 104 THR N N 127.503 0.3 1 388 103 105 GLU H H 9.141 0.025 1 389 103 105 GLU CA C 54.519 0.3 1 390 103 105 GLU CB C 33.775 0.3 1 391 103 105 GLU N N 124.668 0.3 1 392 104 106 LEU H H 8.509 0.025 1 393 104 106 LEU CA C 53.926 0.3 1 394 104 106 LEU CB C 45.3 0.3 1 395 104 106 LEU N N 126.833 0.3 1 396 105 107 ASN H H 8.927 0.025 1 397 105 107 ASN CA C 52.568 0.3 1 398 105 107 ASN CB C 40.109 0.3 1 399 105 107 ASN N N 123.958 0.3 1 400 106 108 GLY H H 8.755 0.025 1 401 106 108 GLY CA C 47.859 0.3 1 402 106 108 GLY N N 112.847 0.3 1 403 107 109 ASP H H 8.736 0.025 1 404 107 109 ASP CA C 53.833 0.3 1 405 107 109 ASP CB C 41.653 0.3 1 406 107 109 ASP N N 124.352 0.3 1 407 108 110 ILE H H 7.789 0.025 1 408 108 110 ILE CA C 58.82 0.3 1 409 108 110 ILE CB C 39.31 0.3 1 410 108 110 ILE N N 117.21 0.3 1 411 109 111 ILE H H 8.903 0.025 1 412 109 111 ILE CA C 58.618 0.3 1 413 109 111 ILE CB C 41.368 0.3 1 414 109 111 ILE N N 125.704 0.3 1 415 110 112 THR H H 8.874 0.025 1 416 110 112 THR CA C 60.28 0.3 1 417 110 112 THR CB C 70.655 0.3 1 418 110 112 THR N N 118.904 0.3 1 419 111 113 ASN H H 9.116 0.025 1 420 111 113 ASN CA C 52.561 0.3 1 421 111 113 ASN CB C 43.161 0.3 1 422 111 113 ASN N N 122.776 0.3 1 423 112 114 THR H H 9.198 0.025 1 424 112 114 THR CA C 61.736 0.3 1 425 112 114 THR CB C 69.761 0.3 1 426 112 114 THR N N 121.323 0.3 1 427 113 115 MET H H 9.136 0.025 1 428 113 115 MET CA C 54.363 0.3 1 429 113 115 MET CB C 37.215 0.3 1 430 113 115 MET N N 125.472 0.3 1 431 114 116 THR H H 8.553 0.025 1 432 114 116 THR CA C 61.18 0.3 1 433 114 116 THR CB C 70.63 0.3 1 434 114 116 THR N N 114.548 0.3 1 435 115 117 LEU H H 8.818 0.025 1 436 115 117 LEU CA C 53.996 0.3 1 437 115 117 LEU CB C 44.501 0.3 1 438 115 117 LEU N N 126.773 0.3 1 439 116 118 GLY H H 9.069 0.025 1 440 116 118 GLY CA C 47.489 0.3 1 441 116 118 GLY N N 115.264 0.3 1 442 117 119 ASP H H 8.606 0.025 1 443 117 119 ASP CA C 54.04 0.3 1 444 117 119 ASP CB C 40.699 0.3 1 445 117 119 ASP N N 123.99 0.3 1 446 118 120 ILE H H 8.351 0.025 1 447 118 120 ILE CA C 61.937 0.3 1 448 118 120 ILE CB C 38.03 0.3 1 449 118 120 ILE N N 120.115 0.3 1 450 119 121 VAL H H 8.296 0.025 1 451 119 121 VAL CA C 61.356 0.3 1 452 119 121 VAL CB C 32.396 0.3 1 453 119 121 VAL N N 124.949 0.3 1 454 120 122 PHE H H 9.209 0.025 1 455 120 122 PHE CA C 53.824 0.3 1 456 120 122 PHE CB C 40.787 0.3 1 457 120 122 PHE N N 128.233 0.3 1 458 121 123 LYS H H 8.306 0.025 1 459 121 123 LYS CA C 54.306 0.3 1 460 121 123 LYS CB C 36.998 0.3 1 461 121 123 LYS N N 127.436 0.3 1 462 122 124 ARG H H 8.574 0.025 1 463 122 124 ARG CA C 55.208 0.3 1 464 122 124 ARG CB C 30.093 0.3 9 465 122 124 ARG N N 121.448 0.3 1 466 123 125 ILE H H 8.687 0.025 1 467 123 125 ILE CA C 61.43 0.3 1 468 123 125 ILE CB C 39.968 0.3 1 469 123 125 ILE N N 122.516 0.3 1 470 124 126 SER H H 9.112 0.025 1 471 124 126 SER CA C 58.49 0.3 9 472 124 126 SER CB C 63.845 0.3 1 473 124 126 SER N N 121.195 0.3 1 474 125 127 LYS H H 8.48 0.025 1 475 125 127 LYS CA C 55.307 0.3 1 476 125 127 LYS CB C 37.163 0.3 1 477 125 127 LYS N N 119.995 0.3 1 478 126 128 ARG H H 9.018 0.025 1 479 126 128 ARG CA C 57.277 0.3 1 480 126 128 ARG CB C 30.901 0.3 1 481 126 128 ARG N N 126.038 0.3 1 482 127 129 ILE H H 8.343 0.025 1 483 127 129 ILE CA C 62.907 0.3 1 484 127 129 ILE CB C 39.991 0.3 1 485 127 129 ILE N N 127.428 0.3 1 stop_ save_