data_27509 ####################### # 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) ; _BMRB_accession_number 27509 _BMRB_flat_file_name bmr27509.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" 123 "13C chemical shifts" 241 "15N chemical shifts" 123 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 27510 '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 NMR 'Nuclear hormone receptor signalling' PPAR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Apo hFABP1 mutant (K57A, E77A, K96A)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label polypeptide $Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant stop_ _System_molecular_weight 14180.3 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Fatty acid binding and transport' stop_ _Database_query_date . _Details 'Apo FABP1 mutant (K57A, E77A, K96A)' 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; 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 $Human_liver_fatty_acid_binding_protein_(hFABP1)_K57A_E77A_K96A_mutant 0.290 mM '[U-99% 13C; U-99% 15N]' MES 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' D2O 10 % '[U-100% 2H]' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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_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_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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _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 'The offset for Nitrogen can be corrected by - 0.9 ppm.' loop_ _Software_label $CARA_1.2 $TOPSPIN $MddNMR stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '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 polypeptide _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 3 MET H H 8.485 0.025 1 2 1 3 MET CA C 55.302 0.3 1 3 1 3 MET CB C 33.604 0.3 1 4 1 3 MET N N 120.119 0.2 1 5 2 4 SER H H 8.191 0.025 1 6 2 4 SER CA C 57.102 0.3 1 7 2 4 SER CB C 64.737 0.3 1 8 2 4 SER N N 114.353 0.2 1 9 3 5 PHE H H 9.568 0.025 1 10 3 5 PHE CA C 59.859 0.3 1 11 3 5 PHE CB C 41.29 0.3 1 12 3 5 PHE N N 120.356 0.2 1 13 4 6 SER H H 8.297 0.025 1 14 4 6 SER CA C 60.114 0.3 1 15 4 6 SER CB C 63.811 0.3 1 16 4 6 SER N N 113.888 0.2 1 17 5 7 GLY H H 8.959 0.025 1 18 5 7 GLY CA C 44.938 0.3 1 19 5 7 GLY N N 108.807 0.2 1 20 6 8 LYS H H 8.206 0.025 1 21 6 8 LYS CA C 54.986 0.3 1 22 6 8 LYS CB C 35.196 0.3 1 23 6 8 LYS N N 117.752 0.2 1 24 7 9 TYR H H 9.181 0.025 1 25 7 9 TYR CA C 56.051 0.3 1 26 7 9 TYR CB C 42.01 0.3 1 27 7 9 TYR N N 117.283 0.2 1 28 8 10 GLN H H 9.21 0.025 1 29 8 10 GLN CA C 54.414 0.3 1 30 8 10 GLN CB C 31.246 0.3 1 31 8 10 GLN N N 122.195 0.2 1 32 9 11 LEU H H 8.599 0.025 1 33 9 11 LEU CA C 57.613 0.3 1 34 9 11 LEU CB C 43.155 0.3 1 35 9 11 LEU N N 129.978 0.2 1 36 10 12 GLN H H 10.071 0.025 1 37 10 12 GLN CA C 56.248 0.3 1 38 10 12 GLN CB C 31.963 0.3 1 39 10 12 GLN N N 123.578 0.2 1 40 11 13 SER H H 7.96 0.025 1 41 11 13 SER CA C 57.55 0.3 1 42 11 13 SER CB C 64.962 0.3 1 43 11 13 SER N N 108.573 0.2 1 44 12 14 GLN H H 8.534 0.025 1 45 12 14 GLN CA C 54.239 0.3 1 46 12 14 GLN CB C 32.876 0.3 1 47 12 14 GLN N N 114.457 0.2 1 48 13 15 GLU H H 9.11 0.025 1 49 13 15 GLU CA C 55.162 0.3 1 50 13 15 GLU CB C 33.972 0.3 1 51 13 15 GLU N N 118.776 0.2 1 52 14 16 ASN H H 9.215 0.025 1 53 14 16 ASN CA C 54.513 0.3 1 54 14 16 ASN CB C 36.179 0.3 1 55 14 16 ASN N N 114.742 0.2 1 56 15 17 PHE H H 8.387 0.025 1 57 15 17 PHE CA C 62.328 0.3 1 58 15 17 PHE CB C 40.38 0.3 1 59 15 17 PHE N N 115.808 0.2 1 60 16 18 GLU H H 9.407 0.025 1 61 16 18 GLU CA C 61.264 0.3 1 62 16 18 GLU CB C 29.115 0.3 1 63 16 18 GLU N N 115.929 0.2 1 64 17 19 ALA H H 8.2 0.025 1 65 17 19 ALA CA C 54.809 0.3 1 66 17 19 ALA CB C 18.816 0.3 1 67 17 19 ALA N N 117.262 0.2 1 68 18 20 PHE H H 7.804 0.025 1 69 18 20 PHE CA C 62.124 0.3 1 70 18 20 PHE CB C 40.385 0.3 1 71 18 20 PHE N N 116.11 0.2 1 72 19 21 MET H H 8.122 0.025 1 73 19 21 MET CA C 56.091 0.3 1 74 19 21 MET CB C 31.502 0.3 1 75 19 21 MET N N 112.249 0.2 1 76 20 22 LYS H H 8.081 0.025 1 77 20 22 LYS CA C 59.215 0.3 1 78 20 22 LYS CB C 32.616 0.3 1 79 20 22 LYS N N 116.659 0.2 1 80 21 23 ALA H H 7.452 0.025 1 81 21 23 ALA CA C 54.814 0.3 1 82 21 23 ALA CB C 18.593 0.3 1 83 21 23 ALA N N 120.7 0.2 1 84 22 24 ILE H H 7.329 0.025 1 85 22 24 ILE CA C 61.557 0.3 1 86 22 24 ILE CB C 38.066 0.3 1 87 22 24 ILE N N 107.976 0.2 1 88 23 25 GLY H H 7.399 0.025 1 89 23 25 GLY CA C 45.644 0.3 1 90 23 25 GLY N N 106.007 0.2 1 91 24 26 LEU H H 7.76 0.025 1 92 24 26 LEU CA C 53.707 0.3 1 93 24 26 LEU CB C 42.29 0.3 1 94 24 26 LEU N N 121.933 0.2 1 95 25 27 PRO CA C 62.679 0.3 1 96 25 27 PRO CB C 32.443 0.3 1 97 26 28 GLU H H 8.721 0.025 1 98 26 28 GLU CA C 60.037 0.3 1 99 26 28 GLU CB C 30.014 0.3 1 100 26 28 GLU N N 121.627 0.2 1 101 27 29 GLU H H 9.291 0.025 1 102 27 29 GLU CA C 59.776 0.3 1 103 27 29 GLU CB C 28.907 0.3 1 104 27 29 GLU N N 115.085 0.2 1 105 28 30 LEU H H 7.153 0.025 1 106 28 30 LEU CA C 56.855 0.3 1 107 28 30 LEU CB C 41.751 0.3 1 108 28 30 LEU N N 115.473 0.2 1 109 29 31 ILE H H 7.768 0.025 1 110 29 31 ILE CA C 66.132 0.3 1 111 29 31 ILE CB C 38.086 0.3 1 112 29 31 ILE N N 120.777 0.2 1 113 30 32 GLN H H 8.182 0.025 1 114 30 32 GLN CA C 58.611 0.3 1 115 30 32 GLN CB C 28.379 0.3 1 116 30 32 GLN N N 114.43 0.2 1 117 31 33 LYS H H 7.46 0.025 1 118 31 33 LYS CA C 58.328 0.3 1 119 31 33 LYS CB C 33.349 0.3 1 120 31 33 LYS N N 113.752 0.2 1 121 32 34 GLY H H 7.842 0.025 1 122 32 34 GLY CA C 45.944 0.3 1 123 32 34 GLY N N 102.981 0.2 1 124 33 35 LYS H H 7.431 0.025 1 125 33 35 LYS CA C 58.812 0.3 1 126 33 35 LYS CB C 32.415 0.3 1 127 33 35 LYS N N 117.182 0.2 1 128 34 36 ASP H H 7.717 0.025 1 129 34 36 ASP CA C 54.125 0.3 1 130 34 36 ASP CB C 41.796 0.3 1 131 34 36 ASP N N 114.902 0.2 1 132 35 37 ILE H H 7.097 0.025 1 133 35 37 ILE CA C 61.166 0.3 1 134 35 37 ILE CB C 38.273 0.3 1 135 35 37 ILE N N 117.879 0.2 1 136 36 38 LYS H H 8.574 0.025 1 137 36 38 LYS CA C 55.12 0.3 1 138 36 38 LYS CB C 32.34 0.3 1 139 36 38 LYS N N 126.16 0.2 1 140 37 39 GLY H H 7.839 0.025 1 141 37 39 GLY CA C 45.341 0.3 1 142 37 39 GLY N N 108.84 0.2 1 143 38 40 VAL H H 8.331 0.025 1 144 38 40 VAL CA C 61.054 0.3 1 145 38 40 VAL CB C 34.182 0.3 1 146 38 40 VAL N N 118.239 0.2 1 147 39 41 SER H H 9.243 0.025 1 148 39 41 SER CA C 57.257 0.3 1 149 39 41 SER CB C 65.192 0.3 1 150 39 41 SER N N 119.515 0.2 1 151 40 42 GLU H H 9.43 0.025 1 152 40 42 GLU CA C 55.097 0.3 1 153 40 42 GLU CB C 31.951 0.3 1 154 40 42 GLU N N 123.385 0.2 1 155 41 43 ILE H H 9.371 0.025 1 156 41 43 ILE CA C 60.105 0.3 1 157 41 43 ILE CB C 40.393 0.3 1 158 41 43 ILE N N 123.999 0.2 1 159 42 44 VAL H H 9.03 0.025 1 160 42 44 VAL CA C 62.34 0.3 1 161 42 44 VAL CB C 34.396 0.3 1 162 42 44 VAL N N 126.167 0.2 1 163 43 45 GLN H H 8.531 0.025 1 164 43 45 GLN CA C 53.749 0.3 1 165 43 45 GLN CB C 30.161 0.3 1 166 43 45 GLN N N 128.559 0.2 1 167 44 46 ASN H H 8.839 0.025 1 168 44 46 ASN CA C 52.366 0.3 1 169 44 46 ASN CB C 39.455 0.3 1 170 44 46 ASN N N 124.411 0.2 1 171 45 47 GLY H H 9.103 0.025 1 172 45 47 GLY CA C 47.568 0.3 1 173 45 47 GLY N N 113.916 0.2 1 174 46 48 LYS H H 8.751 0.025 1 175 46 48 LYS CA C 56.482 0.3 1 176 46 48 LYS CB C 33.348 0.3 1 177 46 48 LYS N N 123.567 0.2 1 178 47 49 HIS H H 8.144 0.025 1 179 47 49 HIS CA C 55.511 0.3 1 180 47 49 HIS CB C 30.045 0.3 1 181 47 49 HIS N N 117.504 0.2 1 182 48 50 PHE H H 8.789 0.025 1 183 48 50 PHE CA C 56.934 0.3 1 184 48 50 PHE CB C 43.837 0.3 1 185 48 50 PHE N N 122.616 0.2 1 186 49 51 LYS H H 8.337 0.025 1 187 49 51 LYS CA C 55.865 0.3 1 188 49 51 LYS CB C 35.485 0.3 1 189 49 51 LYS N N 117.121 0.2 1 190 50 52 PHE H H 9.475 0.025 1 191 50 52 PHE CA C 56.236 0.3 1 192 50 52 PHE CB C 43.083 0.3 1 193 50 52 PHE N N 125.258 0.2 1 194 51 53 THR H H 9.27 0.025 1 195 51 53 THR CA C 62.593 0.3 1 196 51 53 THR CB C 70.331 0.3 1 197 51 53 THR N N 118.913 0.2 1 198 52 54 ILE H H 9.398 0.025 1 199 52 54 ILE CA C 60.253 0.3 1 200 52 54 ILE CB C 41.186 0.3 1 201 52 54 ILE N N 126.269 0.2 1 202 53 55 THR H H 8.631 0.025 1 203 53 55 THR CA C 61.689 0.3 1 204 53 55 THR CB C 69.872 0.3 1 205 53 55 THR N N 119.713 0.2 1 206 54 56 ALA H H 8.737 0.025 1 207 54 56 ALA CA C 50.932 0.3 1 208 54 56 ALA CB C 19.786 0.3 1 209 54 56 ALA N N 128.714 0.2 1 210 55 57 GLY H H 8.876 0.025 1 211 55 57 GLY CA C 47.086 0.3 1 212 55 57 GLY N N 112.464 0.2 1 213 56 58 SER H H 8.742 0.025 1 214 56 58 SER CA C 58.809 0.3 1 215 56 58 SER CB C 63.741 0.3 1 216 56 58 SER N N 118.952 0.2 1 217 57 59 ALA H H 7.796 0.025 1 218 57 59 ALA CA C 51.775 0.3 1 219 57 59 ALA CB C 21.156 0.3 1 220 57 59 ALA N N 123.439 0.2 1 221 58 60 VAL H H 8.176 0.025 1 222 58 60 VAL CA C 61.369 0.3 1 223 58 60 VAL CB C 34.304 0.3 1 224 58 60 VAL N N 119.645 0.2 1 225 59 61 ILE H H 9.04 0.025 1 226 59 61 ILE CA C 60.26 0.3 9 227 59 61 ILE CB C 40.89 0.3 9 228 59 61 ILE N N 126.183 0.2 1 229 60 62 GLN H H 8.731 0.025 1 230 60 62 GLN CA C 53.917 0.3 1 231 60 62 GLN CB C 31.731 0.3 9 232 60 62 GLN N N 124.905 0.2 1 233 62 64 GLU H H 8.983 0.025 1 234 62 64 GLU CA C 55.141 0.3 1 235 62 64 GLU CB C 32.695 0.3 1 236 62 64 GLU N N 120.302 0.2 1 237 63 65 PHE H H 8.174 0.025 1 238 63 65 PHE CA C 56.414 0.3 1 239 63 65 PHE CB C 41.226 0.3 1 240 63 65 PHE N N 115.445 0.2 1 241 64 66 THR H H 9.147 0.025 1 242 64 66 THR CA C 60.969 0.3 1 243 64 66 THR CB C 70.375 0.3 1 244 64 66 THR N N 116.425 0.2 1 245 65 67 VAL H H 9.088 0.025 1 246 65 67 VAL CA C 64.389 0.3 1 247 65 67 VAL CB C 31.494 0.3 1 248 65 67 VAL N N 123.684 0.2 1 249 66 68 GLY H H 8.787 0.025 1 250 66 68 GLY CA C 45.532 0.3 1 251 66 68 GLY N N 107.826 0.2 1 252 67 69 GLU H H 7.78 0.025 1 253 67 69 GLU CA C 54.222 0.3 1 254 67 69 GLU CB C 32.156 0.3 1 255 67 69 GLU N N 117.024 0.2 1 256 68 70 GLU H H 8.917 0.025 1 257 68 70 GLU CA C 58.02 0.3 1 258 68 70 GLU CB C 30.509 0.3 1 259 68 70 GLU N N 123.287 0.2 1 260 69 71 CYS H H 9.205 0.025 1 261 69 71 CYS CA C 55.539 0.3 1 262 69 71 CYS CB C 31.975 0.3 1 263 69 71 CYS N N 119.453 0.2 1 264 70 72 GLU H H 8.384 0.025 1 265 70 72 GLU CA C 55.171 0.3 1 266 70 72 GLU CB C 31.815 0.3 1 267 70 72 GLU N N 117.479 0.2 1 268 71 73 LEU H H 8.77 0.025 1 269 71 73 LEU CA C 53.105 0.3 1 270 71 73 LEU CB C 44.632 0.3 1 271 71 73 LEU N N 123.503 0.2 1 272 72 74 GLU H H 9.264 0.025 1 273 72 74 GLU CA C 55.709 0.3 1 274 72 74 GLU CB C 30.53 0.3 1 275 72 74 GLU N N 121.338 0.2 1 276 73 75 THR H H 8.368 0.025 1 277 73 75 THR CA C 60.509 0.3 1 278 73 75 THR CB C 71.427 0.3 1 279 73 75 THR N N 112.4 0.2 1 280 74 76 MET H H 8.762 0.025 1 281 74 76 MET CA C 57.701 0.3 1 282 74 76 MET CB C 31.947 0.3 1 283 74 76 MET N N 114.535 0.2 1 284 75 77 THR H H 7.491 0.025 1 285 75 77 THR CA C 61.608 0.3 1 286 75 77 THR CB C 68.966 0.3 1 287 75 77 THR N N 103.07 0.2 1 288 76 78 GLY H H 7.805 0.025 1 289 76 78 GLY CA C 44.944 0.3 1 290 76 78 GLY N N 108.098 0.2 1 291 77 79 ALA H H 7.093 0.025 1 292 77 79 ALA CA C 51.599 0.3 1 293 77 79 ALA CB C 19.773 0.3 1 294 77 79 ALA N N 120.414 0.2 1 295 78 80 LYS H H 8.298 0.025 1 296 78 80 LYS CA C 55.017 0.3 1 297 78 80 LYS CB C 34.277 0.3 1 298 78 80 LYS N N 118.555 0.2 1 299 79 81 VAL H H 8.808 0.025 1 300 79 81 VAL CA C 59.579 0.3 1 301 79 81 VAL CB C 35.331 0.3 1 302 79 81 VAL N N 117.858 0.2 1 303 80 82 LYS H H 8.374 0.025 1 304 80 82 LYS CA C 55.352 0.3 1 305 80 82 LYS CB C 32.857 0.3 1 306 80 82 LYS N N 122.508 0.2 1 307 81 83 THR H H 8.823 0.025 1 308 81 83 THR CA C 59.558 0.3 1 309 81 83 THR CB C 69.418 0.3 1 310 81 83 THR N N 118.015 0.2 1 311 82 84 VAL H H 8.272 0.025 1 312 82 84 VAL CA C 61.335 0.3 1 313 82 84 VAL CB C 35.773 0.3 1 314 82 84 VAL N N 117.524 0.2 1 315 83 85 VAL H H 9.764 0.025 1 316 83 85 VAL CA C 61.159 0.3 1 317 83 85 VAL CB C 32.189 0.3 1 318 83 85 VAL N N 130.775 0.2 1 319 84 86 GLN H H 8.82 0.025 1 320 84 86 GLN CA C 53.743 0.3 1 321 84 86 GLN CB C 31.004 0.3 1 322 84 86 GLN N N 122.466 0.2 1 323 85 87 LEU H H 8.429 0.025 1 324 85 87 LEU CA C 54.054 0.3 1 325 85 87 LEU CB C 44.114 0.3 1 326 85 87 LEU N N 121.297 0.2 1 327 86 88 GLU H H 9.085 0.025 1 328 86 88 GLU CA C 55.356 0.3 1 329 86 88 GLU CB C 31.892 0.3 1 330 86 88 GLU N N 126.106 0.2 1 331 87 89 GLY H H 8.347 0.025 1 332 87 89 GLY CA C 45.911 0.3 1 333 87 89 GLY N N 110.198 0.2 1 334 88 90 ASP H H 8.441 0.025 1 335 88 90 ASP CA C 55.102 0.3 1 336 88 90 ASP CB C 42.225 0.3 1 337 88 90 ASP N N 115.578 0.2 1 338 89 91 ASN H H 8.16 0.025 1 339 89 91 ASN CA C 53.425 0.3 1 340 89 91 ASN CB C 40.149 0.3 1 341 89 91 ASN N N 112.052 0.2 1 342 90 92 LYS H H 7.444 0.025 1 343 90 92 LYS CA C 55.478 0.3 1 344 90 92 LYS CB C 36.324 0.3 1 345 90 92 LYS N N 116.545 0.2 1 346 91 93 LEU H H 9.018 0.025 1 347 91 93 LEU CA C 52.944 0.3 1 348 91 93 LEU CB C 44.863 0.3 1 349 91 93 LEU N N 122.467 0.2 1 350 92 94 VAL CA C 60.528 0.3 1 351 92 94 VAL CB C 35.198 0.3 1 352 93 95 THR H H 8.84 0.025 1 353 93 95 THR CA C 61.056 0.3 1 354 93 95 THR CB C 69.9 0.3 1 355 93 95 THR N N 118.723 0.2 1 356 94 96 THR H H 8.101 0.025 1 357 94 96 THR CA C 59.791 0.3 1 358 94 96 THR CB C 71.264 0.3 1 359 94 96 THR N N 115.385 0.2 1 360 95 97 PHE H H 8.397 0.025 1 361 95 97 PHE CA C 55.311 0.3 1 362 95 97 PHE CB C 39.903 0.3 1 363 95 97 PHE N N 119.206 0.2 1 364 96 98 ALA H H 9.082 0.025 1 365 96 98 ALA CA C 53.87 0.3 1 366 96 98 ALA CB C 17.296 0.3 1 367 96 98 ALA N N 122.662 0.2 1 368 97 99 ASN CA C 53.827 0.3 1 369 97 99 ASN CB C 37.461 0.3 1 370 98 100 ILE H H 8.367 0.025 1 371 98 100 ILE CA C 60.62 0.3 1 372 98 100 ILE CB C 39.678 0.3 1 373 98 100 ILE N N 119.913 0.2 1 374 99 101 LYS H H 8.097 0.025 1 375 99 101 LYS CA C 55.318 0.3 1 376 99 101 LYS CB C 34.298 0.3 1 377 99 101 LYS N N 124.57 0.2 1 378 100 102 SER H H 8.883 0.025 1 379 100 102 SER CA C 56.052 0.3 1 380 100 102 SER CB C 64.655 0.3 1 381 100 102 SER N N 119.082 0.2 1 382 101 103 VAL H H 8.887 0.025 1 383 101 103 VAL CA C 61.352 0.3 1 384 101 103 VAL CB C 35.273 0.3 1 385 101 103 VAL N N 126.044 0.2 1 386 102 104 THR H H 9.328 0.025 1 387 102 104 THR CA C 62.331 0.3 1 388 102 104 THR CB C 69.913 0.3 1 389 102 104 THR N N 125.322 0.2 1 390 103 105 GLU H H 9.129 0.025 1 391 103 105 GLU CA C 54.227 0.3 1 392 103 105 GLU CB C 34.754 0.3 1 393 103 105 GLU N N 125.449 0.2 1 394 104 106 LEU H H 8.452 0.025 1 395 104 106 LEU CA C 53.745 0.3 1 396 104 106 LEU CB C 45.521 0.3 1 397 104 106 LEU N N 126.135 0.2 1 398 105 107 ASN H H 8.901 0.025 1 399 105 107 ASN CA C 52.557 0.3 1 400 105 107 ASN CB C 40.407 0.3 1 401 105 107 ASN N N 123.927 0.2 1 402 106 108 GLY H H 8.835 0.025 1 403 106 108 GLY CA C 47.982 0.3 1 404 106 108 GLY N N 113.097 0.2 1 405 107 109 ASP H H 8.762 0.025 1 406 107 109 ASP CA C 53.829 0.3 1 407 107 109 ASP CB C 41.54 0.3 1 408 107 109 ASP N N 124.711 0.2 1 409 108 110 ILE H H 7.867 0.025 1 410 108 110 ILE CA C 58.726 0.3 1 411 108 110 ILE CB C 39.786 0.3 1 412 108 110 ILE N N 117.38 0.2 1 413 109 111 ILE H H 8.796 0.025 1 414 109 111 ILE CA C 58.616 0.3 1 415 109 111 ILE CB C 41.037 0.3 1 416 109 111 ILE N N 123.94 0.2 1 417 110 112 THR H H 8.969 0.025 1 418 110 112 THR CA C 61.039 0.3 1 419 110 112 THR CB C 69.913 0.3 1 420 110 112 THR N N 120.785 0.2 1 421 111 113 ASN H H 9.238 0.025 1 422 111 113 ASN CA C 51.852 0.3 1 423 111 113 ASN CB C 42.091 0.3 1 424 111 113 ASN N N 124.218 0.2 1 425 112 114 THR H H 9.208 0.025 1 426 112 114 THR CA C 61.559 0.3 1 427 112 114 THR CB C 69.7 0.3 1 428 112 114 THR N N 120.17 0.2 1 429 113 115 MET H H 9.201 0.025 1 430 113 115 MET CA C 54.323 0.3 1 431 113 115 MET CB C 37.077 0.3 1 432 113 115 MET N N 125.06 0.2 1 433 114 116 THR H H 8.817 0.025 1 434 114 116 THR CA C 61.46 0.3 1 435 114 116 THR CB C 70.656 0.3 1 436 114 116 THR N N 115.717 0.2 1 437 115 117 LEU H H 8.818 0.025 1 438 115 117 LEU CA C 54.03 0.3 1 439 115 117 LEU CB C 45.057 0.3 1 440 115 117 LEU N N 127.675 0.2 1 441 116 118 GLY H H 9.104 0.025 1 442 116 118 GLY CA C 47.476 0.3 1 443 116 118 GLY N N 115.329 0.2 1 444 117 119 ASP H H 8.582 0.025 1 445 117 119 ASP CA C 53.963 0.3 1 446 117 119 ASP CB C 41.279 0.3 1 447 117 119 ASP N N 123.934 0.2 1 448 118 120 ILE H H 8.349 0.025 1 449 118 120 ILE CA C 61.945 0.3 1 450 118 120 ILE CB C 39.353 0.3 1 451 118 120 ILE N N 120.248 0.2 1 452 119 121 VAL H H 8.297 0.025 1 453 119 121 VAL CA C 61.677 0.3 1 454 119 121 VAL CB C 32.443 0.3 1 455 119 121 VAL N N 125.022 0.2 1 456 120 122 PHE H H 9.261 0.025 1 457 120 122 PHE CA C 53.842 0.3 1 458 120 122 PHE CB C 41.202 0.3 1 459 120 122 PHE N N 129.016 0.2 1 460 121 123 LYS H H 8.126 0.025 1 461 121 123 LYS CA C 54.49 0.3 1 462 121 123 LYS CB C 37.123 0.3 1 463 121 123 LYS N N 127.175 0.2 1 464 122 124 ARG H H 8.703 0.025 1 465 122 124 ARG CA C 55.41 0.3 1 466 122 124 ARG CB C 34.665 0.3 1 467 122 124 ARG N N 121.202 0.2 1 468 123 125 ILE H H 8.743 0.025 1 469 123 125 ILE CA C 61.251 0.3 1 470 123 125 ILE CB C 39.419 0.3 1 471 123 125 ILE N N 123.692 0.2 1 472 124 126 SER H H 9.256 0.025 1 473 124 126 SER CA C 57.754 0.3 1 474 124 126 SER CB C 65.308 0.3 1 475 124 126 SER N N 120.417 0.2 1 476 125 127 LYS H H 8.625 0.025 1 477 125 127 LYS CA C 54.509 0.3 1 478 125 127 LYS CB C 36.772 0.3 1 479 125 127 LYS N N 121.616 0.2 1 480 126 128 ARG H H 9.114 0.025 1 481 126 128 ARG CA C 57.644 0.3 1 482 126 128 ARG CB C 31.748 0.3 1 483 126 128 ARG N N 127.426 0.2 1 484 127 129 ILE H H 8.387 0.025 1 485 127 129 ILE CA C 63.072 0.3 1 486 127 129 ILE CB C 40.577 0.3 1 487 127 129 ILE N N 127.804 0.2 1 stop_ save_