data_25333 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; BILE SALT RECOGNITION BY HUMAN LIVER FATTY ACID BINDING PROTEIN ; _BMRB_accession_number 25333 _BMRB_flat_file_name bmr25333.str _Entry_type original _Submission_date 2014-11-12 _Accession_date 2014-11-12 _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 Favretto Filippo . . 2 Santambrogio Carlo . . 3 D'Onofrio Mariapina . . 4 Molinari Henriette . . 5 Grandori Rita . . 6 Assfalg Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 130 "13C chemical shifts" 250 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-08-25 original BMRB . stop_ _Original_release_date 2015-08-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Bile salt recognition by human liver fatty acid binding protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25639618 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Favretto Filippo . . 2 Santambrogio Carlo . . 3 D'Onofrio Mariapina . . 4 Molinari Henriette . . 5 Grandori Rita . . 6 Assfalg Michael . . stop_ _Journal_abbreviation 'FEBS J.' _Journal_volume 282 _Journal_issue 287 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1271 _Page_last 1288 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hL-FABP:TCH _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human liver fatty acid binding protein' $hL-FABP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hL-FABP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hL-FABP _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; MRGSMSFSGKYQLQSQENFE AFMKAIGLPEELIQKGKDIK GVSEIVQNGKHFKFTITAGS KVIQNEFTVGEECELETMTG EKVKTVVQLEGDNKLVTAFK NIKSVTELNGDIITNTMTLG DIVFKRISKRILVPR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 MET 2 -2 ARG 3 -1 GLY 4 0 SER 5 1 MET 6 2 SER 7 3 PHE 8 4 SER 9 5 GLY 10 6 LYS 11 7 TYR 12 8 GLN 13 9 LEU 14 10 GLN 15 11 SER 16 12 GLN 17 13 GLU 18 14 ASN 19 15 PHE 20 16 GLU 21 17 ALA 22 18 PHE 23 19 MET 24 20 LYS 25 21 ALA 26 22 ILE 27 23 GLY 28 24 LEU 29 25 PRO 30 26 GLU 31 27 GLU 32 28 LEU 33 29 ILE 34 30 GLN 35 31 LYS 36 32 GLY 37 33 LYS 38 34 ASP 39 35 ILE 40 36 LYS 41 37 GLY 42 38 VAL 43 39 SER 44 40 GLU 45 41 ILE 46 42 VAL 47 43 GLN 48 44 ASN 49 45 GLY 50 46 LYS 51 47 HIS 52 48 PHE 53 49 LYS 54 50 PHE 55 51 THR 56 52 ILE 57 53 THR 58 54 ALA 59 55 GLY 60 56 SER 61 57 LYS 62 58 VAL 63 59 ILE 64 60 GLN 65 61 ASN 66 62 GLU 67 63 PHE 68 64 THR 69 65 VAL 70 66 GLY 71 67 GLU 72 68 GLU 73 69 CYS 74 70 GLU 75 71 LEU 76 72 GLU 77 73 THR 78 74 MET 79 75 THR 80 76 GLY 81 77 GLU 82 78 LYS 83 79 VAL 84 80 LYS 85 81 THR 86 82 VAL 87 83 VAL 88 84 GLN 89 85 LEU 90 86 GLU 91 87 GLY 92 88 ASP 93 89 ASN 94 90 LYS 95 91 LEU 96 92 VAL 97 93 THR 98 94 ALA 99 95 PHE 100 96 LYS 101 97 ASN 102 98 ILE 103 99 LYS 104 100 SER 105 101 VAL 106 102 THR 107 103 GLU 108 104 LEU 109 105 ASN 110 106 GLY 111 107 ASP 112 108 ILE 113 109 ILE 114 110 THR 115 111 ASN 116 112 THR 117 113 MET 118 114 THR 119 115 LEU 120 116 GLY 121 117 ASP 122 118 ILE 123 119 VAL 124 120 PHE 125 121 LYS 126 122 ARG 127 123 ILE 128 124 SER 129 125 LYS 130 126 ARG 131 127 ILE 132 128 LEU 133 129 VAL 134 130 PRO 135 131 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 BMRB 17302 L-FABP 93.33 126 99.21 99.21 1.93e-81 BMRB 17303 L-FABP 93.33 126 99.21 99.21 1.93e-81 BMRB 19160 hL-FABP 100.00 135 100.00 100.00 3.75e-90 BMRB 19188 hL-FABP 100.00 135 100.00 100.00 3.75e-90 BMRB 19189 hL-FABP 100.00 135 100.00 100.00 3.75e-90 PDB 2F73 "Crystal Structure Of Human Fatty Acid Binding Protein 1 (Fabp1)" 94.81 149 99.22 99.22 4.55e-83 PDB 2L67 "Solution Structure Of Human Apo L-fabp" 93.33 126 99.21 99.21 1.93e-81 PDB 2L68 "Solution Structure Of Human Holo L-fabp" 93.33 126 99.21 99.21 1.93e-81 PDB 2LKK "Human L-fabp In Complex With Oleate" 93.33 126 99.21 99.21 1.93e-81 PDB 2PY1 "Solution Structure Of Human Liver Fatty Acid Binding Protein" 95.56 129 99.22 99.22 7.86e-84 PDB 3B2H "Iodide Derivative Of Human Lfabp At High Resolution" 97.04 132 97.71 97.71 5.79e-82 PDB 3B2I "Iodide Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3B2J "Iodide Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3B2K "Iodide Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3B2L "Iodide Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3STK "Crystal Structure Of Human Lfabp Complex With Two Molecules Of Palmitic Acid (Holo-Lfabp)" 97.04 132 97.71 97.71 5.79e-82 PDB 3STM "Structure Of Human Lfabp In Complex With One Molecule Of Palmitic Acid" 97.04 132 97.71 97.71 5.79e-82 PDB 3STN "Structure Of Human Lfabp (Apo-Lfabp)" 97.04 132 97.71 97.71 5.79e-82 PDB 3VG2 "Iodide Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3VG3 "Cadmium Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3VG4 "Cadmium Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3VG5 "Barium Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3VG6 "Barium Derivative Of Human Lfabp" 97.04 132 97.71 97.71 5.79e-82 PDB 3VG7 "Structure Of Human Lfabp At High Resolution From S-sad" 97.04 132 97.71 97.71 5.79e-82 DBJ BAI46102 "fatty acid binding protein 1, liver [synthetic construct]" 94.07 127 99.21 99.21 2.19e-82 EMBL CAG46887 "FABP1 [Homo sapiens]" 94.07 127 99.21 99.21 2.19e-82 GB AAA52418 "fatty acid binding protein [Homo sapiens]" 94.07 127 100.00 100.00 3.39e-83 GB AAA52419 "L-FABP [Homo sapiens]" 94.07 127 99.21 99.21 2.19e-82 GB AAH22287 "FABP1 protein, partial [Homo sapiens]" 93.33 134 98.41 99.21 2.53e-81 GB AAH32801 "Fatty acid binding protein 1, liver [Homo sapiens]" 94.07 127 99.21 99.21 2.19e-82 GB AAX37108 "fatty acid binding protein 1 [synthetic construct]" 94.07 128 99.21 99.21 2.34e-82 REF NP_001434 "fatty acid-binding protein, liver [Homo sapiens]" 94.07 127 99.21 99.21 2.19e-82 REF XP_001140263 "PREDICTED: fatty acid-binding protein, liver [Pan troglodytes]" 94.07 127 99.21 99.21 2.19e-82 REF XP_003268834 "PREDICTED: fatty acid-binding protein, liver [Nomascus leucogenys]" 94.07 127 97.64 98.43 6.98e-81 REF XP_003805902 "PREDICTED: fatty acid-binding protein, liver [Pan paniscus]" 94.07 127 99.21 99.21 2.19e-82 REF XP_004029642 "PREDICTED: fatty acid-binding protein, liver [Gorilla gorilla gorilla]" 94.07 127 98.43 99.21 5.49e-82 SP P07148 "RecName: Full=Fatty acid-binding protein, liver; AltName: Full=Fatty acid-binding protein 1; AltName: Full=Liver-type fatty aci" 94.07 127 99.21 99.21 2.19e-82 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hL-FABP 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 $hL-FABP 'recombinant technology' . Escherichia coli . pQE50 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 $hL-FABP 0.5 mM '[U-100% 13C; U-100% 15N]' 'TAUROCHOLIC ACID' 7.5 mM 'natural abundant' 'sodium phosphate' 10 mM 'natural abundant' H2O 93 % 'natural abundant' D2O 7 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 10 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP C 13 protons ppm 0 external indirect . . . 0.251449530 TSP H 1 protons ppm 0 external direct . . . 1 TSP N 15 protons ppm 0 external 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_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' 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 'human liver fatty acid binding protein' _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 2 ARG CA C 53.769 0.3 1 2 -2 2 ARG CB C 28.054 0.3 1 3 -1 3 GLY H H 8.529 0.02 1 4 -1 3 GLY CA C 42.431 0.3 1 5 -1 3 GLY N N 111.043 0.2 1 6 0 4 SER H H 8.187 0.02 1 7 0 4 SER CA C 55.815 0.3 1 8 0 4 SER CB C 61.336 0.3 1 9 0 4 SER N N 115.43 0.2 1 10 1 5 MET H H 8.446 0.02 1 11 1 5 MET CA C 52.538 0.3 1 12 1 5 MET CB C 30.329 0.3 1 13 1 5 MET N N 122.219 0.2 1 14 2 6 SER H H 8.111 0.02 1 15 2 6 SER CA C 54.808 0.3 1 16 2 6 SER CB C 61.685 0.3 1 17 2 6 SER N N 116.678 0.2 1 18 3 7 PHE H H 9.597 0.02 1 19 3 7 PHE CA C 57.234 0.3 1 20 3 7 PHE CB C 38.118 0.3 1 21 3 7 PHE N N 122.035 0.2 1 22 4 8 SER H H 8.318 0.02 1 23 4 8 SER CA C 57.536 0.3 1 24 4 8 SER CB C 61.107 0.3 1 25 4 8 SER N N 116.296 0.2 1 26 5 9 GLY H H 8.857 0.02 1 27 5 9 GLY CA C 42.176 0.3 1 28 5 9 GLY N N 110.946 0.2 1 29 6 10 LYS H H 8.045 0.02 1 30 6 10 LYS CA C 52.954 0.3 1 31 6 10 LYS CB C 32.334 0.3 1 32 6 10 LYS N N 119.898 0.2 1 33 7 11 TYR H H 9.228 0.02 1 34 7 11 TYR CA C 53.889 0.3 1 35 7 11 TYR CB C 39.144 0.3 1 36 7 11 TYR N N 120.901 0.2 1 37 8 12 GLN H H 8.957 0.02 1 38 8 12 GLN CA C 51.454 0.3 1 39 8 12 GLN CB C 29.125 0.3 1 40 8 12 GLN N N 123.016 0.2 1 41 9 13 LEU H H 8.552 0.02 1 42 9 13 LEU CA C 54.681 0.3 1 43 9 13 LEU CB C 39.832 0.3 1 44 9 13 LEU N N 131.529 0.2 1 45 10 14 GLN H H 9.993 0.02 1 46 10 14 GLN CA C 53.701 0.3 1 47 10 14 GLN CB C 29.12 0.3 1 48 10 14 GLN N N 125.815 0.2 1 49 11 15 SER H H 7.966 0.02 1 50 11 15 SER CA C 55.117 0.3 1 51 11 15 SER CB C 62.368 0.3 1 52 11 15 SER N N 110.761 0.2 1 53 12 16 GLN H H 8.554 0.02 1 54 12 16 GLN CA C 51.626 0.3 1 55 12 16 GLN CB C 30.05 0.3 1 56 12 16 GLN N N 116.045 0.2 1 57 13 17 GLU H H 9.061 0.02 1 58 13 17 GLU CA C 52.619 0.3 1 59 13 17 GLU CB C 30.943 0.3 1 60 13 17 GLU N N 121.142 0.2 1 61 14 18 ASN H H 9.236 0.02 1 62 14 18 ASN CA C 51.777 0.3 1 63 14 18 ASN CB C 33.754 0.3 1 64 14 18 ASN N N 118.089 0.2 1 65 15 19 PHE H H 8.337 0.02 1 66 15 19 PHE CA C 59.126 0.3 1 67 15 19 PHE CB C 37.373 0.3 1 68 15 19 PHE N N 117.975 0.2 1 69 16 20 GLU H H 9.473 0.02 1 70 16 20 GLU CA C 58.802 0.3 1 71 16 20 GLU CB C 25.755 0.3 1 72 16 20 GLU N N 118.612 0.2 1 73 17 21 ALA H H 8.192 0.02 1 74 17 21 ALA CA C 52.102 0.3 1 75 17 21 ALA CB C 15.628 0.3 1 76 17 21 ALA N N 119.488 0.2 1 77 18 22 PHE H H 7.676 0.02 1 78 18 22 PHE CA C 59.495 0.3 1 79 18 22 PHE CB C 37.201 0.3 1 80 18 22 PHE N N 118.626 0.2 1 81 19 23 MET H H 7.994 0.02 1 82 19 23 MET CA C 53.656 0.3 1 83 19 23 MET CB C 29.065 0.3 1 84 19 23 MET N N 114.917 0.2 1 85 20 24 LYS H H 8.01 0.02 1 86 20 24 LYS CA C 56.32 0.3 1 87 20 24 LYS CB C 29.558 0.3 1 88 20 24 LYS N N 118.374 0.2 1 89 21 25 ALA H H 7.464 0.02 1 90 21 25 ALA CA C 52.099 0.3 1 91 21 25 ALA CB C 15.617 0.3 1 92 21 25 ALA N N 123.023 0.2 1 93 22 26 ILE H H 7.278 0.02 1 94 22 26 ILE CA C 59.09 0.3 1 95 22 26 ILE CB C 35.027 0.3 1 96 22 26 ILE N N 110.698 0.2 1 97 23 27 GLY H H 7.375 0.02 1 98 23 27 GLY CA C 43.052 0.3 1 99 23 27 GLY N N 108.37 0.2 1 100 24 28 LEU H H 7.558 0.02 1 101 24 28 LEU CA C 50.701 0.3 1 102 24 28 LEU CB C 38.896 0.3 1 103 24 28 LEU N N 122.94 0.2 1 104 25 29 PRO CA C 59.962 0.3 1 105 25 29 PRO CB C 30.107 0.3 1 106 26 30 GLU H H 8.716 0.02 1 107 26 30 GLU CA C 57.169 0.3 1 108 26 30 GLU CB C 26.859 0.3 1 109 26 30 GLU N N 123.345 0.2 1 110 27 31 GLU H H 9.238 0.02 1 111 27 31 GLU CA C 56.102 0.3 1 112 27 31 GLU CB C 26.363 0.3 1 113 27 31 GLU N N 117.363 0.2 1 114 28 32 LEU H H 7.14 0.02 1 115 28 32 LEU CA C 54.204 0.3 1 116 28 32 LEU CB C 39.028 0.3 1 117 28 32 LEU N N 117.313 0.2 1 118 29 33 ILE H H 7.581 0.02 1 119 29 33 ILE CA C 63.483 0.3 1 120 29 33 ILE CB C 34.843 0.3 1 121 29 33 ILE N N 121.363 0.2 1 122 30 34 GLN H H 8.103 0.02 1 123 30 34 GLN CA C 55.905 0.3 1 124 30 34 GLN CB C 25.215 0.3 1 125 30 34 GLN N N 116.092 0.2 1 126 31 35 LYS H H 7.427 0.02 1 127 31 35 LYS CA C 55.751 0.3 1 128 31 35 LYS CB C 30.469 0.3 1 129 31 35 LYS N N 116.087 0.2 1 130 32 36 GLY H H 8.055 0.02 1 131 32 36 GLY CA C 43.518 0.3 1 132 32 36 GLY N N 104.909 0.2 1 133 33 37 LYS H H 7.44 0.02 1 134 33 37 LYS CA C 56.148 0.3 1 135 33 37 LYS CB C 29.512 0.3 1 136 33 37 LYS N N 119.461 0.2 1 137 34 38 ASP H H 7.598 0.02 1 138 34 38 ASP CA C 51.568 0.3 1 139 34 38 ASP CB C 38.872 0.3 1 140 34 38 ASP N N 116.963 0.2 1 141 35 39 ILE H H 7.138 0.02 1 142 35 39 ILE CA C 56.095 0.3 1 143 35 39 ILE CB C 33.038 0.3 1 144 35 39 ILE N N 119.588 0.2 1 145 36 40 LYS H H 8.514 0.02 1 146 36 40 LYS CA C 52.461 0.3 1 147 36 40 LYS CB C 29.371 0.3 1 148 36 40 LYS N N 128.2 0.2 1 149 37 41 GLY H H 7.871 0.02 1 150 37 41 GLY CA C 42.769 0.3 1 151 37 41 GLY N N 111.06 0.2 1 152 38 42 VAL H H 8.212 0.02 1 153 38 42 VAL CA C 58.102 0.3 1 154 38 42 VAL CB C 32.892 0.3 1 155 38 42 VAL N N 120.21 0.2 1 156 39 43 SER H H 9.04 0.02 1 157 39 43 SER CA C 54.183 0.3 1 158 39 43 SER CB C 63.113 0.3 1 159 39 43 SER N N 120.218 0.2 1 160 40 44 GLU H H 9.275 0.02 1 161 40 44 GLU CA C 52.339 0.3 1 162 40 44 GLU CB C 29.579 0.3 1 163 40 44 GLU N N 125.938 0.2 1 164 41 45 ILE H H 9.46 0.02 1 165 41 45 ILE CA C 57.56 0.3 1 166 41 45 ILE CB C 37.159 0.3 1 167 41 45 ILE N N 126.106 0.2 1 168 42 46 VAL H H 8.952 0.02 1 169 42 46 VAL CA C 59.729 0.3 1 170 42 46 VAL CB C 31.318 0.3 1 171 42 46 VAL N N 128.49 0.2 1 172 43 47 GLN H H 8.471 0.02 1 173 43 47 GLN CA C 50.953 0.3 1 174 43 47 GLN CB C 27.048 0.3 1 175 43 47 GLN N N 131.211 0.2 1 176 44 48 ASN H H 8.951 0.02 1 177 44 48 ASN CA C 49.297 0.3 1 178 44 48 ASN CB C 36.876 0.3 1 179 44 48 ASN N N 127.257 0.2 1 180 45 49 GLY H H 9.112 0.02 1 181 45 49 GLY CA C 44.844 0.3 1 182 45 49 GLY N N 115.78 0.2 1 183 46 50 LYS H H 8.689 0.02 1 184 46 50 LYS CA C 53.984 0.3 1 185 46 50 LYS CB C 30.191 0.3 1 186 46 50 LYS N N 125.933 0.2 1 187 47 51 HIS H H 7.952 0.02 1 188 47 51 HIS CA C 53.465 0.3 1 189 47 51 HIS CB C 34.93 0.3 1 190 47 51 HIS N N 120.037 0.2 1 191 48 52 PHE H H 8.702 0.02 1 192 48 52 PHE CA C 54.133 0.3 1 193 48 52 PHE CB C 40.948 0.3 1 194 48 52 PHE N N 124.994 0.2 1 195 49 53 LYS H H 8.132 0.02 1 196 49 53 LYS CA C 53.553 0.3 1 197 49 53 LYS CB C 32.984 0.3 1 198 49 53 LYS N N 119.088 0.2 1 199 50 54 PHE H H 9.405 0.02 1 200 50 54 PHE CB C 41.318 0.3 1 201 50 54 PHE N N 125.355 0.2 1 202 51 55 THR H H 9.259 0.02 1 203 51 55 THR CA C 59.937 0.3 1 204 51 55 THR CB C 67.389 0.3 1 205 51 55 THR N N 120.742 0.2 1 206 52 56 ILE H H 9.378 0.02 1 207 52 56 ILE CA C 57.662 0.3 1 208 52 56 ILE CB C 37.82 0.3 1 209 52 56 ILE N N 130.438 0.2 1 210 53 57 THR H H 8.82 0.02 1 211 53 57 THR CA C 61.877 0.3 1 212 53 57 THR CB C 67.44 0.3 1 213 53 57 THR N N 122.369 0.2 1 214 54 58 ALA H H 8.934 0.02 1 215 54 58 ALA CA C 48.335 0.3 1 216 54 58 ALA CB C 17.291 0.3 1 217 54 58 ALA N N 130.69 0.2 1 218 55 59 GLY H H 8.903 0.02 1 219 55 59 GLY CA C 44.279 0.3 1 220 55 59 GLY N N 114.96 0.2 1 221 56 60 SER H H 8.675 0.02 1 222 56 60 SER CA C 55.96 0.3 1 223 56 60 SER CB C 60.961 0.3 1 224 56 60 SER N N 121.446 0.2 1 225 57 61 LYS H H 7.818 0.02 1 226 57 61 LYS CA C 52.992 0.3 1 227 57 61 LYS CB C 31.338 0.3 1 228 57 61 LYS N N 124.162 0.2 1 229 58 62 VAL H H 8.252 0.02 1 230 58 62 VAL CA C 58.397 0.3 1 231 58 62 VAL CB C 31.356 0.3 1 232 58 62 VAL N N 125.639 0.2 1 233 59 63 ILE H H 9.038 0.02 1 234 59 63 ILE CA C 57.085 0.3 1 235 59 63 ILE CB C 38.631 0.3 1 236 59 63 ILE N N 126.426 0.2 1 237 60 64 GLN H H 8.77 0.02 1 238 60 64 GLN CA C 51.554 0.3 1 239 60 64 GLN CB C 28.82 0.3 1 240 60 64 GLN N N 125.666 0.2 1 241 61 65 ASN H H 8.974 0.02 1 242 61 65 ASN CA C 49.857 0.3 1 243 61 65 ASN CB C 42.241 0.3 1 244 61 65 ASN N N 121.647 0.2 1 245 62 66 GLU H H 8.974 0.02 1 246 62 66 GLU CA C 52.188 0.3 1 247 62 66 GLU CB C 31.064 0.3 1 248 62 66 GLU N N 121.444 0.2 1 249 63 67 PHE H H 8.241 0.02 1 250 63 67 PHE CA C 54.038 0.3 1 251 63 67 PHE CB C 38.64 0.3 1 252 63 67 PHE N N 115.34 0.2 1 253 64 68 THR H H 8.973 0.02 1 254 64 68 THR CA C 58.592 0.3 1 255 64 68 THR CB C 67.768 0.3 1 256 64 68 THR N N 118.046 0.2 1 257 65 69 VAL H H 9.139 0.02 1 258 65 69 VAL CA C 61.504 0.3 1 259 65 69 VAL CB C 29.223 0.3 1 260 65 69 VAL N N 125.144 0.2 1 261 66 70 GLY H H 8.795 0.02 1 262 66 70 GLY CA C 42.71 0.3 1 263 66 70 GLY N N 109.421 0.2 1 264 67 71 GLU H H 7.737 0.02 1 265 67 71 GLU CA C 51.54 0.3 1 266 67 71 GLU CB C 29.08 0.3 1 267 67 71 GLU N N 119.125 0.2 1 268 68 72 GLU H H 8.972 0.02 1 269 68 72 GLU CA C 55.39 0.3 1 270 68 72 GLU CB C 27.368 0.3 1 271 68 72 GLU N N 125.892 0.2 1 272 69 73 CYS H H 9.008 0.02 1 273 69 73 CYS CA C 52.849 0.3 1 274 69 73 CYS CB C 28.684 0.3 1 275 69 73 CYS N N 122.196 0.2 1 276 70 74 GLU H H 8.408 0.02 1 277 70 74 GLU CA C 52.546 0.3 1 278 70 74 GLU CB C 29.302 0.3 1 279 70 74 GLU N N 119.978 0.2 1 280 71 75 LEU H H 8.938 0.02 1 281 71 75 LEU CA C 50.279 0.3 1 282 71 75 LEU CB C 41.937 0.3 1 283 71 75 LEU N N 126.18 0.2 1 284 72 76 GLU H H 9.081 0.02 1 285 72 76 GLU CA C 52.497 0.3 1 286 72 76 GLU CB C 29.35 0.3 1 287 72 76 GLU N N 123.053 0.2 1 288 73 77 THR H H 8.552 0.02 1 289 73 77 THR CA C 57.534 0.3 1 290 73 77 THR CB C 68.253 0.3 1 291 73 77 THR N N 114.591 0.2 1 292 74 78 MET H H 9.004 0.02 1 293 74 78 MET N N 118.049 0.2 1 294 75 79 THR H H 7.619 0.02 1 295 75 79 THR CA C 58.959 0.3 1 296 75 79 THR CB C 66.197 0.3 1 297 75 79 THR N N 105.545 0.2 1 298 76 80 GLY H H 7.647 0.02 1 299 76 80 GLY CA C 42.542 0.3 1 300 76 80 GLY N N 110.126 0.2 1 301 77 81 GLU H H 7.34 0.02 1 302 77 81 GLU CA C 53.467 0.3 1 303 77 81 GLU CB C 27.642 0.3 1 304 77 81 GLU N N 120.775 0.2 1 305 78 82 LYS H H 8.375 0.02 1 306 78 82 LYS CA C 51.965 0.3 1 307 78 82 LYS CB C 31.32 0.3 1 308 78 82 LYS N N 121.077 0.2 1 309 79 83 VAL H H 8.793 0.02 1 310 79 83 VAL CA C 57.048 0.3 1 311 79 83 VAL CB C 31.422 0.3 1 312 79 83 VAL N N 120.585 0.2 1 313 80 84 LYS H H 8.005 0.02 1 314 80 84 LYS CA C 52.202 0.3 1 315 80 84 LYS CB C 30.713 0.3 1 316 80 84 LYS N N 125.027 0.2 1 317 81 85 THR H H 8.43 0.02 1 318 81 85 THR CA C 56.807 0.3 1 319 81 85 THR CB C 66.703 0.3 1 320 81 85 THR N N 117.938 0.2 1 321 82 86 VAL H H 8.137 0.02 1 322 82 86 VAL CA C 58.735 0.3 1 323 82 86 VAL CB C 32.312 0.3 1 324 82 86 VAL N N 120.001 0.2 1 325 83 87 VAL H H 9.717 0.02 1 326 83 87 VAL CA C 58.547 0.3 1 327 83 87 VAL CB C 29.161 0.3 1 328 83 87 VAL N N 133.538 0.2 1 329 84 88 GLN H H 8.8 0.02 1 330 84 88 GLN CA C 51.03 0.3 1 331 84 88 GLN CB C 32.717 0.3 1 332 84 88 GLN N N 124.682 0.2 1 333 85 89 LEU H H 8.468 0.02 1 334 85 89 LEU CA C 51.371 0.3 1 335 85 89 LEU CB C 41.855 0.3 1 336 85 89 LEU N N 123.593 0.2 1 337 86 90 GLU H H 9.083 0.02 1 338 86 90 GLU CA C 52.646 0.3 1 339 86 90 GLU CB C 28.874 0.3 1 340 86 90 GLU N N 128.459 0.2 1 341 87 91 GLY H H 8.413 0.02 1 342 87 91 GLY CA C 43.292 0.3 1 343 87 91 GLY N N 112.807 0.2 1 344 88 92 ASP H H 8.43 0.02 1 345 88 92 ASP CA C 52.067 0.3 1 346 88 92 ASP CB C 39.098 0.3 1 347 88 92 ASP N N 118.014 0.2 1 348 89 93 ASN H H 8.127 0.02 1 349 89 93 ASN CA C 50.757 0.3 1 350 89 93 ASN CB C 37.001 0.3 1 351 89 93 ASN N N 114.543 0.2 1 352 90 94 LYS H H 7.426 0.02 1 353 90 94 LYS CA C 52.528 0.3 1 354 90 94 LYS CB C 33.331 0.3 1 355 90 94 LYS N N 118.583 0.2 1 356 91 95 LEU H H 8.986 0.02 1 357 91 95 LEU CA C 50.143 0.3 1 358 91 95 LEU CB C 41.475 0.3 1 359 91 95 LEU N N 123.983 0.2 1 360 92 96 VAL H H 9.266 0.02 1 361 92 96 VAL CA C 58.068 0.3 1 362 92 96 VAL CB C 32.746 0.3 1 363 92 96 VAL N N 123.675 0.2 1 364 93 97 THR H H 8.792 0.02 1 365 93 97 THR CA C 61.072 0.3 1 366 93 97 THR CB C 66.587 0.3 1 367 93 97 THR N N 120.05 0.2 1 368 94 98 ALA H H 8.348 0.02 1 369 94 98 ALA CA C 48.469 0.3 1 370 94 98 ALA CB C 19.439 0.3 1 371 94 98 ALA N N 125.911 0.2 1 372 95 99 PHE H H 8.562 0.02 1 373 95 99 PHE CA C 55.368 0.3 1 374 95 99 PHE CB C 38.839 0.3 1 375 95 99 PHE N N 121.083 0.2 1 376 96 100 LYS H H 8.792 0.02 1 377 96 100 LYS N N 124.657 0.2 1 378 97 101 ASN CA C 51.055 0.3 1 379 97 101 ASN CB C 34.981 0.3 1 380 98 102 ILE H H 8.435 0.02 1 381 98 102 ILE CA C 58.27 0.3 1 382 98 102 ILE CB C 37.463 0.3 1 383 98 102 ILE N N 121.42 0.2 1 384 99 103 LYS H H 8.236 0.02 1 385 99 103 LYS CA C 52.546 0.3 1 386 99 103 LYS CB C 31.852 0.3 1 387 99 103 LYS N N 127.03 0.2 1 388 100 104 SER H H 8.617 0.02 1 389 100 104 SER CA C 53.244 0.3 1 390 100 104 SER CB C 62.049 0.3 1 391 100 104 SER N N 118.514 0.2 1 392 101 105 VAL H H 8.818 0.02 1 393 101 105 VAL CA C 58.879 0.3 1 394 101 105 VAL CB C 32.452 0.3 1 395 101 105 VAL N N 128.446 0.2 1 396 102 106 THR H H 9.312 0.02 1 397 102 106 THR CA C 59.293 0.3 1 398 102 106 THR CB C 67.436 0.3 1 399 102 106 THR N N 128.175 0.2 1 400 103 107 GLU H H 8.993 0.02 1 401 103 107 GLU CA C 51.173 0.3 1 402 103 107 GLU CB C 31.379 0.3 1 403 103 107 GLU N N 127.131 0.2 1 404 104 108 LEU H H 8.453 0.02 1 405 104 108 LEU CA C 50.923 0.3 1 406 104 108 LEU CB C 45.088 0.3 1 407 104 108 LEU N N 128.497 0.2 1 408 105 109 ASN H H 8.884 0.02 1 409 105 109 ASN CA C 49.91 0.3 1 410 105 109 ASN CB C 37.585 0.3 1 411 105 109 ASN N N 126.343 0.2 1 412 106 110 GLY H H 8.876 0.02 1 413 106 110 GLY CA C 45.165 0.3 1 414 106 110 GLY N N 115.505 0.2 1 415 107 111 ASP H H 8.837 0.02 1 416 107 111 ASP CA C 51.321 0.3 1 417 107 111 ASP CB C 39.285 0.3 1 418 107 111 ASP N N 127.048 0.2 1 419 108 112 ILE H H 7.877 0.02 1 420 108 112 ILE CA C 56.139 0.3 1 421 108 112 ILE CB C 37.104 0.3 1 422 108 112 ILE N N 119.933 0.2 1 423 109 113 ILE H H 8.761 0.02 1 424 109 113 ILE CA C 57.152 0.3 1 425 109 113 ILE CB C 38.08 0.3 1 426 109 113 ILE N N 126.573 0.2 1 427 110 114 THR H H 8.842 0.02 1 428 110 114 THR CA C 58.591 0.3 1 429 110 114 THR CB C 67.258 0.3 1 430 110 114 THR N N 123.443 0.2 1 431 111 115 ASN H H 9.149 0.02 1 432 111 115 ASN CA C 49.14 0.3 1 433 111 115 ASN CB C 39.074 0.3 1 434 111 115 ASN N N 127.269 0.2 1 435 112 116 THR H H 9.24 0.02 1 436 112 116 THR CA C 59.275 0.3 1 437 112 116 THR CB C 66.893 0.3 1 438 112 116 THR N N 123.062 0.2 1 439 113 117 MET H H 9.358 0.02 1 440 113 117 MET CA C 51.531 0.3 1 441 113 117 MET CB C 34.015 0.3 1 442 113 117 MET N N 128.179 0.2 1 443 114 118 THR H H 8.85 0.02 1 444 114 118 THR CA C 58.393 0.3 1 445 114 118 THR CB C 68.284 0.3 1 446 114 118 THR N N 117.315 0.2 1 447 115 119 LEU H H 8.691 0.02 1 448 115 119 LEU CA C 53.875 0.3 1 449 115 119 LEU CB C 41.999 0.3 1 450 115 119 LEU N N 128.862 0.2 1 451 116 120 GLY H H 9.218 0.02 1 452 116 120 GLY CA C 44.74 0.3 1 453 116 120 GLY N N 117.796 0.2 1 454 117 121 ASP H H 8.623 0.02 1 455 117 121 ASP CA C 51.486 0.3 1 456 117 121 ASP CB C 38.118 0.3 1 457 117 121 ASP N N 126.407 0.2 1 458 118 122 ILE H H 8.308 0.02 1 459 118 122 ILE CA C 59.126 0.3 1 460 118 122 ILE CB C 35.974 0.3 1 461 118 122 ILE N N 122.558 0.2 1 462 119 123 VAL H H 8.334 0.02 1 463 119 123 VAL CA C 59.1 0.3 1 464 119 123 VAL CB C 29.444 0.3 1 465 119 123 VAL N N 127.569 0.2 1 466 120 124 PHE H H 9.303 0.02 1 467 120 124 PHE CA C 51.277 0.3 1 468 120 124 PHE CB C 38.311 0.3 1 469 120 124 PHE N N 131.516 0.2 1 470 121 125 LYS H H 8.037 0.02 1 471 121 125 LYS CA C 51.68 0.3 1 472 121 125 LYS CB C 34.32 0.3 1 473 121 125 LYS N N 128.164 0.2 1 474 122 126 ARG H H 8.631 0.02 1 475 122 126 ARG CA C 52.785 0.3 1 476 122 126 ARG CB C 31.629 0.3 1 477 122 126 ARG N N 122.567 0.2 1 478 123 127 ILE H H 8.739 0.02 1 479 123 127 ILE CB C 44.187 0.3 1 480 123 127 ILE N N 126.245 0.2 1 481 124 128 SER H H 9.27 0.02 1 482 124 128 SER CA C 56.164 0.3 1 483 124 128 SER CB C 62.795 0.3 1 484 124 128 SER N N 122.808 0.2 1 485 125 129 LYS H H 8.596 0.02 1 486 125 129 LYS CA C 51.765 0.3 1 487 125 129 LYS CB C 32.486 0.3 1 488 125 129 LYS N N 122.984 0.2 1 489 126 130 ARG H H 9.22 0.02 1 490 126 130 ARG CA C 54.475 0.3 1 491 126 130 ARG CB C 28.723 0.3 1 492 126 130 ARG N N 129.394 0.2 1 493 127 131 ILE H H 8.632 0.02 1 494 127 131 ILE CA C 58.201 0.3 1 495 127 131 ILE CB C 36.78 0.3 1 496 127 131 ILE N N 126.163 0.2 1 497 128 132 LEU H H 8.268 0.02 1 498 128 132 LEU CA C 52.14 0.3 1 499 128 132 LEU CB C 39.869 0.3 1 500 128 132 LEU N N 127.024 0.2 1 501 129 133 VAL H H 8.028 0.02 1 502 129 133 VAL CA C 56.918 0.3 1 503 129 133 VAL CB C 30.017 0.3 1 504 129 133 VAL N N 123.03 0.2 1 505 130 134 PRO CA C 60.57 0.3 1 506 130 134 PRO CB C 31.46 0.3 1 507 131 135 ARG H H 7.937 0.02 1 508 131 135 ARG CA C 55.116 0.3 1 509 131 135 ARG CB C 28.339 0.3 1 510 131 135 ARG N N 125.371 0.2 1 stop_ save_