data_7356 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HN,CA,CB Chemical shift assignments for apo-Rat intestinal fatty acid binding protein, Clofibric acid-Rat intestinal fatty acid binding protein complex, Fenofibric acid-Rat intestinal fatty acid binding protein complex and Tolfenamic acid-Rat intestinal fatty acid binding protein complex. ; _BMRB_accession_number 7356 _BMRB_flat_file_name bmr7356.str _Entry_type original _Submission_date 2006-12-17 _Accession_date 2006-12-17 _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 Velkov Tony . . 2 Scanlon Martin J. . 3 Porter Christopher J.H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 247 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-14 update BMRB 'complete entry citation' 2007-03-08 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15082 apo 7355 'Clofibric_acid bound' 7357 'tolfenamic bound' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Examination of the role of intestinal fatty acid-binding protein in drug absorption using a parallel artificial membrane permeability assay. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17462580 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Velkov Tony . . 2 Horne James . . 3 Languerre Aisha . . 4 Jones Eric . . 5 Scanlon Martin J. . 6 Porter Christopher J.H. . stop_ _Journal_abbreviation 'Chem. Biol.' _Journal_name_full 'Chemistry & Biology' _Journal_volume 14 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 453 _Page_last 465 _Year 2007 _Details . loop_ _Keyword 'Intestinal fatty acid binding protein' 'intestinal lipophilic drug transport' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Rat intestinal fatty acid binding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'single polypeptide chain' $Rat_intestinal_fatty_acid_binding_protein Fenofibric_acid $Fenofibric_acid 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_Rat_intestinal_fatty_acid_binding_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Rat_intestinal_fatty_acid_binding_protein _Molecular_mass 14993.0 _Mol_thiol_state 'not present' loop_ _Biological_function 'cytosolic fatty acid binding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 131 _Mol_residue_sequence ; AFDGTWKVDRNENYEKFMEK MGINVVKRKLGAHDNLKLTI TQEGNKFTVKESSNFRNIDV VFELGVDFAYSLADGTELTG TWTMEGNKLVGKFKRVDNGK ELIAVREISGNELIQTYTYE GVEAKRIFKKE ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 PHE 3 ASP 4 GLY 5 THR 6 TRP 7 LYS 8 VAL 9 ASP 10 ARG 11 ASN 12 GLU 13 ASN 14 TYR 15 GLU 16 LYS 17 PHE 18 MET 19 GLU 20 LYS 21 MET 22 GLY 23 ILE 24 ASN 25 VAL 26 VAL 27 LYS 28 ARG 29 LYS 30 LEU 31 GLY 32 ALA 33 HIS 34 ASP 35 ASN 36 LEU 37 LYS 38 LEU 39 THR 40 ILE 41 THR 42 GLN 43 GLU 44 GLY 45 ASN 46 LYS 47 PHE 48 THR 49 VAL 50 LYS 51 GLU 52 SER 53 SER 54 ASN 55 PHE 56 ARG 57 ASN 58 ILE 59 ASP 60 VAL 61 VAL 62 PHE 63 GLU 64 LEU 65 GLY 66 VAL 67 ASP 68 PHE 69 ALA 70 TYR 71 SER 72 LEU 73 ALA 74 ASP 75 GLY 76 THR 77 GLU 78 LEU 79 THR 80 GLY 81 THR 82 TRP 83 THR 84 MET 85 GLU 86 GLY 87 ASN 88 LYS 89 LEU 90 VAL 91 GLY 92 LYS 93 PHE 94 LYS 95 ARG 96 VAL 97 ASP 98 ASN 99 GLY 100 LYS 101 GLU 102 LEU 103 ILE 104 ALA 105 VAL 106 ARG 107 GLU 108 ILE 109 SER 110 GLY 111 ASN 112 GLU 113 LEU 114 ILE 115 GLN 116 THR 117 TYR 118 THR 119 TYR 120 GLU 121 GLY 122 VAL 123 GLU 124 ALA 125 LYS 126 ARG 127 ILE 128 PHE 129 LYS 130 LYS 131 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 15082 Rat_intestinal_fatty_acid_binding_protein 100.00 131 100.00 100.00 2.90e-87 BMRB 7355 Rat_intestinal_fatty_acid_binding_protein 100.00 131 100.00 100.00 2.90e-87 BMRB 7357 Rat_intestinal_fatty_acid_binding_protein 100.00 131 100.00 100.00 2.90e-87 PDB 1AEL "Nmr Structure Of Apo Intestinal Fatty Acid-Binding Protein, 20 Structures" 100.00 131 100.00 100.00 2.90e-87 PDB 1DC9 "Properties And Crystal Structure Of A Beta-Barrel Folding Mutant, V60n Intestinal Fatty Acid Binding Protein (Ifabp)" 100.00 131 99.24 99.24 3.86e-86 PDB 1ICM "Escherichia Coli-Derived Rat Intestinal Fatty Acid Binding Protein With Bound Myristate At 1.5 A Resolution And I- Fabparg106--" 100.00 131 100.00 100.00 2.90e-87 PDB 1ICN "Escherichia Coli-Derived Rat Intestinal Fatty Acid Binding Protein With Bound Myristate At 1.5 A Resolution And I- Fabparg106--" 100.00 131 99.24 100.00 1.11e-86 PDB 1IFB "Refined Apoprotein Structure Of Rat Intestinal Fatty Acid Binding Protein Produced In Escherichia Coli" 100.00 131 100.00 100.00 2.90e-87 PDB 1IFC "Refinement Of The Structure Of Recombinant Rat Intestinal Fatty Acid- Binding Apoprotein At 1.2 Angstroms Resolution" 100.00 132 100.00 100.00 2.69e-87 PDB 1T8V "The Nmr Structure Of D34a I-Fabp: Implications For The Determinants Of Ligand Binding Stoichiometry" 100.00 131 99.24 99.24 3.14e-86 PDB 1URE "Nmr Structure Of Intestinal Fatty Acid-Binding Protein Complexed With Palmitate, 20 Structures" 100.00 131 100.00 100.00 2.90e-87 PDB 2IFB "Crystal Structure Of Rat Intestinal Fatty-acid-binding Protein. Refinement And Analysis Of The Escherichia Coli- Drived Protein" 100.00 131 100.00 100.00 2.90e-87 PDB 3AKN "X-Ray Structure Of Ifabp From Human And Rat With Bound Fluorescent Fatty Acid Analogue" 100.00 131 100.00 100.00 2.90e-87 GB AAA41133 "fatty acid binding protein, partial [Rattus norvegicus]" 60.31 80 100.00 100.00 3.35e-48 GB AAA41138 "intestinal FABP [Rattus norvegicus]" 100.00 132 98.47 98.47 1.37e-84 GB AAA41141 "fatty acid binding protein (FABP) [Rattus norvegicus]" 100.00 132 100.00 100.00 2.69e-87 GB EDL82110 "fatty acid binding protein 2, intestinal [Rattus norvegicus]" 100.00 132 100.00 100.00 2.69e-87 PRF 1202232A "protein,fatty acid binding" 100.00 132 100.00 100.00 2.69e-87 PRF 1202232A:PDB=1IFC "protein,fatty acid binding" 100.00 132 100.00 100.00 2.69e-87 REF NP_037200 "fatty acid-binding protein, intestinal [Rattus norvegicus]" 100.00 132 100.00 100.00 2.69e-87 SP P02693 "RecName: Full=Fatty acid-binding protein, intestinal; AltName: Full=Fatty acid-binding protein 2; AltName: Full=Intestinal-type" 100.00 132 100.00 100.00 2.69e-87 stop_ save_ ############# # Ligands # ############# save_FENO _Saveframe_category ligand _Mol_type "non-polymer (non_polymer)" _Name_common Fenofibric_acid _BMRB_code . _PDB_code . _Molecular_mass . _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic . _Details . _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Rat_intestinal_fatty_acid_binding_protein 'Norway rat' 10116 Eukaryota Metazoa Rattus norvegicus 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 $Rat_intestinal_fatty_acid_binding_protein 'recombinant technology' . Escherichia coli BL21(DE3) pTrc99A stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Fenofibric_acid-Rat_FABP2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Rat_intestinal_fatty_acid_binding_protein 0.5 mM '[U-99% 13C; U-99% 15N]' 'Fenofibric acid' 5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $Fenofibric_acid-Rat_FABP2 save_ ####################### # Sample conditions # ####################### save_sample_cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 5.5 . pH temperature 295.15 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 $entry_citation $entry_citation 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' stop_ loop_ _Sample_label $Fenofibric_acid-Rat_FABP2 stop_ _Sample_conditions_label $sample_cond _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'single polypeptide chain' _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 CA C 52.446 0.400 1 2 1 1 ALA CB C 19.341 0.400 1 3 2 2 PHE H H 9.344 0.040 1 4 2 2 PHE CA C 59.630 0.400 1 5 2 2 PHE CB C 40.060 0.400 1 6 2 2 PHE N N 116.902 0.400 1 7 3 3 ASP H H 7.925 0.040 1 8 3 3 ASP CA C 55.249 0.400 1 9 3 3 ASP CB C 41.564 0.400 1 10 3 3 ASP N N 116.650 0.400 1 11 4 4 GLY H H 8.523 0.040 1 12 4 4 GLY CA C 43.800 0.400 1 13 4 4 GLY N N 108.673 0.400 1 14 5 5 THR H H 8.356 0.040 1 15 5 5 THR CA C 62.501 0.400 1 16 5 5 THR CB C 69.807 0.400 1 17 5 5 THR N N 116.982 0.400 1 18 6 6 TRP H H 9.370 0.040 1 19 6 6 TRP CA C 54.773 0.400 1 20 6 6 TRP CB C 31.374 0.400 1 21 6 6 TRP N N 128.043 0.400 1 22 7 7 LYS H H 9.535 0.040 1 23 7 7 LYS CA C 54.710 0.400 1 24 7 7 LYS CB C 35.435 0.400 1 25 7 7 LYS N N 124.563 0.400 1 26 8 8 VAL H H 8.844 0.040 1 27 8 8 VAL CA C 65.007 0.400 1 28 8 8 VAL CB C 31.360 0.400 1 29 8 8 VAL N N 129.569 0.400 1 30 9 9 ASP H H 9.713 0.040 1 31 9 9 ASP CA C 55.426 0.400 1 32 9 9 ASP CB C 46.845 0.400 1 33 9 9 ASP N N 127.602 0.400 1 34 10 10 ARG H H 7.767 0.040 1 35 10 10 ARG CA C 54.878 0.400 1 36 10 10 ARG CB C 31.659 0.400 1 37 10 10 ARG N N 112.863 0.400 1 38 11 11 ASN H H 8.695 0.040 1 39 11 11 ASN CA C 51.245 0.400 1 40 11 11 ASN CB C 43.567 0.400 1 41 11 11 ASN N N 116.618 0.400 1 42 12 12 GLU H H 9.465 0.040 1 43 12 12 GLU CA C 55.825 0.400 1 44 12 12 GLU CB C 32.584 0.400 1 45 12 12 GLU N N 120.480 0.400 1 46 13 13 ASN H H 9.393 0.040 1 47 13 13 ASN CA C 54.289 0.400 1 48 13 13 ASN CB C 39.909 0.400 1 49 13 13 ASN N N 122.578 0.400 1 50 14 14 TYR H H 8.412 0.040 1 51 14 14 TYR CA C 58.727 0.400 1 52 14 14 TYR CB C 40.390 0.400 1 53 14 14 TYR N N 119.309 0.400 1 54 15 15 GLU H H 9.032 0.040 1 55 15 15 GLU CA C 61.600 0.400 1 56 15 15 GLU CB C 28.040 0.400 1 57 15 15 GLU N N 120.021 0.400 1 58 16 16 LYS H H 8.321 0.040 1 59 16 16 LYS CA C 58.440 0.400 1 60 16 16 LYS CB C 31.448 0.400 1 61 16 16 LYS N N 119.907 0.400 1 62 17 17 PHE H H 7.826 0.040 1 63 17 17 PHE CA C 62.847 0.400 1 64 17 17 PHE CB C 41.029 0.400 1 65 17 17 PHE N N 121.976 0.400 1 66 18 18 MET H H 8.574 0.040 1 67 18 18 MET CA C 60.073 0.400 1 68 18 18 MET CB C 35.466 0.400 1 69 18 18 MET N N 117.813 0.400 1 70 19 19 GLU H H 7.860 0.040 1 71 19 19 GLU CA C 59.858 0.400 1 72 19 19 GLU CB C 29.530 0.400 1 73 19 19 GLU N N 118.455 0.400 1 74 20 20 LYS H H 8.030 0.040 1 75 20 20 LYS CA C 57.420 0.400 1 76 20 20 LYS CB C 31.431 0.400 1 77 20 20 LYS N N 123.737 0.400 1 78 21 21 MET H H 7.708 0.040 1 79 21 21 MET CA C 55.821 0.400 1 80 21 21 MET CB C 32.617 0.400 1 81 21 21 MET N N 115.285 0.400 1 82 22 22 GLY H H 7.671 0.040 1 83 22 22 GLY CA C 45.457 0.400 1 84 22 22 GLY N N 107.757 0.400 1 85 23 23 ILE H H 7.189 0.040 1 86 23 23 ILE CA C 59.198 0.400 1 87 23 23 ILE CB C 36.146 0.400 1 88 23 23 ILE N N 120.290 0.400 1 89 24 24 ASN H H 8.875 0.040 1 90 24 24 ASN CA C 54.594 0.400 1 91 24 24 ASN CB C 40.027 0.400 1 92 24 24 ASN N N 127.691 0.400 1 93 25 25 VAL H H 8.521 0.040 1 94 25 25 VAL CA C 66.478 0.400 1 95 25 25 VAL CB C 32.040 0.400 1 96 25 25 VAL N N 122.330 0.400 1 97 26 26 VAL H H 7.629 0.040 1 98 26 26 VAL CA C 66.178 0.400 1 99 26 26 VAL CB C 31.818 0.400 1 100 26 26 VAL N N 120.693 0.400 1 101 27 27 LYS H H 7.713 0.040 1 102 27 27 LYS CA C 58.707 0.400 1 103 27 27 LYS CB C 32.676 0.400 1 104 27 27 LYS N N 118.193 0.400 1 105 28 28 ARG H H 8.611 0.040 1 106 28 28 ARG CA C 59.492 0.400 1 107 28 28 ARG CB C 30.796 0.400 1 108 28 28 ARG N N 119.571 0.400 1 109 29 29 LYS H H 7.633 0.040 1 110 29 29 LYS CA C 59.322 0.400 1 111 29 29 LYS CB C 32.020 0.400 1 112 29 29 LYS N N 119.510 0.400 1 113 30 30 LEU H H 7.424 0.040 1 114 30 30 LEU CA C 56.479 0.400 1 115 30 30 LEU CB C 42.324 0.400 1 116 30 30 LEU N N 117.853 0.400 1 117 31 31 GLY H H 8.748 0.040 1 118 31 31 GLY CA C 47.566 0.400 1 119 31 31 GLY N N 107.638 0.400 1 120 32 32 ALA H H 8.014 0.040 1 121 32 32 ALA CA C 53.801 0.400 1 122 32 32 ALA CB C 18.585 0.400 1 123 32 32 ALA N N 119.748 0.400 1 124 33 33 HIS H H 7.433 0.040 1 125 33 33 HIS CA C 53.824 0.400 1 126 33 33 HIS CB C 28.625 0.400 1 127 33 33 HIS N N 117.615 0.400 1 128 34 34 ASP H H 7.136 0.040 1 129 34 34 ASP CA C 54.777 0.400 1 130 34 34 ASP CB C 41.164 0.400 1 131 34 34 ASP N N 117.512 0.400 1 132 35 35 ASN H H 9.244 0.040 1 133 35 35 ASN CA C 53.718 0.400 1 134 35 35 ASN CB C 37.577 0.400 1 135 35 35 ASN N N 119.078 0.400 1 136 36 36 LEU H H 6.959 0.040 1 137 36 36 LEU CA C 57.112 0.400 1 138 36 36 LEU CB C 42.274 0.400 1 139 36 36 LEU N N 118.910 0.400 1 140 37 37 LYS H H 9.588 0.040 1 141 37 37 LYS CA C 54.752 0.400 1 142 37 37 LYS CB C 36.393 0.400 1 143 37 37 LYS N N 127.702 0.400 1 144 38 38 LEU H H 9.356 0.040 1 145 38 38 LEU CA C 52.567 0.400 1 146 38 38 LEU CB C 45.812 0.400 1 147 38 38 LEU N N 123.152 0.400 1 148 39 39 THR H H 9.142 0.040 1 149 39 39 THR CA C 62.478 0.400 1 150 39 39 THR CB C 70.146 0.400 1 151 39 39 THR N N 120.992 0.400 1 152 40 40 ILE H H 9.572 0.040 1 153 40 40 ILE CA C 61.631 0.400 1 154 40 40 ILE CB C 40.020 0.400 1 155 40 40 ILE N N 129.212 0.400 1 156 41 41 THR H H 8.773 0.040 1 157 41 41 THR CA C 61.663 0.400 1 158 41 41 THR CB C 71.506 0.400 1 159 41 41 THR N N 123.021 0.400 1 160 42 42 GLN H H 8.982 0.040 1 161 42 42 GLN CA C 54.420 0.400 1 162 42 42 GLN CB C 29.615 0.400 1 163 42 42 GLN N N 128.747 0.400 1 164 43 43 GLU H H 8.890 0.040 1 165 43 43 GLU CA C 54.767 0.400 1 166 43 43 GLU CB C 31.296 0.400 1 167 43 43 GLU N N 129.529 0.400 1 168 44 44 GLY H H 9.027 0.040 1 169 44 44 GLY CA C 47.378 0.400 1 170 44 44 GLY N N 117.710 0.400 1 171 45 45 ASN H H 8.902 0.040 1 172 45 45 ASN CA C 53.040 0.400 1 173 45 45 ASN CB C 38.944 0.400 1 174 45 45 ASN N N 125.561 0.400 1 175 46 46 LYS H H 7.950 0.040 1 176 46 46 LYS CA C 55.616 0.400 1 177 46 46 LYS CB C 34.422 0.400 1 178 46 46 LYS N N 120.733 0.400 1 179 47 47 PHE H H 9.107 0.040 1 180 47 47 PHE CA C 56.398 0.400 1 181 47 47 PHE CB C 42.787 0.400 1 182 47 47 PHE N N 126.039 0.400 1 183 48 48 THR H H 8.316 0.040 1 184 48 48 THR CA C 62.043 0.400 1 185 48 48 THR CB C 70.037 0.400 1 186 48 48 THR N N 115.637 0.400 1 187 49 49 VAL H H 9.665 0.040 1 188 49 49 VAL CA C 60.573 0.400 1 189 49 49 VAL CB C 34.282 0.400 1 190 49 49 VAL N N 127.998 0.400 1 191 50 50 LYS H H 9.276 0.040 1 192 50 50 LYS CA C 55.614 0.400 1 193 50 50 LYS CB C 32.107 0.400 1 194 50 50 LYS N N 128.300 0.400 1 195 51 51 GLU H H 9.389 0.040 1 196 51 51 GLU CA C 55.004 0.400 1 197 51 51 GLU CB C 30.817 0.400 1 198 51 51 GLU N N 128.781 0.400 1 199 52 52 SER H H 9.071 0.040 1 200 52 52 SER CA C 56.525 0.400 1 201 52 52 SER CB C 65.163 0.400 1 202 52 52 SER N N 121.107 0.400 1 203 53 53 SER H H 9.014 0.040 1 204 53 53 SER CA C 57.169 0.400 1 205 53 53 SER CB C 67.962 0.400 1 206 53 53 SER N N 121.105 0.400 1 207 54 54 ASN H H 9.223 0.040 1 208 54 54 ASN CA C 54.448 0.400 1 209 54 54 ASN CB C 37.891 0.400 1 210 54 54 ASN N N 115.752 0.400 1 211 55 55 PHE H H 8.207 0.040 1 212 55 55 PHE CA C 59.927 0.400 1 213 55 55 PHE CB C 40.571 0.400 1 214 55 55 PHE N N 114.128 0.400 1 215 56 56 ARG H H 7.463 0.040 1 216 56 56 ARG CA C 55.452 0.400 1 217 56 56 ARG CB C 30.685 0.400 1 218 56 56 ARG N N 112.282 0.400 1 219 57 57 ASN H H 8.543 0.040 1 220 57 57 ASN CA C 52.864 0.400 1 221 57 57 ASN CB C 40.590 0.400 1 222 57 57 ASN N N 119.095 0.400 1 223 58 58 ILE H H 8.892 0.040 1 224 58 58 ILE CA C 59.947 0.400 1 225 58 58 ILE CB C 43.028 0.400 1 226 58 58 ILE N N 117.658 0.400 1 227 59 59 ASP H H 8.527 0.040 1 228 59 59 ASP CA C 53.404 0.400 1 229 59 59 ASP CB C 33.052 0.400 1 230 59 59 ASP N N 123.204 0.400 1 231 60 60 VAL H H 9.130 0.040 1 232 60 60 VAL CA C 61.856 0.400 1 233 60 60 VAL CB C 34.342 0.400 1 234 60 60 VAL N N 123.349 0.400 1 235 61 61 VAL H H 8.259 0.040 1 236 61 61 VAL CA C 60.028 0.400 1 237 61 61 VAL CB C 34.415 0.400 1 238 61 61 VAL N N 125.868 0.400 1 239 62 62 PHE H H 8.390 0.040 1 240 62 62 PHE CA C 55.515 0.400 1 241 62 62 PHE CB C 40.516 0.400 1 242 62 62 PHE N N 121.454 0.400 1 243 63 63 GLU H H 9.466 0.040 1 244 63 63 GLU CA C 53.589 0.400 1 245 63 63 GLU CB C 32.507 0.400 1 246 63 63 GLU N N 120.486 0.400 1 247 64 64 LEU H H 8.958 0.040 1 248 64 64 LEU CA C 56.374 0.400 1 249 64 64 LEU CB C 41.190 0.400 1 250 64 64 LEU N N 125.205 0.400 1 251 65 65 GLY H H 9.305 0.040 1 252 65 65 GLY CA C 46.139 0.400 1 253 65 65 GLY N N 108.380 0.400 1 254 66 66 VAL H H 7.952 0.040 1 255 66 66 VAL CA C 62.476 0.400 1 256 66 66 VAL CB C 32.717 0.400 1 257 66 66 VAL N N 122.426 0.400 1 258 67 67 ASP H H 8.792 0.040 1 259 67 67 ASP CA C 55.420 0.400 1 260 67 67 ASP CB C 41.774 0.400 1 261 67 67 ASP N N 132.355 0.400 1 262 68 68 PHE H H 9.272 0.040 1 263 68 68 PHE CA C 56.066 0.400 1 264 68 68 PHE CB C 41.819 0.400 1 265 68 68 PHE N N 120.308 0.400 1 266 69 69 ALA H H 8.401 0.040 1 267 69 69 ALA CA C 50.853 0.400 1 268 69 69 ALA CB C 21.071 0.400 1 269 69 69 ALA N N 122.156 0.400 1 270 70 70 TYR H H 8.465 0.040 1 271 70 70 TYR CA C 57.824 0.400 1 272 70 70 TYR CB C 42.967 0.400 1 273 70 70 TYR N N 123.605 0.400 1 274 71 71 SER H H 7.773 0.040 1 275 71 71 SER CA C 56.090 0.400 1 276 71 71 SER CB C 64.627 0.400 1 277 71 71 SER N N 121.114 0.400 1 278 72 72 LEU H H 9.037 0.040 1 279 72 72 LEU CA C 54.372 0.400 1 280 72 72 LEU N N 122.312 0.400 1 281 73 73 ALA CA C 54.548 0.400 1 282 73 73 ALA CB C 17.505 0.400 1 283 74 74 ASP H H 7.666 0.040 1 284 74 74 ASP CA C 53.126 0.400 1 285 74 74 ASP CB C 40.155 0.400 1 286 74 74 ASP N N 114.729 0.400 1 287 75 75 GLY H H 7.978 0.040 1 288 75 75 GLY CA C 44.469 0.400 1 289 75 75 GLY N N 108.861 0.400 1 290 76 76 THR H H 7.786 0.040 1 291 76 76 THR CA C 64.989 0.400 1 292 76 76 THR CB C 67.908 0.400 1 293 76 76 THR N N 119.337 0.400 1 294 77 77 GLU H H 8.617 0.040 1 295 77 77 GLU CA C 57.307 0.400 1 296 77 77 GLU CB C 30.857 0.400 1 297 77 77 GLU N N 128.947 0.400 1 298 78 78 LEU H H 8.942 0.040 1 299 78 78 LEU CA C 53.491 0.400 1 300 78 78 LEU CB C 46.440 0.400 1 301 78 78 LEU N N 122.241 0.400 1 302 79 79 THR H H 8.563 0.040 1 303 79 79 THR CA C 60.475 0.400 1 304 79 79 THR CB C 70.821 0.400 1 305 79 79 THR N N 112.822 0.400 1 306 80 80 GLY H H 8.518 0.040 1 307 80 80 GLY CA C 46.572 0.400 1 308 80 80 GLY N N 110.773 0.400 1 309 81 81 THR H H 6.774 0.040 1 310 81 81 THR CA C 60.405 0.400 1 311 81 81 THR CB C 72.899 0.400 1 312 81 81 THR N N 107.088 0.400 1 313 82 82 TRP H H 9.348 0.040 1 314 82 82 TRP CA C 55.866 0.400 1 315 82 82 TRP CB C 32.527 0.400 1 316 82 82 TRP N N 123.648 0.400 1 317 83 83 THR H H 9.304 0.040 1 318 83 83 THR CA C 60.440 0.400 1 319 83 83 THR CB C 72.115 0.400 1 320 83 83 THR N N 113.672 0.400 1 321 84 84 MET H H 8.928 0.040 1 322 84 84 MET CA C 54.041 0.400 1 323 84 84 MET CB C 33.045 0.400 1 324 84 84 MET N N 121.310 0.400 1 325 85 85 GLU H H 9.089 0.040 1 326 85 85 GLU CA C 54.872 0.400 1 327 85 85 GLU CB C 30.615 0.400 1 328 85 85 GLU N N 127.774 0.400 1 329 86 86 GLY H H 9.072 0.040 1 330 86 86 GLY CA C 47.664 0.400 1 331 86 86 GLY N N 117.172 0.400 1 332 87 87 ASN H H 8.858 0.040 1 333 87 87 ASN CA C 53.194 0.400 1 334 87 87 ASN CB C 38.639 0.400 1 335 87 87 ASN N N 123.455 0.400 1 336 88 88 LYS H H 8.032 0.040 1 337 88 88 LYS CA C 55.761 0.400 1 338 88 88 LYS CB C 34.816 0.400 1 339 88 88 LYS N N 119.280 0.400 1 340 89 89 LEU H H 8.549 0.040 1 341 89 89 LEU CA C 53.887 0.400 1 342 89 89 LEU CB C 44.392 0.400 1 343 89 89 LEU N N 124.609 0.400 1 344 90 90 VAL H H 9.587 0.040 1 345 90 90 VAL CA C 62.755 0.400 1 346 90 90 VAL CB C 33.451 0.400 1 347 90 90 VAL N N 126.029 0.400 1 348 91 91 GLY H H 10.130 0.040 1 349 91 91 GLY CA C 44.302 0.400 1 350 91 91 GLY N N 124.027 0.400 1 351 92 92 LYS H H 7.633 0.040 1 352 92 92 LYS CA C 55.146 0.400 1 353 92 92 LYS CB C 33.215 0.400 1 354 92 92 LYS N N 124.825 0.400 1 355 93 93 PHE H H 9.030 0.040 1 356 93 93 PHE CA C 55.611 0.400 1 357 93 93 PHE CB C 43.425 0.400 1 358 93 93 PHE N N 123.340 0.400 1 359 94 94 LYS H H 9.351 0.040 1 360 94 94 LYS CA C 54.744 0.400 1 361 94 94 LYS CB C 35.485 0.400 1 362 94 94 LYS N N 121.381 0.400 1 363 95 95 ARG H H 8.741 0.040 1 364 95 95 ARG CA C 56.725 0.400 1 365 95 95 ARG CB C 30.811 0.400 1 366 95 95 ARG N N 123.903 0.400 1 367 96 96 VAL H H 8.409 0.040 1 368 96 96 VAL CA C 65.397 0.400 1 369 96 96 VAL CB C 32.390 0.400 1 370 96 96 VAL N N 126.232 0.400 1 371 97 97 ASP H H 9.155 0.040 1 372 97 97 ASP CA C 56.509 0.400 1 373 97 97 ASP CB C 38.695 0.400 1 374 97 97 ASP N N 118.848 0.400 1 375 98 98 ASN H H 8.648 0.040 1 376 98 98 ASN CA C 51.497 0.400 1 377 98 98 ASN CB C 39.278 0.400 1 378 98 98 ASN N N 117.069 0.400 1 379 99 99 GLY H H 7.966 0.040 1 380 99 99 GLY CA C 46.507 0.400 1 381 99 99 GLY N N 109.365 0.400 1 382 100 100 LYS H H 8.171 0.040 1 383 100 100 LYS CA C 56.992 0.400 1 384 100 100 LYS CB C 34.094 0.400 1 385 100 100 LYS N N 120.234 0.400 1 386 101 101 GLU H H 8.410 0.040 1 387 101 101 GLU CA C 56.170 0.400 1 388 101 101 GLU CB C 32.736 0.400 1 389 101 101 GLU N N 119.682 0.400 1 390 102 102 LEU H H 9.080 0.040 1 391 102 102 LEU CA C 54.141 0.400 1 392 102 102 LEU CB C 46.429 0.400 1 393 102 102 LEU N N 127.643 0.400 1 394 103 103 ILE H H 8.674 0.040 1 395 103 103 ILE CA C 59.026 0.400 1 396 103 103 ILE CB C 39.489 0.400 1 397 103 103 ILE N N 125.961 0.400 1 398 104 104 ALA H H 9.508 0.040 1 399 104 104 ALA CA C 49.878 0.400 1 400 104 104 ALA CB C 23.807 0.400 1 401 104 104 ALA N N 122.453 0.400 1 402 105 105 VAL H H 9.234 0.040 1 403 105 105 VAL CA C 61.073 0.400 1 404 105 105 VAL N N 122.427 0.400 1 405 106 106 ARG H H 9.701 0.040 1 406 106 106 ARG CA C 54.906 0.400 1 407 106 106 ARG CB C 33.041 0.400 1 408 106 106 ARG N N 125.657 0.400 1 409 107 107 GLU H H 8.605 0.040 1 410 107 107 GLU CA C 54.389 0.400 1 411 107 107 GLU CB C 34.550 0.400 1 412 107 107 GLU N N 121.040 0.400 1 413 108 108 ILE H H 8.778 0.040 1 414 108 108 ILE CA C 58.701 0.400 1 415 108 108 ILE CB C 37.131 0.400 1 416 108 108 ILE N N 124.117 0.400 1 417 109 109 SER H H 8.982 0.040 1 418 109 109 SER CA C 56.393 0.400 1 419 109 109 SER CB C 63.663 0.400 1 420 109 109 SER N N 123.270 0.400 1 421 110 110 GLY H H 9.249 0.040 1 422 110 110 GLY CA C 47.785 0.400 1 423 110 110 GLY N N 119.613 0.400 1 424 111 111 ASN H H 8.899 0.040 1 425 111 111 ASN CA C 53.028 0.400 1 426 111 111 ASN CB C 38.796 0.400 1 427 111 111 ASN N N 123.947 0.400 1 428 112 112 GLU H H 8.094 0.040 1 429 112 112 GLU CA C 55.214 0.400 1 430 112 112 GLU CB C 33.537 0.400 1 431 112 112 GLU N N 118.280 0.400 1 432 113 113 LEU H H 8.320 0.040 1 433 113 113 LEU CA C 54.036 0.400 1 434 113 113 LEU CB C 43.451 0.400 1 435 113 113 LEU N N 123.611 0.400 1 436 114 114 ILE H H 9.374 0.040 1 437 114 114 ILE CA C 61.305 0.400 1 438 114 114 ILE CB C 38.974 0.400 1 439 114 114 ILE N N 127.642 0.400 1 440 115 115 GLN H H 9.056 0.040 1 441 115 115 GLN CA C 53.463 0.400 1 442 115 115 GLN CB C 42.196 0.400 1 443 115 115 GLN N N 131.005 0.400 1 444 116 116 THR H H 9.297 0.040 1 445 116 116 THR CA C 61.849 0.400 1 446 116 116 THR CB C 70.053 0.400 1 447 116 116 THR N N 125.794 0.400 1 448 117 117 TYR H H 9.484 0.040 1 449 117 117 TYR CA C 53.773 0.400 1 450 117 117 TYR CB C 43.877 0.400 1 451 117 117 TYR N N 127.920 0.400 1 452 118 118 THR H H 9.249 0.040 1 453 118 118 THR CA C 62.290 0.400 1 454 118 118 THR CB C 71.492 0.400 1 455 118 118 THR N N 113.507 0.400 1 456 119 119 TYR H H 9.094 0.040 1 457 119 119 TYR CA C 58.645 0.400 1 458 119 119 TYR CB C 43.136 0.400 1 459 119 119 TYR N N 126.421 0.400 1 460 120 120 GLU H H 9.597 0.040 1 461 120 120 GLU CA C 56.369 0.400 1 462 120 120 GLU CB C 28.888 0.400 1 463 120 120 GLU N N 125.937 0.400 1 464 121 121 GLY H H 8.627 0.040 1 465 121 121 GLY CA C 45.386 0.400 1 466 121 121 GLY N N 102.742 0.400 1 467 122 122 VAL H H 8.411 0.040 1 468 122 122 VAL CA C 62.287 0.400 1 469 122 122 VAL CB C 33.044 0.400 1 470 122 122 VAL N N 123.750 0.400 1 471 123 123 GLU H H 8.619 0.040 1 472 123 123 GLU CA C 53.976 0.400 1 473 123 123 GLU CB C 33.970 0.400 1 474 123 123 GLU N N 126.728 0.400 1 475 124 124 ALA H H 8.881 0.040 1 476 124 124 ALA CA C 51.025 0.400 1 477 124 124 ALA CB C 23.982 0.400 1 478 124 124 ALA N N 125.410 0.400 1 479 125 125 LYS H H 8.952 0.040 1 480 125 125 LYS CA C 54.468 0.400 1 481 125 125 LYS CB C 38.223 0.400 1 482 125 125 LYS N N 115.495 0.400 1 483 126 126 ARG H H 9.005 0.040 1 484 126 126 ARG CA C 56.505 0.400 1 485 126 126 ARG CB C 33.275 0.400 1 486 126 126 ARG N N 118.591 0.400 1 487 127 127 ILE H H 8.871 0.040 1 488 127 127 ILE CA C 61.247 0.400 1 489 127 127 ILE CB C 39.914 0.400 1 490 127 127 ILE N N 123.772 0.400 1 491 128 128 PHE H H 9.947 0.040 1 492 128 128 PHE CA C 55.981 0.400 1 493 128 128 PHE CB C 42.842 0.400 1 494 128 128 PHE N N 126.932 0.400 1 495 129 129 LYS H H 8.979 0.040 1 496 129 129 LYS CA C 54.968 0.400 1 497 129 129 LYS CB C 35.991 0.400 1 498 129 129 LYS N N 119.490 0.400 1 499 130 130 LYS H H 8.610 0.040 1 500 130 130 LYS CA C 56.782 0.400 1 501 130 130 LYS CB C 33.280 0.400 1 502 130 130 LYS N N 125.840 0.400 1 503 131 131 GLU H H 8.411 0.040 1 504 131 131 GLU CA C 58.428 0.400 1 stop_ save_