data_15082 ####################### # 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 15082 _BMRB_flat_file_name bmr15082.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" 130 "13C chemical shifts" 248 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2007-03-08 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 7355 'fabp_clof bound' 7356 'fenofibricAcid 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 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _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 2015-02-06 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 PDB 1AEL "Nmr Structure Of Apo Intestinal Fatty Acid-Binding Protein, 20 Structures" 100.00 131 100.00 100.00 2.92e-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 3.89e-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 2.92e-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 1.12e-86 PDB 1IFB "Refined Apoprotein Structure Of Rat Intestinal Fatty Acid Binding Protein Produced In Escherichia Coli" 100.00 131 100.00 100.00 2.92e-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 2.71e-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 3.16e-86 PDB 1URE "Nmr Structure Of Intestinal Fatty Acid-Binding Protein Complexed With Palmitate, 20 Structures" 100.00 131 100.00 100.00 2.92e-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 2.92e-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 2.92e-87 GB AAA41133 "fatty acid binding protein, partial [Rattus norvegicus]" 60.31 80 100.00 100.00 3.38e-48 GB AAA41138 "intestinal FABP [Rattus norvegicus]" 100.00 132 98.47 98.47 1.38e-84 GB AAA41141 "fatty acid binding protein (FABP) [Rattus norvegicus]" 100.00 132 100.00 100.00 2.71e-87 GB EDL82110 "fatty acid binding protein 2, intestinal [Rattus norvegicus]" 100.00 132 100.00 100.00 2.71e-87 PRF 1202232A "protein,fatty acid binding" 100.00 132 100.00 100.00 2.71e-87 PRF 1202232A:PDB=1IFC "protein,fatty acid binding" 100.00 132 100.00 100.00 2.71e-87 REF NP_037200 "fatty acid-binding protein, intestinal [Rattus norvegicus]" 100.00 132 100.00 100.00 2.71e-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 2.71e-87 stop_ 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_apo-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]' 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 $apo-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 . 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 . 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_apo-Rat_fatty_acid_binding_protein _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' stop_ loop_ _Sample_label $apo-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 52.302 0.400 1 2 1 1 ALA CB C 19.285 0.400 1 3 2 2 PHE H H 9.334 0.040 1 4 2 2 PHE CA C 59.543 0.400 1 5 2 2 PHE CB C 40.203 0.400 1 6 2 2 PHE N N 116.972 0.400 1 7 3 3 ASP H H 7.947 0.040 1 8 3 3 ASP CA C 55.276 0.400 1 9 3 3 ASP CB C 41.534 0.400 1 10 3 3 ASP N N 116.421 0.400 1 11 4 4 GLY H H 8.520 0.040 1 12 4 4 GLY CA C 43.818 0.400 1 13 4 4 GLY N N 108.537 0.400 1 14 5 5 THR H H 8.361 0.040 1 15 5 5 THR CA C 62.291 0.400 1 16 5 5 THR CB C 69.884 0.400 1 17 5 5 THR N N 116.922 0.400 1 18 6 6 TRP H H 9.425 0.040 1 19 6 6 TRP CA C 54.809 0.400 1 20 6 6 TRP CB C 31.384 0.400 1 21 6 6 TRP N N 127.995 0.400 1 22 7 7 LYS H H 9.627 0.040 1 23 7 7 LYS CA C 54.853 0.400 1 24 7 7 LYS CB C 35.411 0.400 1 25 7 7 LYS N N 124.619 0.400 1 26 8 8 VAL H H 8.823 0.040 1 27 8 8 VAL CA C 64.798 0.400 1 28 8 8 VAL CB C 31.499 0.400 1 29 8 8 VAL N N 129.284 0.400 1 30 9 9 ASP H H 9.710 0.040 1 31 9 9 ASP CA C 55.388 0.400 1 32 9 9 ASP CB C 46.803 0.400 1 33 9 9 ASP N N 127.534 0.400 1 34 10 10 ARG H H 7.735 0.040 1 35 10 10 ARG CA C 54.905 0.400 1 36 10 10 ARG CB C 31.840 0.400 1 37 10 10 ARG N N 112.866 0.400 1 38 11 11 ASN H H 8.682 0.040 1 39 11 11 ASN CA C 51.371 0.400 1 40 11 11 ASN CB C 43.470 0.400 1 41 11 11 ASN N N 116.943 0.400 1 42 12 12 GLU H H 9.521 0.040 1 43 12 12 GLU CA C 55.745 0.400 1 44 12 12 GLU CB C 32.573 0.400 1 45 12 12 GLU N N 120.614 0.400 1 46 13 13 ASN H H 9.407 0.040 1 47 13 13 ASN CA C 54.223 0.400 1 48 13 13 ASN CB C 39.704 0.400 1 49 13 13 ASN N N 122.752 0.400 1 50 14 14 TYR H H 8.360 0.040 1 51 14 14 TYR CA C 60.076 0.400 1 52 14 14 TYR CB C 39.928 0.400 1 53 14 14 TYR N N 119.668 0.400 1 54 15 15 GLU H H 9.001 0.040 1 55 15 15 GLU CA C 61.172 0.400 1 56 15 15 GLU CB C 28.211 0.400 1 57 15 15 GLU N N 119.805 0.400 1 58 16 16 LYS H H 7.970 0.040 1 59 16 16 LYS CA C 58.656 0.400 1 60 16 16 LYS CB C 31.599 0.400 1 61 16 16 LYS N N 119.523 0.400 1 62 17 17 PHE H H 7.648 0.040 1 63 17 17 PHE CA C 61.781 0.400 1 64 17 17 PHE CB C 40.281 0.400 1 65 17 17 PHE N N 121.117 0.400 1 66 18 18 MET H H 8.221 0.040 1 67 18 18 MET CA C 59.770 0.400 1 68 18 18 MET CB C 34.057 0.400 1 69 18 18 MET N N 118.257 0.400 1 70 19 19 GLU H H 8.275 0.040 1 71 19 19 GLU CA C 59.755 0.400 1 72 19 19 GLU CB C 29.698 0.400 1 73 19 19 GLU N N 119.507 0.400 1 74 20 20 LYS H H 8.116 0.040 1 75 20 20 LYS CA C 57.254 0.400 1 76 20 20 LYS CB C 31.817 0.400 1 77 20 20 LYS N N 123.775 0.400 1 78 21 21 MET H H 7.573 0.040 1 79 21 21 MET CA C 55.849 0.400 1 80 21 21 MET CB C 32.499 0.400 1 81 21 21 MET N N 114.891 0.400 1 82 22 22 GLY H H 7.807 0.040 1 83 22 22 GLY CA C 45.473 0.400 1 84 22 22 GLY N N 108.467 0.400 1 85 23 23 ILE H H 7.390 0.040 1 86 23 23 ILE CA C 60.594 0.400 1 87 23 23 ILE CB C 37.174 0.400 1 88 23 23 ILE N N 121.483 0.400 1 89 24 24 ASN H H 8.676 0.040 1 90 24 24 ASN CA C 53.992 0.400 1 91 24 24 ASN CB C 39.183 0.400 1 92 24 24 ASN N N 127.087 0.400 1 93 25 25 VAL H H 8.397 0.040 1 94 25 25 VAL CA C 66.269 0.400 1 95 25 25 VAL CB C 32.063 0.400 1 96 25 25 VAL N N 120.460 0.400 1 97 26 26 VAL H H 7.705 0.040 1 98 26 26 VAL CA C 66.055 0.400 1 99 26 26 VAL CB C 31.879 0.400 1 100 26 26 VAL N N 121.230 0.400 1 101 27 27 LYS H H 7.870 0.040 1 102 27 27 LYS CA C 58.911 0.400 1 103 27 27 LYS CB C 32.747 0.400 1 104 27 27 LYS N N 118.812 0.400 1 105 28 28 ARG H H 8.481 0.040 1 106 28 28 ARG CA C 59.234 0.400 1 107 28 28 ARG CB C 30.629 0.400 1 108 28 28 ARG N N 120.755 0.400 1 109 29 29 LYS H H 7.718 0.040 1 110 29 29 LYS CA C 59.159 0.400 1 111 29 29 LYS CB C 31.965 0.400 1 112 29 29 LYS N N 119.719 0.400 1 113 30 30 LEU H H 7.521 0.040 1 114 30 30 LEU CA C 56.914 0.400 1 115 30 30 LEU CB C 42.095 0.400 1 116 30 30 LEU N N 118.297 0.400 1 117 31 31 GLY H H 8.244 0.040 1 118 31 31 GLY CA C 46.864 0.400 1 119 31 31 GLY N N 120.599 0.400 1 120 32 32 ALA H H 7.759 0.040 1 121 32 32 ALA CA C 51.274 0.400 1 122 32 32 ALA CB C 18.835 0.400 1 123 32 32 ALA N N 119.821 0.400 1 124 33 33 HIS H H 7.554 0.040 1 125 33 33 HIS CA C 54.067 0.400 1 126 33 33 HIS CB C 28.476 0.400 1 127 33 33 HIS N N 117.438 0.400 1 128 34 34 ASP H H 7.448 0.040 1 129 34 34 ASP CA C 54.406 0.400 1 130 34 34 ASP CB C 41.301 0.400 1 131 34 34 ASP N N 118.291 0.400 1 132 35 35 ASN H H 9.143 0.040 1 133 35 35 ASN CA C 53.850 0.400 1 134 35 35 ASN CB C 37.566 0.400 1 135 35 35 ASN N N 119.103 0.400 1 136 36 36 LEU H H 6.990 0.040 1 137 36 36 LEU CA C 56.980 0.400 1 138 36 36 LEU CB C 42.230 0.400 1 139 36 36 LEU N N 119.263 0.400 1 140 37 37 LYS H H 9.377 0.040 1 141 37 37 LYS CA C 54.654 0.400 1 142 37 37 LYS CB C 36.323 0.400 1 143 37 37 LYS N N 126.947 0.400 1 144 38 38 LEU H H 9.451 0.040 1 145 38 38 LEU CA C 52.499 0.400 1 146 38 38 LEU CB C 45.537 0.400 1 147 38 38 LEU N N 123.274 0.400 1 148 39 39 THR H H 9.149 0.040 1 149 39 39 THR CA C 62.550 0.400 1 150 39 39 THR CB C 70.034 0.400 1 151 39 39 THR N N 120.927 0.400 1 152 40 40 ILE H H 9.556 0.040 1 153 40 40 ILE CA C 61.517 0.400 1 154 40 40 ILE CB C 40.002 0.400 1 155 40 40 ILE N N 116.351 0.400 1 156 41 41 THR H H 8.778 0.040 1 157 41 41 THR CA C 61.451 0.400 1 158 41 41 THR CB C 71.453 0.400 1 159 41 41 THR N N 122.977 0.400 1 160 42 42 GLN H H 8.969 0.040 1 161 42 42 GLN CA C 54.354 0.400 1 162 42 42 GLN CB C 29.575 0.400 1 163 42 42 GLN N N 113.305 0.400 1 164 43 43 GLU H H 8.859 0.040 1 165 43 43 GLU CA C 54.565 0.400 1 166 43 43 GLU CB C 31.243 0.400 1 167 43 43 GLU N N 115.280 0.400 1 168 44 44 GLY H H 9.015 0.040 1 169 44 44 GLY CA C 47.291 0.400 1 170 44 44 GLY N N 117.720 0.400 1 171 45 45 ASN H H 8.871 0.040 1 172 45 45 ASN CA C 52.957 0.400 1 173 45 45 ASN CB C 38.936 0.400 1 174 45 45 ASN N N 125.599 0.400 1 175 46 46 LYS H H 7.922 0.040 1 176 46 46 LYS CA C 55.464 0.400 1 177 46 46 LYS CB C 34.450 0.400 1 178 46 46 LYS N N 120.755 0.400 1 179 47 47 PHE H H 9.046 0.040 1 180 47 47 PHE CA C 56.262 0.400 1 181 47 47 PHE CB C 42.968 0.400 1 182 47 47 PHE N N 125.885 0.400 1 183 48 48 THR H H 8.287 0.040 1 184 48 48 THR CA C 61.941 0.400 1 185 48 48 THR CB C 69.894 0.400 1 186 48 48 THR N N 115.604 0.400 1 187 49 49 VAL H H 9.586 0.040 1 188 49 49 VAL CA C 60.501 0.400 1 189 49 49 VAL N N 127.634 0.400 1 190 50 50 LYS H H 9.241 0.040 1 191 50 50 LYS CA C 55.633 0.400 1 192 50 50 LYS CB C 32.884 0.400 1 193 50 50 LYS N N 128.750 0.400 1 194 51 51 GLU H H 9.362 0.040 1 195 51 51 GLU CA C 55.063 0.400 1 196 51 51 GLU CB C 30.270 0.400 1 197 51 51 GLU N N 127.180 0.400 1 198 52 52 SER H H 9.124 0.040 1 199 52 52 SER CA C 56.557 0.400 1 200 52 52 SER CB C 64.924 0.400 1 201 52 52 SER N N 121.187 0.400 1 202 53 53 SER H H 8.895 0.040 1 203 53 53 SER CA C 56.924 0.400 1 204 53 53 SER CB C 67.453 0.400 1 205 53 53 SER N N 120.728 0.400 1 206 54 54 ASN H H 9.019 0.040 1 207 54 54 ASN CA C 54.724 0.400 1 208 54 54 ASN CB C 37.859 0.400 1 209 54 54 ASN N N 116.356 0.400 1 210 55 55 PHE H H 8.023 0.040 1 211 55 55 PHE CA C 58.452 0.400 1 212 55 55 PHE CB C 40.879 0.400 1 213 55 55 PHE N N 114.811 0.400 1 214 56 56 ARG H H 7.356 0.040 1 215 56 56 ARG CA C 55.921 0.400 1 216 56 56 ARG CB C 31.834 0.400 1 217 56 56 ARG N N 115.298 0.400 1 218 57 57 ASN H H 8.700 0.040 1 219 57 57 ASN CA C 52.827 0.400 1 220 57 57 ASN CB C 40.425 0.400 1 221 57 57 ASN N N 122.011 0.400 1 222 58 58 ILE H H 8.678 0.040 1 223 58 58 ILE CA C 59.913 0.400 1 224 58 58 ILE CB C 42.752 0.400 1 225 58 58 ILE N N 119.528 0.400 1 226 59 59 ASP H H 8.603 0.040 1 227 59 59 ASP CA C 53.529 0.400 1 228 59 59 ASP CB C 42.014 0.400 1 229 59 59 ASP N N 124.882 0.400 1 230 60 60 VAL H H 9.029 0.040 1 231 60 60 VAL CA C 61.974 0.400 1 232 60 60 VAL N N 125.769 0.400 1 233 61 61 VAL H H 8.254 0.040 1 234 61 61 VAL CA C 60.129 0.400 1 235 61 61 VAL CB C 34.352 0.400 1 236 61 61 VAL N N 126.575 0.400 1 237 62 62 PHE H H 8.309 0.040 1 238 62 62 PHE CA C 55.394 0.400 1 239 62 62 PHE CB C 40.001 0.400 1 240 62 62 PHE N N 121.256 0.400 1 241 63 63 GLU H H 9.440 0.040 1 242 63 63 GLU CA C 53.440 0.400 1 243 63 63 GLU CB C 32.342 0.400 1 244 63 63 GLU N N 120.513 0.400 1 245 64 64 LEU H H 8.901 0.040 1 246 64 64 LEU CA C 56.290 0.400 1 247 64 64 LEU CB C 41.025 0.400 1 248 64 64 LEU N N 125.096 0.400 1 249 65 65 GLY H H 9.242 0.040 1 250 65 65 GLY CA C 46.076 0.400 1 251 65 65 GLY N N 108.491 0.400 1 252 66 66 VAL H H 7.901 0.040 1 253 66 66 VAL CA C 62.385 0.400 1 254 66 66 VAL CB C 32.909 0.400 1 255 66 66 VAL N N 122.423 0.400 1 256 67 67 ASP H H 8.785 0.040 1 257 67 67 ASP CA C 55.499 0.400 1 258 67 67 ASP CB C 42.063 0.400 1 259 67 67 ASP N N 132.595 0.400 1 260 68 68 PHE H H 9.578 0.040 1 261 68 68 PHE CA C 56.047 0.400 1 262 68 68 PHE CB C 41.731 0.400 1 263 68 68 PHE N N 122.409 0.400 1 264 69 69 ALA H H 8.206 0.040 1 265 69 69 ALA CA C 50.757 0.400 1 266 69 69 ALA CB C 20.818 0.400 1 267 69 69 ALA N N 121.506 0.400 1 268 70 70 TYR H H 8.386 0.040 1 269 70 70 TYR CA C 56.005 0.400 1 270 70 70 TYR CB C 42.041 0.400 1 271 70 70 TYR N N 123.013 0.400 1 272 71 71 SER H H 7.686 0.040 1 273 71 71 SER CA C 55.725 0.400 1 274 71 71 SER CB C 64.962 0.400 1 275 71 71 SER N N 118.415 0.400 1 276 72 72 LEU H H 8.162 0.040 1 277 72 72 LEU CA C 54.109 0.400 1 278 72 72 LEU CB C 42.264 0.400 1 279 72 72 LEU N N 121.155 0.400 1 280 73 73 ALA H H 8.691 0.040 1 281 73 73 ALA CA C 54.713 0.400 1 282 73 73 ALA CB C 18.525 0.400 1 283 73 73 ALA N N 123.318 0.400 1 284 74 74 ASP H H 7.593 0.040 1 285 74 74 ASP CA C 54.522 0.400 1 286 74 74 ASP CB C 41.274 0.400 1 287 74 74 ASP N N 112.500 0.400 1 288 75 75 GLY H H 7.860 0.040 1 289 75 75 GLY CA C 44.258 0.400 1 290 75 75 GLY N N 122.119 0.400 1 291 76 76 THR H H 7.793 0.040 1 292 76 76 THR CA C 65.144 0.400 1 293 76 76 THR CB C 68.147 0.400 1 294 76 76 THR N N 119.015 0.400 1 295 77 77 GLU H H 8.328 0.040 1 296 77 77 GLU CA C 57.082 0.400 1 297 77 77 GLU CB C 30.499 0.400 1 298 77 77 GLU N N 112.870 0.400 1 299 78 78 LEU H H 8.820 0.040 1 300 78 78 LEU CA C 53.508 0.400 1 301 78 78 LEU CB C 46.633 0.400 1 302 78 78 LEU N N 123.637 0.400 1 303 79 79 THR H H 8.576 0.040 1 304 79 79 THR CA C 60.151 0.400 1 305 79 79 THR CB C 70.895 0.400 1 306 79 79 THR N N 111.511 0.400 1 307 80 80 GLY H H 8.650 0.040 1 308 80 80 GLY CA C 46.603 0.400 1 309 80 80 GLY N N 111.577 0.400 1 310 81 81 THR H H 6.767 0.040 1 311 81 81 THR CA C 59.662 0.400 1 312 81 81 THR CB C 72.756 0.400 1 313 81 81 THR N N 107.231 0.400 1 314 82 82 TRP H H 9.253 0.040 1 315 82 82 TRP CA C 55.901 0.400 1 316 82 82 TRP CB C 32.651 0.400 1 317 82 82 TRP N N 122.555 0.400 1 318 83 83 THR H H 9.315 0.040 1 319 83 83 THR CA C 60.501 0.400 1 320 83 83 THR CB C 71.977 0.400 1 321 83 83 THR N N 113.741 0.400 1 322 84 84 MET H H 8.911 0.040 1 323 84 84 MET CA C 54.127 0.400 1 324 84 84 MET CB C 33.618 0.400 1 325 84 84 MET N N 121.453 0.400 1 326 85 85 GLU H H 9.083 0.040 1 327 85 85 GLU CA C 54.699 0.400 1 328 85 85 GLU CB C 30.767 0.400 1 329 85 85 GLU N N 128.030 0.400 1 330 86 86 GLY H H 9.083 0.040 1 331 86 86 GLY CA C 47.497 0.400 1 332 86 86 GLY N N 117.270 0.400 1 333 87 87 ASN H H 8.847 0.040 1 334 87 87 ASN CA C 53.183 0.400 1 335 87 87 ASN CB C 38.638 0.400 1 336 87 87 ASN N N 123.348 0.400 1 337 88 88 LYS H H 8.047 0.040 1 338 88 88 LYS CA C 55.713 0.400 1 339 88 88 LYS CB C 35.064 0.400 1 340 88 88 LYS N N 119.284 0.400 1 341 89 89 LEU H H 8.539 0.040 1 342 89 89 LEU CA C 53.876 0.400 1 343 89 89 LEU CB C 44.281 0.400 1 344 89 89 LEU N N 124.018 0.400 1 345 90 90 VAL H H 9.525 0.040 1 346 90 90 VAL CA C 62.353 0.400 1 347 90 90 VAL CB C 33.852 0.400 1 348 90 90 VAL N N 125.059 0.400 1 349 91 91 GLY H H 10.151 0.040 1 350 91 91 GLY CA C 44.544 0.400 1 351 91 91 GLY N N 122.711 0.400 1 352 92 92 LYS H H 7.596 0.040 1 353 92 92 LYS CA C 55.144 0.400 1 354 92 92 LYS CB C 32.873 0.400 1 355 92 92 LYS N N 125.627 0.400 1 356 93 93 PHE H H 8.503 0.040 1 357 93 93 PHE CA C 55.585 0.400 1 358 93 93 PHE CB C 43.946 0.400 1 359 93 93 PHE N N 122.641 0.400 1 360 94 94 LYS H H 9.292 0.040 1 361 94 94 LYS CA C 54.865 0.400 1 362 94 94 LYS CB C 35.954 0.400 1 363 94 94 LYS N N 120.106 0.400 1 364 95 95 ARG H H 8.922 0.040 1 365 95 95 ARG CA C 56.910 0.400 1 366 95 95 ARG CB C 30.825 0.400 1 367 95 95 ARG N N 122.967 0.400 1 368 96 96 VAL H H 8.228 0.040 1 369 96 96 VAL CA C 65.202 0.400 1 370 96 96 VAL CB C 32.428 0.400 1 371 96 96 VAL N N 125.976 0.400 1 372 97 97 ASP H H 9.107 0.040 1 373 97 97 ASP CA C 56.296 0.400 1 374 97 97 ASP CB C 38.828 0.400 1 375 97 97 ASP N N 118.461 0.400 1 376 98 98 ASN H H 8.561 0.040 1 377 98 98 ASN CA C 51.542 0.400 1 378 98 98 ASN CB C 39.218 0.400 1 379 98 98 ASN N N 117.285 0.400 1 380 99 99 GLY H H 7.951 0.040 1 381 99 99 GLY CA C 46.392 0.400 1 382 99 99 GLY N N 109.098 0.400 1 383 100 100 LYS H H 8.183 0.040 1 384 100 100 LYS CA C 57.066 0.400 1 385 100 100 LYS CB C 34.221 0.400 1 386 100 100 LYS N N 120.277 0.400 1 387 101 101 GLU H H 8.525 0.040 1 388 101 101 GLU CA C 56.794 0.400 1 389 101 101 GLU CB C 32.228 0.400 1 390 101 101 GLU N N 120.076 0.400 1 391 102 102 LEU H H 8.779 0.040 1 392 102 102 LEU CA C 54.751 0.400 1 393 102 102 LEU CB C 46.371 0.400 1 394 102 102 LEU N N 126.163 0.400 1 395 103 103 ILE H H 8.402 0.040 1 396 103 103 ILE CA C 58.784 0.400 1 397 103 103 ILE CB C 38.883 0.400 1 398 103 103 ILE N N 125.718 0.400 1 399 104 104 ALA H H 9.495 0.040 1 400 104 104 ALA CA C 49.370 0.400 1 401 104 104 ALA CB C 24.200 0.400 1 402 104 104 ALA N N 112.241 0.400 1 403 105 105 VAL H H 9.175 0.040 1 404 105 105 VAL CA C 60.886 0.400 1 405 105 105 VAL CB C 35.992 0.400 1 406 105 105 VAL N N 121.440 0.400 1 407 106 106 ARG H H 9.600 0.040 1 408 106 106 ARG CA C 54.984 0.400 1 409 106 106 ARG CB C 33.663 0.400 1 410 106 106 ARG N N 125.095 0.400 1 411 107 107 GLU H H 8.586 0.040 1 412 107 107 GLU CA C 54.268 0.400 1 413 107 107 GLU CB C 34.236 0.400 1 414 107 107 GLU N N 120.827 0.400 1 415 108 108 ILE H H 8.817 0.040 1 416 108 108 ILE CA C 58.574 0.400 1 417 108 108 ILE CB C 37.295 0.400 1 418 108 108 ILE N N 124.131 0.400 1 419 109 109 SER H H 8.996 0.040 1 420 109 109 SER CA C 56.273 0.400 1 421 109 109 SER CB C 63.614 0.400 1 422 109 109 SER N N 123.369 0.400 1 423 110 110 GLY H H 9.257 0.040 1 424 110 110 GLY CA C 47.609 0.400 1 425 110 110 GLY N N 119.701 0.400 1 426 111 111 ASN H H 8.894 0.040 1 427 111 111 ASN CA C 52.932 0.400 1 428 111 111 ASN CB C 38.788 0.400 1 429 111 111 ASN N N 123.691 0.400 1 430 112 112 GLU H H 8.091 0.040 1 431 112 112 GLU CA C 55.178 0.400 1 432 112 112 GLU CB C 33.379 0.400 1 433 112 112 GLU N N 118.528 0.400 1 434 113 113 LEU H H 8.364 0.040 1 435 113 113 LEU CA C 54.195 0.400 1 436 113 113 LEU CB C 43.471 0.400 1 437 113 113 LEU N N 123.585 0.400 1 438 114 114 ILE H H 9.411 0.040 1 439 114 114 ILE CA C 61.195 0.400 1 440 114 114 ILE CB C 39.110 0.400 1 441 114 114 ILE N N 127.235 0.400 1 442 115 115 GLN H H 9.383 0.040 1 443 115 115 GLN CA C 53.387 0.400 1 444 115 115 GLN CB C 33.868 0.400 1 445 115 115 GLN N N 130.870 0.400 1 446 116 116 THR H H 9.564 0.040 1 447 116 116 THR CA C 61.745 0.400 1 448 116 116 THR CB C 70.019 0.400 1 449 116 116 THR N N 126.601 0.400 1 450 117 117 TYR H H 9.316 0.040 1 451 117 117 TYR CA C 53.845 0.400 1 452 117 117 TYR CB C 43.027 0.400 1 453 117 117 TYR N N 125.402 0.400 1 454 118 118 THR H H 9.119 0.040 1 455 118 118 THR CA C 62.090 0.400 1 456 118 118 THR CB C 70.549 0.400 1 457 118 118 THR N N 115.270 0.400 1 458 119 119 TYR H H 9.160 0.040 1 459 119 119 TYR CA C 57.733 0.400 1 460 119 119 TYR CB C 43.507 0.400 1 461 119 119 TYR N N 127.592 0.400 1 462 120 120 GLU H H 9.543 0.040 1 463 120 120 GLU CA C 56.423 0.400 1 464 120 120 GLU CB C 28.901 0.400 1 465 120 120 GLU N N 126.291 0.400 1 466 121 121 GLY H H 8.607 0.040 1 467 121 121 GLY CA C 45.315 0.400 1 468 121 121 GLY N N 102.818 0.400 1 469 122 122 VAL H H 8.379 0.040 1 470 122 122 VAL CA C 62.407 0.400 1 471 122 122 VAL CB C 33.176 0.400 1 472 122 122 VAL N N 123.643 0.400 1 473 123 123 GLU H H 8.637 0.040 1 474 123 123 GLU CA C 54.156 0.400 1 475 123 123 GLU CB C 33.462 0.400 1 476 123 123 GLU N N 128.114 0.400 1 477 124 124 ALA H H 9.308 0.040 1 478 124 124 ALA CA C 50.566 0.400 1 479 124 124 ALA CB C 24.135 0.400 1 480 124 124 ALA N N 126.963 0.400 1 481 125 125 LYS H H 9.004 0.040 1 482 125 125 LYS CA C 54.478 0.400 1 483 125 125 LYS CB C 37.532 0.400 1 484 125 125 LYS N N 117.176 0.400 1 485 126 126 ARG H H 9.020 0.040 1 486 126 126 ARG CA C 56.368 0.400 1 487 126 126 ARG CB C 33.293 0.400 1 488 126 126 ARG N N 119.925 0.400 1 489 127 127 ILE H H 8.831 0.040 1 490 127 127 ILE CA C 61.336 0.400 1 491 127 127 ILE CB C 39.731 0.400 1 492 127 127 ILE N N 124.290 0.400 1 493 128 128 PHE H H 9.982 0.040 1 494 128 128 PHE CA C 55.956 0.400 1 495 128 128 PHE CB C 43.020 0.400 1 496 128 128 PHE N N 126.870 0.400 1 497 129 129 LYS H H 8.990 0.040 1 498 129 129 LYS CA C 54.965 0.400 1 499 129 129 LYS CB C 35.980 0.400 1 500 129 129 LYS N N 119.741 0.400 1 501 130 130 LYS H H 8.702 0.040 1 502 130 130 LYS CA C 57.027 0.400 1 503 130 130 LYS CB C 33.284 0.400 1 504 130 130 LYS N N 126.079 0.400 1 505 131 131 GLU H H 8.396 0.040 1 506 131 131 GLU CA C 58.317 0.400 1 507 131 131 GLU CB C 31.648 0.400 1 stop_ save_