data_7357 ####################### # 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 7357 _BMRB_flat_file_name bmr7357.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" 239 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2007-03-09 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15082 apo 7355 'Clofibric_acid bound' 7356 'fenofibricAcid 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 365 _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 Tolfenamic_acid $Tolfenamic_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 7356 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_TOLF _Saveframe_category ligand _Mol_type "non-polymer (non_polymer)" _Name_common Tolfenamic_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_Tolfenamic_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]' 'Tolfenamic 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 $Tolfenamic_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 $Tolfenamic_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 H H 9.339 0.040 1 2 1 1 ALA CA C 52.271 0.400 1 3 1 1 ALA CB C 19.242 0.400 1 4 1 1 ALA N N 116.750 0.400 1 5 2 2 PHE H H 8.787 0.040 1 6 2 2 PHE CA C 59.676 0.400 1 7 2 2 PHE CB C 40.000 0.400 1 8 2 2 PHE N N 116.548 0.400 1 9 4 4 GLY H H 8.637 0.040 1 10 4 4 GLY CA C 52.721 0.400 1 11 4 4 GLY N N 123.567 0.400 1 12 5 5 THR H H 8.796 0.040 1 13 5 5 THR CA C 62.505 0.400 1 14 5 5 THR CB C 70.193 0.400 1 15 5 5 THR N N 114.114 0.400 1 16 6 6 TRP H H 9.532 0.040 1 17 6 6 TRP CA C 54.839 0.400 1 18 6 6 TRP CB C 31.480 0.400 1 19 6 6 TRP N N 115.585 0.400 1 20 7 7 LYS H H 9.273 0.040 1 21 7 7 LYS CA C 54.839 0.400 1 22 7 7 LYS CB C 35.534 0.400 1 23 7 7 LYS N N 118.921 0.400 1 24 8 8 VAL H H 9.131 0.040 1 25 8 8 VAL CA C 65.085 0.400 1 26 8 8 VAL CB C 31.626 0.400 1 27 8 8 VAL N N 110.352 0.400 1 28 9 9 ASP H H 8.736 0.040 1 29 9 9 ASP CA C 55.430 0.400 1 30 9 9 ASP CB C 46.796 0.400 1 31 9 9 ASP N N 117.080 0.400 1 32 10 10 ARG H H 8.121 0.040 1 33 10 10 ARG CA C 54.881 0.400 1 34 10 10 ARG CB C 31.992 0.400 1 35 10 10 ARG N N 114.337 0.400 1 36 11 11 ASN H H 8.989 0.040 1 37 11 11 ASN CA C 51.219 0.400 1 38 11 11 ASN CB C 43.242 0.400 1 39 11 11 ASN N N 118.167 0.400 1 40 12 12 GLU H H 9.447 0.040 1 41 12 12 GLU CA C 55.733 0.400 1 42 12 12 GLU CB C 32.373 0.400 1 43 12 12 GLU N N 121.287 0.400 1 44 13 13 ASN H H 8.907 0.040 1 45 13 13 ASN CA C 54.011 0.400 1 46 13 13 ASN CB C 39.456 0.400 1 47 13 13 ASN N N 121.181 0.400 1 48 14 14 TYR H H 8.538 0.040 1 49 14 14 TYR CA C 60.372 0.400 1 50 14 14 TYR CB C 40.193 0.400 1 51 14 14 TYR N N 119.221 0.400 1 52 15 15 GLU H H 8.651 0.040 1 53 15 15 GLU CA C 61.326 0.400 1 54 15 15 GLU CB C 28.265 0.400 1 55 15 15 GLU N N 119.361 0.400 1 56 16 16 LYS H H 7.927 0.040 1 57 16 16 LYS CA C 58.687 0.400 1 58 16 16 LYS CB C 31.501 0.400 1 59 16 16 LYS N N 120.034 0.400 1 60 17 17 PHE H H 7.900 0.040 1 61 17 17 PHE CA C 62.021 0.400 1 62 17 17 PHE CB C 40.412 0.400 1 63 17 17 PHE N N 119.799 0.400 1 64 19 19 GLU H H 8.113 0.040 1 65 19 19 GLU CA C 59.655 0.400 1 66 19 19 GLU CB C 29.486 0.400 1 67 19 19 GLU N N 120.833 0.400 1 68 20 20 LYS H H 7.855 0.040 1 69 20 20 LYS CA C 57.346 0.400 1 70 20 20 LYS CB C 32.232 0.400 1 71 20 20 LYS N N 119.816 0.400 1 72 21 21 MET H H 7.664 0.040 1 73 21 21 MET CA C 55.726 0.400 1 74 21 21 MET CB C 32.477 0.400 1 75 21 21 MET N N 119.269 0.400 1 76 22 22 GLY H H 7.668 0.040 1 77 22 22 GLY CA C 45.388 0.400 1 78 22 22 GLY N N 124.831 0.400 1 79 23 23 ILE H H 8.114 0.040 1 80 23 23 ILE CA C 60.443 0.400 1 81 23 23 ILE CB C 37.008 0.400 1 82 23 23 ILE N N 115.177 0.400 1 83 24 24 ASN H H 8.770 0.040 1 84 24 24 ASN CA C 54.219 0.400 1 85 24 24 ASN CB C 39.805 0.400 1 86 24 24 ASN N N 119.127 0.400 1 87 25 25 VAL H H 8.178 0.040 1 88 25 25 VAL CA C 66.401 0.400 1 89 25 25 VAL CB C 31.858 0.400 1 90 25 25 VAL N N 121.224 0.400 1 91 26 26 VAL H H 7.761 0.040 1 92 26 26 VAL CA C 66.272 0.400 1 93 26 26 VAL CB C 31.398 0.400 1 94 26 26 VAL N N 119.934 0.400 1 95 27 27 LYS H H 8.050 0.040 1 96 27 27 LYS CA C 58.453 0.400 1 97 27 27 LYS CB C 32.774 0.400 1 98 27 27 LYS N N 119.055 0.400 1 99 28 28 ARG H H 8.168 0.040 1 100 28 28 ARG CA C 59.300 0.400 1 101 28 28 ARG CB C 30.615 0.400 1 102 28 28 ARG N N 119.705 0.400 1 103 29 29 LYS H H 7.690 0.040 1 104 29 29 LYS CA C 59.104 0.400 1 105 29 29 LYS CB C 32.292 0.400 1 106 29 29 LYS N N 119.030 0.400 1 107 30 30 LEU H H 7.851 0.040 1 108 30 30 LEU CA C 56.639 0.400 1 109 30 30 LEU CB C 42.429 0.400 1 110 30 30 LEU N N 120.997 0.400 1 111 31 31 GLY H H 8.155 0.040 1 112 31 31 GLY CA C 45.929 0.400 1 113 31 31 GLY N N 123.636 0.400 1 114 32 32 ALA H H 7.667 0.040 1 115 32 32 ALA CA C 53.431 0.400 1 116 32 32 ALA CB C 19.022 0.400 1 117 32 32 ALA N N 118.589 0.400 1 118 33 33 HIS H H 7.472 0.040 1 119 33 33 HIS CA C 54.003 0.400 1 120 33 33 HIS CB C 28.464 0.400 1 121 33 33 HIS N N 117.653 0.400 1 122 34 34 ASP H H 8.086 0.040 1 123 34 34 ASP CA C 54.571 0.400 1 124 34 34 ASP CB C 41.327 0.400 1 125 34 34 ASP N N 118.476 0.400 1 126 35 35 ASN H H 8.285 0.040 1 127 35 35 ASN CA C 53.617 0.400 1 128 35 35 ASN CB C 37.494 0.400 1 129 35 35 ASN N N 118.797 0.400 1 130 36 36 LEU H H 8.030 0.040 1 131 36 36 LEU CA C 57.256 0.400 1 132 36 36 LEU CB C 42.439 0.400 1 133 36 36 LEU N N 115.458 0.400 1 134 37 37 LYS H H 9.451 0.040 1 135 37 37 LYS CA C 54.625 0.400 1 136 37 37 LYS CB C 36.420 0.400 1 137 37 37 LYS N N 115.143 0.400 1 138 38 38 LEU H H 9.287 0.040 1 139 38 38 LEU CA C 52.394 0.400 1 140 38 38 LEU CB C 45.668 0.400 1 141 38 38 LEU N N 122.102 0.400 1 142 39 39 THR H H 9.295 0.040 1 143 39 39 THR CA C 62.613 0.400 1 144 39 39 THR CB C 70.449 0.400 1 145 39 39 THR N N 116.773 0.400 1 146 40 40 ILE H H 9.276 0.040 1 147 40 40 ILE CA C 61.610 0.400 1 148 40 40 ILE CB C 40.317 0.400 1 149 40 40 ILE N N 115.845 0.400 1 150 41 41 THR H H 8.869 0.040 1 151 41 41 THR CA C 61.557 0.400 1 152 41 41 THR CB C 71.571 0.400 1 153 41 41 THR N N 117.865 0.400 1 154 42 42 GLN H H 8.930 0.040 1 155 42 42 GLN CA C 54.310 0.400 1 156 42 42 GLN CB C 29.425 0.400 1 157 42 42 GLN N N 110.870 0.400 1 158 43 43 GLU H H 8.940 0.040 1 159 43 43 GLU CA C 54.500 0.400 1 160 43 43 GLU CB C 31.397 0.400 1 161 43 43 GLU N N 114.006 0.400 1 162 44 44 GLY H H 8.995 0.040 1 163 44 44 GLY CA C 47.110 0.400 1 164 44 44 GLY N N 119.696 0.400 1 165 45 45 ASN H H 8.509 0.040 1 166 45 45 ASN CA C 52.887 0.400 1 167 45 45 ASN CB C 39.137 0.400 1 168 45 45 ASN N N 123.661 0.400 1 169 46 46 LYS H H 8.391 0.040 1 170 46 46 LYS CA C 55.485 0.400 1 171 46 46 LYS CB C 34.400 0.400 1 172 46 46 LYS N N 122.778 0.400 1 173 47 47 PHE H H 8.760 0.040 1 174 47 47 PHE CA C 56.456 0.400 1 175 47 47 PHE CB C 42.899 0.400 1 176 47 47 PHE N N 121.613 0.400 1 177 48 48 THR H H 8.854 0.040 1 178 48 48 THR CA C 62.105 0.400 1 179 48 48 THR CB C 70.317 0.400 1 180 48 48 THR N N 113.258 0.400 1 181 49 49 VAL H H 9.536 0.040 1 182 49 49 VAL CA C 60.748 0.400 1 183 49 49 VAL CB C 34.292 0.400 1 184 49 49 VAL N N 110.256 0.400 1 185 50 50 LYS H H 9.301 0.040 1 186 50 50 LYS CA C 55.642 0.400 1 187 50 50 LYS N N 110.503 0.400 1 188 51 51 GLU H H 9.061 0.040 1 189 51 51 GLU CA C 55.108 0.400 1 190 51 51 GLU CB C 30.956 0.400 1 191 51 51 GLU N N 121.043 0.400 1 192 52 52 SER H H 9.062 0.040 1 193 52 52 SER CA C 56.640 0.400 1 194 52 52 SER CB C 65.183 0.400 1 195 52 52 SER N N 121.055 0.400 1 196 53 53 SER H H 9.129 0.040 1 197 53 53 SER CA C 56.950 0.400 1 198 53 53 SER CB C 68.349 0.400 1 199 53 53 SER N N 115.903 0.400 1 200 54 54 ASN H H 8.750 0.040 1 201 54 54 ASN CA C 54.498 0.400 1 202 54 54 ASN CB C 37.508 0.400 1 203 54 54 ASN N N 115.336 0.400 1 204 55 55 PHE H H 7.893 0.040 1 205 55 55 PHE CA C 58.878 0.400 1 206 55 55 PHE CB C 40.502 0.400 1 207 55 55 PHE N N 114.177 0.400 1 208 56 56 ARG H H 7.468 0.040 1 209 56 56 ARG CA C 55.531 0.400 1 210 56 56 ARG CB C 31.343 0.400 1 211 56 56 ARG N N 113.706 0.400 1 212 57 57 ASN H H 8.751 0.040 1 213 57 57 ASN CA C 52.722 0.400 1 214 57 57 ASN CB C 40.498 0.400 1 215 57 57 ASN N N 118.238 0.400 1 216 58 58 ILE H H 8.670 0.040 1 217 58 58 ILE CA C 59.847 0.400 1 218 58 58 ILE CB C 42.937 0.400 1 219 58 58 ILE N N 120.380 0.400 1 220 59 59 ASP H H 8.800 0.040 1 221 59 59 ASP CA C 53.433 0.400 1 222 59 59 ASP CB C 41.728 0.400 1 223 59 59 ASP N N 124.700 0.400 1 224 60 60 VAL H H 8.829 0.040 1 225 60 60 VAL CA C 62.300 0.400 1 226 60 60 VAL CB C 33.521 0.400 1 227 60 60 VAL N N 126.400 0.400 1 228 61 61 VAL H H 8.293 0.040 1 229 61 61 VAL CA C 60.220 0.400 1 230 61 61 VAL CB C 34.556 0.400 1 231 61 61 VAL N N 124.365 0.400 1 232 62 62 PHE H H 8.792 0.040 1 233 62 62 PHE CA C 55.413 0.400 1 234 62 62 PHE CB C 40.390 0.400 1 235 62 62 PHE N N 121.002 0.400 1 236 63 63 GLU H H 9.260 0.040 1 237 63 63 GLU CA C 53.409 0.400 1 238 63 63 GLU CB C 32.430 0.400 1 239 63 63 GLU N N 122.302 0.400 1 240 64 64 LEU H H 9.060 0.040 1 241 64 64 LEU CA C 56.334 0.400 1 242 64 64 LEU CB C 41.386 0.400 1 243 64 64 LEU N N 125.637 0.400 1 244 65 65 GLY H H 8.916 0.040 1 245 65 65 GLY CA C 45.947 0.400 1 246 65 65 GLY N N 125.464 0.400 1 247 66 66 VAL H H 8.273 0.040 1 248 66 66 VAL CA C 62.498 0.400 1 249 66 66 VAL CB C 32.740 0.400 1 250 66 66 VAL N N 119.247 0.400 1 251 67 67 ASP H H 9.085 0.040 1 252 67 67 ASP CA C 55.430 0.400 1 253 67 67 ASP CB C 41.989 0.400 1 254 67 67 ASP N N 117.436 0.400 1 255 68 68 PHE H H 9.006 0.040 1 256 68 68 PHE CA C 56.188 0.400 1 257 68 68 PHE CB C 41.435 0.400 1 258 68 68 PHE N N 121.619 0.400 1 259 69 69 ALA H H 8.313 0.040 1 260 69 69 ALA CA C 50.450 0.400 1 261 69 69 ALA CB C 21.406 0.400 1 262 69 69 ALA N N 122.159 0.400 1 263 70 70 TYR H H 8.057 0.040 1 264 70 70 TYR CA C 57.214 0.400 1 265 70 70 TYR CB C 46.427 0.400 1 266 70 70 TYR N N 122.189 0.400 1 267 71 71 SER H H 7.902 0.040 1 268 71 71 SER CA C 55.636 0.400 1 269 71 71 SER CB C 64.847 0.400 1 270 71 71 SER N N 121.468 0.400 1 271 72 72 LEU H H 8.473 0.040 1 272 72 72 LEU CA C 54.476 0.400 1 273 72 72 LEU CB C 41.875 0.400 1 274 72 72 LEU N N 122.700 0.400 1 275 73 73 ALA H H 8.656 0.040 1 276 73 73 ALA N N 123.175 0.400 1 277 74 74 ASP H H 7.681 0.040 1 278 74 74 ASP CA C 54.600 0.400 1 279 74 74 ASP N N 113.350 0.400 1 280 75 75 GLY H H 7.790 0.040 1 281 75 75 GLY CA C 44.890 0.400 1 282 75 75 GLY N N 124.459 0.400 1 283 76 76 THR H H 8.085 0.040 1 284 76 76 THR CA C 65.473 0.400 1 285 76 76 THR CB C 68.224 0.400 1 286 76 76 THR N N 115.997 0.400 1 287 77 77 GLU H H 8.671 0.040 1 288 77 77 GLU CA C 57.175 0.400 1 289 77 77 GLU CB C 30.585 0.400 1 290 77 77 GLU N N 115.693 0.400 1 291 78 78 LEU H H 8.858 0.040 1 292 78 78 LEU CA C 53.389 0.400 1 293 78 78 LEU CB C 46.654 0.400 1 294 78 78 LEU N N 118.537 0.400 1 295 79 79 THR H H 8.555 0.040 1 296 79 79 THR CA C 60.218 0.400 1 297 79 79 THR CB C 70.908 0.400 1 298 79 79 THR N N 111.462 0.400 1 299 80 80 GLY H H 8.075 0.040 1 300 80 80 GLY CA C 46.361 0.400 1 301 80 80 GLY N N 114.753 0.400 1 302 81 81 THR H H 7.693 0.040 1 303 81 81 THR CA C 59.712 0.400 1 304 81 81 THR CB C 73.274 0.400 1 305 81 81 THR N N 123.940 0.400 1 306 82 82 TRP H H 9.286 0.040 1 307 82 82 TRP CA C 55.911 0.400 1 308 82 82 TRP CB C 32.735 0.400 1 309 82 82 TRP N N 119.077 0.400 1 310 83 83 THR H H 9.161 0.040 1 311 83 83 THR CA C 60.584 0.400 1 312 83 83 THR CB C 72.056 0.400 1 313 83 83 THR N N 116.670 0.400 1 314 84 84 MET H H 8.996 0.040 1 315 84 84 MET CA C 54.188 0.400 1 316 84 84 MET CB C 33.354 0.400 1 317 84 84 MET N N 116.835 0.400 1 318 85 85 GLU H H 9.082 0.040 1 319 85 85 GLU CA C 54.877 0.400 1 320 85 85 GLU CB C 30.509 0.400 1 321 85 85 GLU N N 112.785 0.400 1 322 86 86 GLY H H 9.036 0.040 1 323 86 86 GLY CA C 47.307 0.400 1 324 86 86 GLY N N 118.713 0.400 1 325 87 87 ASN H H 8.557 0.040 1 326 87 87 ASN CA C 52.924 0.400 1 327 87 87 ASN CB C 38.546 0.400 1 328 87 87 ASN N N 121.790 0.400 1 329 88 88 LYS H H 8.227 0.040 1 330 88 88 LYS CA C 55.610 0.400 1 331 88 88 LYS CB C 35.256 0.400 1 332 88 88 LYS N N 121.144 0.400 1 333 89 89 LEU H H 8.908 0.040 1 334 89 89 LEU CA C 53.762 0.400 1 335 89 89 LEU CB C 44.428 0.400 1 336 89 89 LEU N N 124.228 0.400 1 337 90 90 VAL H H 9.772 0.040 1 338 90 90 VAL CA C 62.431 0.400 1 339 90 90 VAL CB C 33.780 0.400 1 340 90 90 VAL N N 123.949 0.400 1 341 91 91 GLY H H 9.505 0.040 1 342 91 91 GLY CA C 52.306 0.400 1 343 91 91 GLY N N 123.371 0.400 1 344 92 92 LYS H H 8.032 0.040 1 345 92 92 LYS CA C 55.307 0.400 1 346 92 92 LYS CB C 32.822 0.400 1 347 92 92 LYS N N 124.454 0.400 1 348 93 93 PHE H H 8.875 0.040 1 349 93 93 PHE CA C 55.764 0.400 1 350 93 93 PHE CB C 44.012 0.400 1 351 93 93 PHE N N 121.987 0.400 1 352 94 94 LYS H H 9.122 0.040 1 353 94 94 LYS CA C 54.779 0.400 1 354 94 94 LYS CB C 36.035 0.400 1 355 94 94 LYS N N 121.402 0.400 1 356 95 95 ARG H H 8.643 0.040 1 357 95 95 ARG CA C 56.703 0.400 1 358 95 95 ARG CB C 30.978 0.400 1 359 95 95 ARG N N 124.251 0.400 1 360 96 96 VAL H H 8.696 0.040 1 361 96 96 VAL CA C 65.521 0.400 1 362 96 96 VAL CB C 32.418 0.400 1 363 96 96 VAL N N 123.193 0.400 1 364 97 97 ASP H H 8.985 0.040 1 365 97 97 ASP CA C 56.424 0.400 1 366 97 97 ASP CB C 38.905 0.400 1 367 97 97 ASP N N 118.152 0.400 1 368 98 98 ASN H H 8.372 0.040 1 369 98 98 ASN CA C 51.346 0.400 1 370 98 98 ASN CB C 39.199 0.400 1 371 98 98 ASN N N 121.200 0.400 1 372 99 99 GLY H H 8.035 0.040 1 373 99 99 GLY CA C 46.156 0.400 1 374 99 99 GLY N N 125.524 0.400 1 375 100 100 LYS H H 8.324 0.040 1 376 100 100 LYS CA C 57.116 0.400 1 377 100 100 LYS CB C 34.339 0.400 1 378 100 100 LYS N N 119.985 0.400 1 379 101 101 GLU H H 8.665 0.040 1 380 101 101 GLU CA C 56.590 0.400 1 381 101 101 GLU CB C 32.313 0.400 1 382 101 101 GLU N N 122.220 0.400 1 383 102 102 LEU H H 8.692 0.040 1 384 102 102 LEU CA C 55.068 0.400 1 385 102 102 LEU CB C 46.309 0.400 1 386 102 102 LEU N N 125.479 0.400 1 387 103 103 ILE H H 8.802 0.040 1 388 103 103 ILE CA C 58.840 0.400 1 389 103 103 ILE CB C 39.547 0.400 1 390 103 103 ILE N N 120.022 0.400 1 391 104 104 ALA H H 9.267 0.040 1 392 104 104 ALA CA C 49.287 0.400 1 393 104 104 ALA CB C 24.446 0.400 1 394 104 104 ALA N N 116.154 0.400 1 395 105 105 VAL H H 9.254 0.040 1 396 105 105 VAL CA C 60.994 0.400 1 397 105 105 VAL CB C 36.314 0.400 1 398 105 105 VAL N N 122.789 0.400 1 399 106 106 ARG H H 9.168 0.040 1 400 106 106 ARG CA C 55.030 0.400 1 401 106 106 ARG CB C 34.000 0.400 1 402 106 106 ARG N N 123.465 0.400 1 403 107 107 GLU H H 8.703 0.040 1 404 107 107 GLU CA C 54.333 0.400 1 405 107 107 GLU CB C 34.405 0.400 1 406 107 107 GLU N N 122.332 0.400 1 407 108 108 ILE H H 8.876 0.040 1 408 108 108 ILE CA C 58.537 0.400 1 409 108 108 ILE CB C 37.340 0.400 1 410 108 108 ILE N N 123.653 0.400 1 411 109 109 SER H H 9.102 0.040 1 412 109 109 SER CA C 56.321 0.400 1 413 109 109 SER CB C 63.629 0.400 1 414 109 109 SER N N 121.773 0.400 1 415 110 110 GLY H H 9.165 0.040 1 416 110 110 GLY CA C 47.324 0.400 1 417 110 110 GLY N N 120.643 0.400 1 418 111 111 ASN H H 8.546 0.040 1 419 111 111 ASN CA C 52.922 0.400 1 420 111 111 ASN CB C 38.711 0.400 1 421 111 111 ASN N N 121.542 0.400 1 422 112 112 GLU H H 8.167 0.040 1 423 112 112 GLU CA C 55.257 0.400 1 424 112 112 GLU CB C 33.367 0.400 1 425 112 112 GLU N N 120.589 0.400 1 426 113 113 LEU H H 8.725 0.040 1 427 113 113 LEU CA C 53.882 0.400 1 428 113 113 LEU CB C 43.493 0.400 1 429 113 113 LEU N N 117.959 0.400 1 430 114 114 ILE H H 9.358 0.040 1 431 114 114 ILE CA C 61.434 0.400 1 432 114 114 ILE N N 110.192 0.400 1 433 115 115 GLN H H 9.262 0.040 1 434 115 115 GLN CA C 53.865 0.400 1 435 115 115 GLN N N 112.485 0.400 1 436 116 116 THR H H 9.302 0.040 1 437 116 116 THR CA C 61.403 0.400 1 438 116 116 THR CB C 70.359 0.400 1 439 116 116 THR N N 115.813 0.400 1 440 117 117 TYR H H 9.165 0.040 1 441 117 117 TYR CA C 54.096 0.400 1 442 117 117 TYR CB C 42.906 0.400 1 443 117 117 TYR N N 121.331 0.400 1 444 118 118 THR H H 9.128 0.040 1 445 118 118 THR CA C 62.162 0.400 1 446 118 118 THR CB C 70.607 0.400 1 447 118 118 THR N N 120.026 0.400 1 448 119 119 TYR H H 9.291 0.040 1 449 119 119 TYR CA C 57.839 0.400 1 450 119 119 TYR CB C 43.311 0.400 1 451 119 119 TYR N N 126.778 0.400 1 452 120 120 GLU H H 9.167 0.040 1 453 120 120 GLU CA C 56.313 0.400 1 454 120 120 GLU CB C 28.813 0.400 1 455 120 120 GLU N N 123.939 0.400 1 456 121 121 GLY H H 8.550 0.040 1 457 121 121 GLY CA C 45.110 0.400 1 458 121 121 GLY N N 121.434 0.400 1 459 122 122 VAL H H 8.470 0.040 1 460 122 122 VAL CA C 62.532 0.400 1 461 122 122 VAL CB C 32.884 0.400 1 462 122 122 VAL N N 118.054 0.400 1 463 123 123 GLU H H 8.885 0.040 1 464 123 123 GLU CA C 54.097 0.400 1 465 123 123 GLU CB C 33.540 0.400 1 466 123 123 GLU N N 116.797 0.400 1 467 124 124 ALA H H 9.106 0.040 1 468 124 124 ALA CA C 50.473 0.400 1 469 124 124 ALA CB C 24.259 0.400 1 470 124 124 ALA N N 122.796 0.400 1 471 125 125 LYS H H 8.998 0.040 1 472 125 125 LYS CA C 54.387 0.400 1 473 125 125 LYS CB C 37.619 0.400 1 474 125 125 LYS N N 117.635 0.400 1 475 126 126 ARG H H 9.020 0.040 1 476 126 126 ARG CA C 56.467 0.400 1 477 126 126 ARG CB C 33.709 0.400 1 478 126 126 ARG N N 121.593 0.400 1 479 127 127 ILE H H 9.283 0.040 1 480 127 127 ILE CA C 61.513 0.400 1 481 127 127 ILE CB C 39.411 0.400 1 482 127 127 ILE N N 125.103 0.400 1 483 128 128 PHE H H 9.595 0.040 1 484 128 128 PHE CA C 56.048 0.400 1 485 128 128 PHE CB C 43.168 0.400 1 486 128 128 PHE N N 123.904 0.400 1 487 129 129 LYS H H 8.868 0.040 1 488 129 129 LYS CA C 54.911 0.400 1 489 129 129 LYS CB C 36.181 0.400 1 490 129 129 LYS N N 121.956 0.400 1 491 130 130 LYS H H 8.588 0.040 1 492 130 130 LYS CA C 56.857 0.400 1 493 130 130 LYS CB C 33.408 0.400 1 494 130 130 LYS N N 121.016 0.400 1 495 131 131 GLU H H 8.394 0.040 1 496 131 131 GLU CA C 58.480 0.400 1 stop_ save_