data_7355 ####################### # 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. ; 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_ _BMRB_accession_number 7355 _BMRB_flat_file_name bmr7355.str _Entry_type new _Submission_date 2006-12-17 _Accession_date 2006-12-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 121 "13C chemical shifts" 226 "15N chemical shifts" 120 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB "complete entry citation" 2007-03-05 update BMRB "Chem_comp saveframe added" 2007-02-09 original author "Original release" stop_ loop_ _Related_BMRB_accession_number _Relationship 15082 apo 7356 "fenofibric Acid bound" 7357 "tolfenamic bound" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _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 _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 and Biology" _Journal_volume 14 _Journal_issue 4 _Journal_CSD ? _Page_first 453 _Page_last 465 _Year 2007 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" _Abbreviation_common "Rat intestinal fatty acid binding protein" loop_ _Mol_system_component_name _Mol_label "single polypeptide chain" $Rat_intestinal_fatty_acid_binding_protein Clofibric_acid $Clofibric_acid stop_ _System_physical_state native _System_oligomer_state monomer loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_relation_type _Database_entry_details PDB 1ICM ? "Structure used for drug docking and chemical shift mapping" ? PDB 2IFB ? "Structure used for palmitic acid chemical shift mapping" ? stop_ 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_ ############################## # 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 7356 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_ #################### # 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" ? ? ? BL21(DE3) pTrc99A stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Clofibric_acid-Rat_FABP2 _Saveframe_category sample _Sample_type solution 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]" "Clofibric acid" 5 mM ? H2O 90 % ? D2O 10 % ? stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY loop_ _Vendor _Address _Electronic_address Goddard ? ? stop_ loop_ _Task "chemical shift assignment" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_nmr_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name "3D CBCA(CO)NH" _Sample_label $Clofibric_acid-Rat_FABP2 save_ ####################### # Sample conditions # ####################### save_sample_cond _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 295.15 ? K pH 5.5 ? pH "ionic strength" 0.05 ? M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 "methyl protons" ppm 0.00 internal direct ? ? ? 1.000000000 DSS C 13 "methyl protons" ppm 0.00 n/a indirect ? ? ? 0.251449530 DSS N 15 "methyl protons" ppm 0.00 n/a 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 loop_ _Software_label $SPARKY stop_ loop_ _Sample_label $Clofibric_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" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 ALA H H 9.279 0.040 1 2 1 ALA CA C 52.305 0.400 1 3 1 ALA CB C 19.083 0.400 1 4 1 ALA N N 116.536 0.400 1 5 2 PHE H H 7.959 0.040 1 6 2 PHE CA C 59.464 0.400 1 7 2 PHE CB C 39.683 0.400 1 8 2 PHE N N 116.052 0.400 1 9 3 ASP H H 8.572 0.040 1 10 3 ASP CA C 54.947 0.400 1 11 3 ASP CB C 41.589 0.400 1 12 3 ASP N N 126.598 0.400 1 13 4 GLY H H 8.302 0.040 1 14 4 GLY CA C 43.908 0.400 1 15 4 GLY N N 116.821 0.400 1 16 5 THR H H 9.509 0.040 1 17 5 THR CA C 62.348 0.400 1 18 5 THR CB C 69.920 0.400 1 19 5 THR N N 109.991 0.400 1 20 6 TRP H H 9.617 0.040 1 21 6 TRP CA C 54.929 0.400 1 22 6 TRP CB C 31.734 0.400 1 23 6 TRP N N 123.905 0.400 1 24 7 LYS H H 8.715 0.040 1 25 7 LYS CA C 54.696 0.400 1 26 7 LYS CB C 35.480 0.400 1 27 7 LYS N N 110.653 0.400 1 28 8 VAL H H 9.723 0.040 1 29 8 VAL CA C 64.872 0.400 1 30 8 VAL CB C 31.529 0.400 1 31 8 VAL N N 109.618 0.400 1 32 9 ASP H H 7.796 0.040 1 33 9 ASP CA C 55.398 0.400 1 34 9 ASP CB C 46.479 0.400 1 35 9 ASP N N 112.999 0.400 1 36 10 ARG H H 8.670 0.040 1 37 10 ARG CA C 54.967 0.400 1 38 10 ARG CB C 31.963 0.400 1 39 10 ARG N N 116.979 0.400 1 40 11 ASN H H 9.511 0.040 1 41 11 ASN CA C 51.453 0.400 1 42 11 ASN CB C 43.264 0.400 1 43 11 ASN N N 120.465 0.400 1 44 12 GLU H H 9.386 0.040 1 45 12 GLU CA C 55.703 0.400 1 46 12 GLU CB C 32.400 0.400 1 47 12 GLU N N 122.773 0.400 1 48 13 ASN H H 8.226 0.040 1 49 13 ASN CA C 54.000 0.400 1 50 13 ASN CB C 39.514 0.400 1 51 13 ASN N N 119.027 0.400 1 52 14 TYR H H 8.957 0.040 1 53 14 TYR CA C 60.429 0.400 1 54 14 TYR CB C 40.321 0.400 1 55 14 TYR N N 119.303 0.400 1 56 15 GLU H H 8.106 0.040 1 57 15 GLU CA C 61.150 0.400 1 58 15 GLU CB C 28.151 0.400 1 59 15 GLU N N 119.307 0.400 1 60 16 LYS H H 7.657 0.040 1 61 16 LYS CA C 58.628 0.400 1 62 16 LYS CB C 31.481 0.400 1 63 16 LYS N N 121.133 0.400 1 64 17 PHE H H 8.297 0.040 1 65 17 PHE CA C 61.928 0.400 1 66 17 PHE CB C 40.584 0.400 1 67 17 PHE N N 117.757 0.400 1 68 18 MET H H 8.218 0.040 1 69 18 MET CA C 59.527 0.400 1 70 18 MET CB C 33.672 0.400 1 71 18 MET N N 119.213 0.400 1 72 19 GLU H H 8.051 0.040 1 73 19 GLU CA C 59.661 0.400 1 74 19 GLU CB C 29.460 0.400 1 75 19 GLU N N 123.448 0.400 1 76 20 LYS H H 7.594 0.040 1 77 20 LYS CA C 57.288 0.400 1 78 20 LYS CB C 31.777 0.400 1 79 20 LYS N N 114.880 0.400 1 80 21 MET H H 7.793 0.040 1 81 21 MET CA C 55.896 0.400 1 82 21 MET CB C 32.669 0.400 1 83 21 MET N N 126.430 0.400 1 84 22 GLY H H 7.420 0.040 1 85 22 GLY CA C 45.502 0.400 1 86 22 GLY N N 121.420 0.400 1 87 23 ILE H H 8.754 0.040 1 88 23 ILE CA C 60.444 0.400 1 89 23 ILE CB C 37.418 0.400 1 90 23 ILE N N 127.152 0.400 1 91 24 ASN H H 8.401 0.040 1 92 24 ASN CA C 53.997 0.400 1 93 24 ASN CB C 39.297 0.400 1 94 24 ASN N N 120.944 0.400 1 95 25 VAL H H 7.709 0.040 1 96 25 VAL CA C 65.937 0.400 1 97 25 VAL CB C 32.210 0.400 1 98 25 VAL N N 121.123 0.400 1 99 26 VAL H H 7.851 0.040 1 100 26 VAL CA C 65.810 0.400 1 101 26 VAL CB C 31.871 0.400 1 102 26 VAL N N 118.933 0.400 1 103 27 LYS H H 8.417 0.040 1 104 27 LYS CA C 58.396 0.400 1 105 27 LYS CB C 32.828 0.400 1 106 27 LYS N N 119.676 0.400 1 107 28 ARG H H 7.725 0.040 1 108 28 ARG CA C 58.847 0.400 1 109 28 ARG CB C 33.904 0.400 1 110 28 ARG N N 119.490 0.400 1 111 29 LYS H H 7.725 0.040 1 112 29 LYS CA C 58.917 0.400 1 113 29 LYS CB C 30.460 0.400 1 114 29 LYS N N 119.490 0.400 1 115 31 GLY H H 7.806 0.040 1 116 31 GLY CA C 46.910 0.400 1 117 31 GLY N N 119.926 0.400 1 118 32 ALA H H 7.811 0.040 1 119 32 ALA CA C 53.469 0.400 1 120 32 ALA CB C 18.834 0.400 1 121 32 ALA N N 119.939 0.400 1 122 35 ASN H H 7.092 0.040 1 123 35 ASN CA C 53.556 0.400 1 124 35 ASN CB C 37.579 0.400 1 125 35 ASN N N 119.625 0.400 1 126 36 LEU H H 9.434 0.040 1 127 36 LEU CA C 57.175 0.400 1 128 36 LEU CB C 42.411 0.400 1 129 36 LEU N N 109.860 0.400 1 130 37 LYS H H 9.419 0.040 1 131 37 LYS CA C 54.884 0.400 1 132 37 LYS CB C 36.245 0.400 1 133 37 LYS N N 123.658 0.400 1 134 38 LEU H H 9.168 0.040 1 135 38 LEU CA C 52.799 0.400 1 136 38 LEU CB C 46.337 0.400 1 137 38 LEU N N 120.625 0.400 1 138 39 THR H H 9.478 0.040 1 139 39 THR CA C 62.461 0.400 1 140 39 THR CB C 70.312 0.400 1 141 39 THR N N 111.095 0.400 1 142 40 ILE H H 8.718 0.040 1 143 40 ILE CA C 61.051 0.400 1 144 40 ILE CB C 40.403 0.400 1 145 40 ILE N N 122.344 0.400 1 146 41 THR H H 8.957 0.040 1 147 41 THR CA C 61.367 0.400 1 148 41 THR CB C 71.677 0.400 1 149 41 THR N N 110.231 0.400 1 150 42 GLN H H 8.924 0.040 1 151 42 GLN CA C 54.396 0.400 1 152 42 GLN CB C 29.516 0.400 1 153 42 GLN N N 111.331 0.400 1 154 43 GLU H H 9.032 0.040 1 155 43 GLU CA C 54.576 0.400 1 156 43 GLU CB C 30.913 0.400 1 157 43 GLU N N 117.745 0.400 1 158 44 GLY H H 8.861 0.040 1 159 44 GLY CA C 47.308 0.400 1 160 44 GLY N N 125.487 0.400 1 161 45 ASN H H 7.904 0.040 1 162 45 ASN CA C 52.983 0.400 1 163 45 ASN CB C 38.894 0.400 1 164 45 ASN N N 120.602 0.400 1 165 46 LYS H H 9.108 0.040 1 166 46 LYS CA C 55.478 0.400 1 167 46 LYS CB C 34.480 0.400 1 168 46 LYS N N 126.192 0.400 1 169 47 PHE H H 8.378 0.040 1 170 47 PHE CA C 56.053 0.400 1 171 47 PHE CB C 42.980 0.400 1 172 47 PHE N N 115.094 0.400 1 173 48 THR H H 9.502 0.040 1 174 48 THR CA C 62.044 0.400 1 175 48 THR CB C 69.902 0.400 1 176 48 THR N N 109.734 0.400 1 177 49 VAL H H 9.175 0.040 1 178 49 VAL CA C 61.349 0.400 1 179 49 VAL CB C 34.560 0.400 1 180 49 VAL N N 109.427 0.400 1 181 50 LYS H H 9.347 0.040 1 182 50 LYS CA C 55.425 0.400 1 183 50 LYS CB C 32.713 0.400 1 184 50 LYS N N 110.745 0.400 1 185 51 GLU H H 9.060 0.040 1 186 51 GLU CA C 54.913 0.400 1 187 51 GLU CB C 31.339 0.400 1 188 51 GLU N N 121.050 0.400 1 189 52 SER H H 8.998 0.040 1 190 52 SER CA C 56.587 0.400 1 191 52 SER CB C 65.318 0.400 1 192 52 SER N N 120.957 0.400 1 193 53 SER H H 9.046 0.040 1 194 53 SER CA C 56.941 0.400 1 195 53 SER CB C 67.481 0.400 1 196 53 SER N N 116.050 0.400 1 197 54 ASN H H 8.223 0.040 1 198 54 ASN CA C 54.695 0.400 1 199 54 ASN CB C 37.834 0.400 1 200 54 ASN N N 114.756 0.400 1 201 55 PHE H H 7.464 0.040 1 202 55 PHE CA C 58.903 0.400 1 203 55 PHE CB C 40.686 0.400 1 204 55 PHE N N 114.157 0.400 1 205 56 ARG H H 7.456 0.040 1 206 56 ARG CA C 55.757 0.400 1 207 56 ARG N N 114.157 0.400 1 208 57 ASN H H 8.869 0.040 1 209 57 ASN CA C 52.874 0.400 1 210 57 ASN CB C 40.792 0.400 1 211 57 ASN N N 119.161 0.400 1 212 58 ILE H H 8.460 0.040 1 213 58 ILE CA C 60.086 0.400 1 214 58 ILE CB C 42.837 0.400 1 215 58 ILE N N 123.675 0.400 1 216 59 ASP H H 9.380 0.040 1 217 59 ASP CA C 52.893 0.400 1 218 59 ASP CB C 41.976 0.400 1 219 59 ASP N N 125.271 0.400 1 220 60 VAL H H 8.206 0.040 1 221 60 VAL CA C 61.922 0.400 1 222 60 VAL CB C 35.090 0.400 1 223 60 VAL N N 125.852 0.400 1 224 61 VAL H H 8.582 0.040 1 225 61 VAL CA C 59.896 0.400 1 226 61 VAL CB C 34.277 0.400 1 227 61 VAL N N 121.851 0.400 1 228 62 PHE H H 9.605 0.040 1 229 62 PHE CA C 55.543 0.400 1 230 62 PHE CB C 41.290 0.400 1 231 62 PHE N N 120.112 0.400 1 232 63 GLU H H 8.929 0.040 1 233 63 GLU CA C 53.429 0.400 1 234 63 GLU CB C 31.979 0.400 1 235 63 GLU N N 125.116 0.400 1 236 64 LEU H H 9.244 0.040 1 237 64 LEU CA C 56.490 0.400 1 238 64 LEU CB C 41.306 0.400 1 239 64 LEU N N 126.553 0.400 1 240 65 GLY H H 7.970 0.040 1 241 65 GLY CA C 46.188 0.400 1 242 65 GLY N N 122.366 0.400 1 243 66 VAL H H 8.876 0.040 1 244 66 VAL CA C 62.330 0.400 1 245 66 VAL CB C 32.952 0.400 1 246 66 VAL N N 114.201 0.400 1 247 67 ASP H H 9.487 0.040 1 248 67 ASP CA C 55.333 0.400 1 249 67 ASP CB C 41.269 0.400 1 250 67 ASP N N 121.449 0.400 1 251 68 PHE H H 8.258 0.040 1 252 68 PHE CA C 56.175 0.400 1 253 68 PHE CB C 41.765 0.400 1 254 68 PHE N N 121.468 0.400 1 255 69 ALA H H 8.260 0.040 1 256 69 ALA CA C 50.442 0.400 1 257 69 ALA CB C 21.843 0.400 1 258 69 ALA N N 121.485 0.400 1 259 71 SER H H 8.404 0.040 1 260 71 SER CA C 55.835 0.400 1 261 71 SER CB C 64.696 0.400 1 262 71 SER N N 123.008 0.400 1 263 72 LEU H H 8.409 0.040 1 264 72 LEU CA C 54.615 0.400 1 265 72 LEU N N 123.035 0.400 1 266 74 ASP H H 7.873 0.040 1 267 74 ASP CA C 53.872 0.400 1 268 74 ASP CB C 40.477 0.400 1 269 74 ASP N N 126.117 0.400 1 270 75 GLY H H 7.812 0.040 1 271 75 GLY CA C 44.349 0.400 1 272 75 GLY N N 119.474 0.400 1 273 76 THR H H 8.450 0.040 1 274 76 THR CA C 65.120 0.400 1 275 76 THR CB C 67.988 0.400 1 276 76 THR N N 110.831 0.400 1 277 77 GLU H H 9.140 0.040 1 278 77 GLU CA C 56.589 0.400 1 279 77 GLU CB C 30.335 0.400 1 280 77 GLU N N 124.504 0.400 1 281 78 LEU H H 8.562 0.040 1 282 78 LEU CA C 53.457 0.400 1 283 78 LEU CB C 46.474 0.400 1 284 78 LEU N N 110.961 0.400 1 285 79 THR H H 8.531 0.040 1 286 79 THR CA C 59.830 0.400 1 287 79 THR CB C 71.102 0.400 1 288 79 THR N N 111.806 0.400 1 289 80 GLY H H 6.533 0.040 1 290 80 GLY CA C 46.527 0.400 1 291 80 GLY N N 124.706 0.400 1 292 81 THR H H 9.151 0.040 1 293 81 THR CA C 59.545 0.400 1 294 81 THR CB C 72.823 0.400 1 295 81 THR N N 122.655 0.400 1 296 82 TRP H H 9.162 0.040 1 297 82 TRP CA C 56.047 0.400 1 298 82 TRP CB C 33.416 0.400 1 299 82 TRP N N 113.500 0.400 1 300 83 THR H H 8.956 0.040 1 301 83 THR CA C 60.665 0.400 1 302 83 THR CB C 72.170 0.400 1 303 83 THR N N 122.076 0.400 1 304 84 MET H H 9.085 0.040 1 305 84 MET CA C 54.399 0.400 1 306 84 MET CB C 33.456 0.400 1 307 84 MET N N 110.001 0.400 1 308 85 GLU H H 9.082 0.040 1 309 85 GLU CA C 54.867 0.400 1 310 85 GLU CB C 30.441 0.400 1 311 85 GLU N N 117.052 0.400 1 312 86 GLY H H 8.878 0.040 1 313 86 GLY CA C 47.631 0.400 1 314 86 GLY N N 123.151 0.400 1 315 87 ASN H H 8.029 0.040 1 316 87 ASN CA C 53.007 0.400 1 317 87 ASN CB C 38.563 0.400 1 318 87 ASN N N 119.324 0.400 1 319 88 LYS H H 8.396 0.040 1 320 88 LYS CA C 55.511 0.400 1 321 88 LYS CB C 35.267 0.400 1 322 88 LYS N N 123.648 0.400 1 323 89 LEU H H 9.483 0.040 1 324 89 LEU CA C 53.912 0.400 1 325 89 LEU CB C 44.357 0.400 1 326 89 LEU N N 124.225 0.400 1 327 90 VAL H H 9.477 0.040 1 328 90 VAL CA C 62.444 0.400 1 329 90 VAL N N 124.225 0.400 1 330 91 GLY H H 7.485 0.040 1 331 91 GLY CA C 45.016 0.400 1 332 91 GLY N N 124.947 0.400 1 333 92 LYS H H 8.628 0.040 1 334 92 LYS CA C 55.159 0.400 1 335 92 LYS CB C 33.017 0.400 1 336 92 LYS N N 123.648 0.400 1 337 93 PHE H H 9.325 0.040 1 338 93 PHE CA C 55.988 0.400 1 339 93 PHE CB C 43.527 0.400 1 340 93 PHE N N 120.855 0.400 1 341 94 LYS H H 8.803 0.040 1 342 94 LYS CA C 54.770 0.400 1 343 94 LYS CB C 35.863 0.400 1 344 94 LYS N N 123.249 0.400 1 345 95 ARG H H 8.388 0.040 1 346 95 ARG CA C 56.561 0.400 1 347 95 ARG CB C 30.845 0.400 1 348 95 ARG N N 125.924 0.400 1 349 96 VAL H H 9.164 0.040 1 350 96 VAL CA C 65.306 0.400 1 351 96 VAL CB C 32.505 0.400 1 352 96 VAL N N 118.575 0.400 1 353 97 ASP H H 8.575 0.040 1 354 97 ASP CA C 56.417 0.400 1 355 97 ASP CB C 38.764 0.400 1 356 97 ASP N N 117.117 0.400 1 357 98 ASN H H 8.000 0.040 1 358 98 ASN CA C 51.414 0.400 1 359 98 ASN CB C 39.175 0.400 1 360 98 ASN N N 109.427 0.400 1 361 99 GLY H H 8.214 0.040 1 362 99 GLY CA C 46.398 0.400 1 363 99 GLY N N 120.286 0.400 1 364 100 LYS H H 8.492 0.040 1 365 100 LYS CA C 56.833 0.400 1 366 100 LYS CB C 34.082 0.400 1 367 100 LYS N N 119.837 0.400 1 368 101 GLU H H 9.117 0.040 1 369 101 GLU CA C 56.400 0.400 1 370 101 GLU CB C 31.990 0.400 1 371 101 GLU N N 126.867 0.400 1 372 102 LEU H H 8.416 0.040 1 373 102 LEU CA C 55.094 0.400 1 374 102 LEU CB C 46.357 0.400 1 375 102 LEU N N 124.648 0.400 1 376 103 ILE H H 9.214 0.040 1 377 103 ILE CA C 58.898 0.400 1 378 103 ILE CB C 39.343 0.400 1 379 103 ILE N N 113.299 0.400 1 380 105 VAL H H 9.042 0.040 1 381 105 VAL CA C 54.431 0.400 1 382 105 VAL CB C 41.966 0.400 1 383 105 VAL N N 123.368 0.400 1 384 106 ARG H H 8.548 0.040 1 385 106 ARG CA C 54.781 0.400 1 386 106 ARG CB C 33.836 0.400 1 387 106 ARG N N 120.229 0.400 1 388 107 GLU H H 8.803 0.040 1 389 107 GLU CA C 54.494 0.400 1 390 107 GLU CB C 34.469 0.400 1 391 107 GLU N N 123.551 0.400 1 392 108 ILE H H 8.963 0.040 1 393 108 ILE CA C 58.502 0.400 1 394 108 ILE CB C 37.509 0.400 1 395 108 ILE N N 123.020 0.400 1 396 109 SER H H 9.287 0.040 1 397 109 SER CA C 56.378 0.400 1 398 109 SER CB C 63.807 0.400 1 399 109 SER N N 119.761 0.400 1 400 110 GLY H H 8.817 0.040 1 401 110 GLY CA C 47.421 0.400 1 402 110 GLY N N 123.750 0.400 1 403 111 ASN H H 8.121 0.040 1 404 111 ASN CA C 53.040 0.400 1 405 111 ASN CB C 38.735 0.400 1 406 111 ASN N N 118.352 0.400 1 407 112 GLU H H 8.245 0.040 1 408 112 GLU CA C 55.279 0.400 1 409 112 GLU CB C 32.976 0.400 1 410 112 GLU N N 124.021 0.400 1 411 113 LEU H H 9.325 0.040 1 412 113 LEU CA C 53.943 0.400 1 413 113 LEU CB C 43.405 0.400 1 414 113 LEU N N 109.427 0.400 1 415 114 ILE H H 9.025 0.040 1 416 114 ILE CB C 38.982 0.400 1 417 114 ILE N N 114.228 0.400 1 418 118 THR H H 9.151 0.040 1 419 118 THR CA C 62.164 0.400 1 420 118 THR CB C 70.894 0.400 1 421 118 THR N N 127.286 0.400 1 422 119 TYR H H 9.530 0.040 1 423 119 TYR CA C 57.881 0.400 1 424 119 TYR CB C 43.357 0.400 1 425 119 TYR N N 125.913 0.400 1 426 120 GLU H H 8.599 0.040 1 427 120 GLU CA C 56.336 0.400 1 428 120 GLU CB C 28.541 0.400 1 429 120 GLU N N 120.605 0.400 1 430 121 GLY H H 8.362 0.040 1 431 121 GLY CA C 45.326 0.400 1 432 121 GLY N N 123.665 0.400 1 433 122 VAL H H 8.650 0.040 1 434 122 VAL CA C 62.432 0.400 1 435 122 VAL CB C 32.849 0.400 1 436 122 VAL N N 109.677 0.400 1 437 123 GLU H H 9.277 0.040 1 438 123 GLU CA C 53.906 0.400 1 439 123 GLU CB C 33.057 0.400 1 440 123 GLU N N 109.512 0.400 1 441 124 ALA H H 8.896 0.040 1 442 124 ALA CA C 50.617 0.400 1 443 124 ALA CB C 23.872 0.400 1 444 124 ALA N N 115.914 0.400 1 445 125 LYS H H 9.059 0.040 1 446 125 LYS CA C 54.967 0.400 1 447 125 LYS CB C 31.248 0.400 1 448 125 LYS N N 121.330 0.400 1 449 126 ARG H H 8.799 0.040 1 450 126 ARG CA C 56.686 0.400 1 451 126 ARG CB C 33.902 0.400 1 452 126 ARG N N 124.154 0.400 1 453 127 ILE H H 9.985 0.040 1 454 127 ILE CA C 61.294 0.400 1 455 127 ILE CB C 39.876 0.400 1 456 127 ILE N N 126.873 0.400 1 457 128 PHE H H 9.024 0.040 1 458 128 PHE CA C 56.117 0.400 1 459 128 PHE CB C 43.058 0.400 1 460 128 PHE N N 119.405 0.400 1 461 129 LYS H H 8.745 0.040 1 462 129 LYS CA C 54.875 0.400 1 463 129 LYS CB C 36.097 0.400 1 464 129 LYS N N 125.816 0.400 1 465 130 LYS H H 8.422 0.040 1 466 130 LYS CA C 56.926 0.400 1 467 130 LYS CB C 33.337 0.400 1 stop_ save_