data_27378 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments of WT HIV-1 Protease bound to Darunavir ; _BMRB_accession_number 27378 _BMRB_flat_file_name bmr27378.str _Entry_type original _Submission_date 2018-01-22 _Accession_date 2018-01-22 _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 Ishima Rieko . . 2 Persons John D. . 3 Khan Shahid N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 164 "13C chemical shifts" 167 "15N chemical shifts" 164 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-03-22 update BMRB 'update entry citation' 2018-03-07 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27377 'HIV-1 Protease Homodimer [(Flap + mutant) bound to Darunavir]' stop_ _Original_release_date 2018-01-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Probing Structural Changes among Analogous Inhibitor-Bound Forms of HIV-1 Protease and a Drug-Resistant Mutant in Solution by Nuclear Magnetic Resonance ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29457713 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Khan Shahid N. . 2 Persons John D. . 3 Paulsen Janet L. . 4 Guerrero Michel . . 5 Schiffer Celia A. . 6 Kurt-Yilmaz Nese . . 7 Ishima Rieko . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 57 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1652 _Page_last 1662 _Year 2018 _Details . loop_ _Keyword 'Drug Design' HIV-1 Inhibitor MD NMR Protease 'Structural Biology' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HIV-1 Protease Homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HIV-1_Protease, subunit 1' $HIV-1_Protease 'HIV-1_Protease, subunit 2' $HIV-1_Protease ligand $entity_K13 stop_ _System_molecular_weight 22041 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Inhibitor bound HIV-1 Protease Homodimer' save_ ######################## # Monomeric polymers # ######################## save_HIV-1_Protease _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HIV-1_Protease _Molecular_mass 10739.70 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; PQITLWKRPLVTIRIGGQLK EALLDTGADDTVIEEMNLPG KWKPKMIGGIGGFIKVRQYD QIPIEIAGHKAIGTVLVGPT PVNIIGRNLLTQIGATLNF ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 GLN 3 ILE 4 THR 5 LEU 6 TRP 7 LYS 8 ARG 9 PRO 10 LEU 11 VAL 12 THR 13 ILE 14 ARG 15 ILE 16 GLY 17 GLY 18 GLN 19 LEU 20 LYS 21 GLU 22 ALA 23 LEU 24 LEU 25 ASP 26 THR 27 GLY 28 ALA 29 ASP 30 ASP 31 THR 32 VAL 33 ILE 34 GLU 35 GLU 36 MET 37 ASN 38 LEU 39 PRO 40 GLY 41 LYS 42 TRP 43 LYS 44 PRO 45 LYS 46 MET 47 ILE 48 GLY 49 GLY 50 ILE 51 GLY 52 GLY 53 PHE 54 ILE 55 LYS 56 VAL 57 ARG 58 GLN 59 TYR 60 ASP 61 GLN 62 ILE 63 PRO 64 ILE 65 GLU 66 ILE 67 ALA 68 GLY 69 HIS 70 LYS 71 ALA 72 ILE 73 GLY 74 THR 75 VAL 76 LEU 77 VAL 78 GLY 79 PRO 80 THR 81 PRO 82 VAL 83 ASN 84 ILE 85 ILE 86 GLY 87 ARG 88 ASN 89 LEU 90 LEU 91 THR 92 GLN 93 ILE 94 GLY 95 ALA 96 THR 97 LEU 98 ASN 99 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_K13 _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common ; (3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl [(1S,2R)-3-{[(4-aminophenyl)sulfonyl][(2S)-2-methylbutyl]amino}-1-benzyl-2-hydroxypropyl]carbamate ; _BMRB_code K13 _PDB_code K13 _Molecular_mass 561.690 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? S8 S8 S . 0 . ? O9 O9 O . 0 . ? O10 O10 O . 0 . ? N11 N11 N . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? C18 C18 C . 0 . ? O18 O18 O . 0 . ? C19 C19 C . 0 . ? N20 N20 N . 0 . ? C21 C21 C . 0 . ? O22 O22 O . 0 . ? O23 O23 O . 0 . ? C24 C24 C . 0 . ? C25 C25 C . 0 . ? O26 O26 O . 0 . ? C27 C27 C . 0 . ? O28 O28 O . 0 . ? C29 C29 C . 0 . ? C30 C30 C . 0 . ? C31 C31 C . 0 . ? C32 C32 C . 0 . ? C33 C33 C . 0 . ? C34 C34 C . 0 . ? C35 C35 C . 0 . ? C36 C36 C . 0 . ? C37 C37 C . 0 . ? C38 C38 C . 0 . ? HN1 HN1 H . 0 . ? HN1A HN1A H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H6 H6 H . 0 . ? H7 H7 H . 0 . ? H12 H12 H . 0 . ? H12A H12A H . 0 . ? H13 H13 H . 0 . ? H14 H14 H . 0 . ? H14A H14A H . 0 . ? H14B H14B H . 0 . ? H15 H15 H . 0 . ? H15A H15A H . 0 . ? H16 H16 H . 0 . ? H16A H16A H . 0 . ? H17 H17 H . 0 . ? H18 H18 H . 0 . ? H18A H18A H . 0 . ? H18B H18B H . 0 . ? HO18 HO18 H . 0 . ? H19 H19 H . 0 . ? HN20 HN20 H . 0 . ? H24 H24 H . 0 . ? H25 H25 H . 0 . ? H25A H25A H . 0 . ? H27 H27 H . 0 . ? H29 H29 H . 0 . ? H29A H29A H . 0 . ? H30 H30 H . 0 . ? H30A H30A H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H32A H32A H . 0 . ? H33 H33 H . 0 . ? H34 H34 H . 0 . ? H35 H35 H . 0 . ? H36 H36 H . 0 . ? H37 H37 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C2 ? ? DOUB C2 C3 ? ? SING C2 C7 ? ? SING C3 C4 ? ? DOUB C4 C5 ? ? SING C5 C6 ? ? SING C5 S8 ? ? DOUB C6 C7 ? ? DOUB S8 O9 ? ? DOUB S8 O10 ? ? SING S8 N11 ? ? SING N11 C12 ? ? SING N11 C16 ? ? SING C12 C13 ? ? SING C13 C14 ? ? SING C13 C15 ? ? SING C15 C18 ? ? SING C16 C17 ? ? SING C17 O18 ? ? SING C17 C19 ? ? SING C19 N20 ? ? SING C19 C32 ? ? SING N20 C21 ? ? DOUB C21 O22 ? ? SING C21 O23 ? ? SING O23 C24 ? ? SING C24 C25 ? ? SING C24 C31 ? ? SING C25 O26 ? ? SING O26 C27 ? ? SING C27 O28 ? ? SING C27 C31 ? ? SING O28 C29 ? ? SING C29 C30 ? ? SING C30 C31 ? ? SING C32 C38 ? ? DOUB C33 C34 ? ? SING C33 C38 ? ? SING C34 C35 ? ? DOUB C35 C36 ? ? SING C36 C37 ? ? DOUB C37 C38 ? ? SING N1 HN1 ? ? SING N1 HN1A ? ? SING C3 H3 ? ? SING C4 H4 ? ? SING C6 H6 ? ? SING C7 H7 ? ? SING C12 H12 ? ? SING C12 H12A ? ? SING C13 H13 ? ? SING C14 H14 ? ? SING C14 H14A ? ? SING C14 H14B ? ? SING C15 H15 ? ? SING C15 H15A ? ? SING C16 H16 ? ? SING C16 H16A ? ? SING C17 H17 ? ? SING C18 H18 ? ? SING C18 H18A ? ? SING C18 H18B ? ? SING O18 HO18 ? ? SING C19 H19 ? ? SING N20 HN20 ? ? SING C24 H24 ? ? SING C25 H25 ? ? SING C25 H25A ? ? SING C27 H27 ? ? SING C29 H29 ? ? SING C29 H29A ? ? SING C30 H30 ? ? SING C30 H30A ? ? SING C31 H31 ? ? SING C32 H32 ? ? SING C32 H32A ? ? SING C33 H33 ? ? SING C34 H34 ? ? SING C35 H35 ? ? SING C36 H36 ? ? SING C37 H37 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HIV-1_Protease HIV-1 11676 Viruses . Lentivirus HIV-1 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 $HIV-1_Protease 'recombinant technology' . Escherichia coli BL21-(DE3) pJ414 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HIV-1_Protease 250 uM '[U-99% 13C; U-99% 15N]' $entity_K13 2:1 ratio 'natural abundance' 'phosphate buffer' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_TopSpin _Saveframe_category software _Name TopSpin _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 . pH pressure 1 . atm temperature 293 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_1 _Saveframe_category assigned_chemical_shifts _Details ; A designates that the subunit that contains this residue is bound to the bis-THF side of the inhibitor. B designates that the subunit that contains this residue is bound to the aniline side of the inhibitor. If blank, the assignment to bis-THF or aniline functional group part of the inhibitor is unknown. ; loop_ _Software_label $NMRPipe $NMRDraw $TopSpin $Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HIV-1_Protease, subunit 1' _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 PRO CA C 62.023 0.011 6 2 2 2 GLN H H 8.537 0.001 6 3 2 2 GLN CA C 55.549 0.011 6 4 2 2 GLN N N 120.354 0.01 6 5 3 3 ILE H H 9.408 0.001 6 6 3 3 ILE CA C 60.618 0.011 6 7 3 3 ILE N N 128.235 0.01 6 8 4 4 THR H H 8.337 0.001 6 9 4 4 THR CA C 60.778 0.011 6 10 4 4 THR N N 115.752 0.01 6 11 5 5 LEU H H 9.15 0.001 6 12 5 5 LEU CA C 54.094 0.011 6 13 5 5 LEU N N 116.833 0.01 6 14 6 6 TRP H H 7.329 0.001 6 15 6 6 TRP CA C 58.977 0.011 6 16 6 6 TRP N N 120.865 0.01 6 17 7 7 LYS H H 7.458 0.001 6 18 7 7 LYS CA C 53.494 0.011 6 19 7 7 LYS N N 115.14 0.01 6 20 8 8 ARG H H 8.834 0.001 6 21 8 8 ARG CA C 56.112 0.011 6 22 8 8 ARG N N 120.51 0.01 6 23 9 9 PRO CA C 61.706 0.011 6 24 10 10 LEU H H 7.612 0.001 6 25 10 10 LEU CA C 53.635 0.011 6 26 10 10 LEU N N 126.975 0.01 6 27 11 11 VAL H H 9.169 0.001 6 28 11 11 VAL CA C 58.663 0.011 6 29 11 11 VAL N N 120.076 0.01 6 30 12 12 THR H H 8.522 0.001 6 31 12 12 THR CA C 62.765 0.011 6 32 12 12 THR N N 116.18 0.01 6 33 13 13 ILE H H 9.305 0.001 6 34 13 13 ILE CA C 57.994 0.011 6 35 13 13 ILE N N 121.05 0.01 6 36 14 14 ARG H H 8.59 0.001 6 37 14 14 ARG CA C 54.656 0.011 6 38 14 14 ARG N N 120.572 0.01 6 39 15 15 ILE H H 8.908 0.001 6 40 15 15 ILE CA C 59.101 0.011 6 41 15 15 ILE N N 124.82 0.01 6 42 16 16 GLY H H 9.729 0.001 6 43 16 16 GLY CA C 46.909 0.011 6 44 16 16 GLY N N 118.144 0.01 6 45 17 17 GLY H H 8.765 0.001 6 46 17 17 GLY CA C 45.036 0.011 6 47 17 17 GLY N N 105.52 0.01 6 48 18 18 GLN H H 8.003 0.001 6 49 18 18 GLN CA C 54.246 0.011 6 50 18 18 GLN N N 119.947 0.01 6 51 19 19 LEU H H 8.461 0.001 6 52 19 19 LEU CA C 54.151 0.011 6 53 19 19 LEU N N 123.376 0.01 6 54 20 20 LYS H H 8.982 0.001 6 55 20 20 LYS CA C 54.117 0.011 6 56 20 20 LYS N N 123.227 0.01 6 57 21 21 GLU H H 8.654 0.001 6 58 21 21 GLU CA C 55.093 0.011 6 59 21 21 GLU N N 120.64 0.01 6 60 22 22 ALA H H 9.31 0.001 1 61 22 22 ALA CA C 50.705 0.011 1 62 22 22 ALA N N 125.548 0.01 1 63 23 23 LEU H H 8.776 0.001 1 64 23 23 LEU CA C 53.259 0.011 1 65 23 23 LEU N N 121.888 0.01 1 66 24 24 LEU H H 8.411 0.001 1 67 24 24 LEU CA C 55.542 0.011 1 68 24 24 LEU N N 125.341 0.01 1 69 25 25 ASP H H 8.698 0.001 1 70 25 25 ASP CA C 52.264 0.011 1 71 25 25 ASP N N 128.875 0.01 1 72 26 26 THR H H 8.215 0.001 1 73 26 26 THR CA C 65.528 0.011 1 74 26 26 THR N N 111.071 0.01 1 75 27 27 GLY H H 7.821 0.001 1 76 27 27 GLY CA C 45.34 0.011 1 77 27 27 GLY N N 108.859 0.01 1 78 28 28 ALA H H 7.581 0.001 1 79 28 28 ALA CA C 50.014 0.011 1 80 28 28 ALA N N 126.505 0.01 1 81 29 29 ASP H H 8.688 0.001 1 82 29 29 ASP CA C 57.693 0.011 1 83 29 29 ASP N N 125.937 0.01 1 84 30 30 ASP H H 7.602 0.001 1 85 30 30 ASP CA C 52.877 0.011 1 86 30 30 ASP N N 115.638 0.01 1 87 31 31 THR H H 8.253 0.001 1 88 31 31 THR CA C 63.088 0.011 1 89 31 31 THR N N 117.133 0.01 1 90 32 32 VAL H H 8.318 0.001 1 91 32 32 VAL CA C 59.989 0.011 1 92 32 32 VAL N N 128.12 0.01 1 93 33 33 ILE H H 9.245 0.001 1 94 33 33 ILE CA C 57.138 0.011 1 95 33 33 ILE N N 125.942 0.01 1 96 34 34 GLU H H 8.064 0.001 1 97 34 34 GLU CA C 55.223 0.011 1 98 34 34 GLU N N 120.019 0.01 1 99 35 35 GLU H H 7.54 0.001 1 100 35 35 GLU CA C 58.163 0.011 1 101 35 35 GLU N N 115.073 0.01 1 102 36 36 MET H H 6.979 0.001 1 103 36 36 MET CA C 54.708 0.011 1 104 36 36 MET N N 120.515 0.01 1 105 37 37 ASN H H 8.631 0.001 6 106 37 37 ASN CA C 52.602 0.011 6 107 37 37 ASN N N 118.687 0.01 6 108 38 38 LEU H H 7.261 0.001 6 109 38 38 LEU CA C 51.844 0.011 6 110 38 38 LEU N N 124.555 0.01 6 111 39 39 PRO CA C 62.677 0.011 6 112 40 40 GLY H H 8.381 0.001 6 113 40 40 GLY CA C 44.301 0.011 6 114 40 40 GLY N N 106.078 0.01 6 115 41 41 LYS H H 8.399 0.001 6 116 41 41 LYS CA C 56.236 0.011 6 117 41 41 LYS N N 119.167 0.01 6 118 42 42 TRP H H 7.406 0.001 6 119 42 42 TRP CA C 53.898 0.011 6 120 42 42 TRP N N 118.258 0.01 6 121 43 43 LYS H H 8.353 0.001 6 122 43 43 LYS CA C 52.884 0.011 6 123 43 43 LYS N N 117.96 0.01 6 124 44 44 PRO CA C 62.935 0.011 6 125 45 45 LYS H H 8.546 0.001 1 126 45 45 LYS CA C 55.51 0.011 1 127 45 45 LYS N N 121.692 0.01 1 128 46 46 MET H H 8.504 0.001 1 129 46 46 MET CA C 53.741 0.011 1 130 46 46 MET N N 121.599 0.01 1 131 47 47 ILE H H 8.871 0.001 1 132 47 47 ILE CA C 59.048 0.011 1 133 47 47 ILE N N 118.026 0.01 1 134 48 48 GLY H H 8.294 0.001 1 135 48 48 GLY CA C 44.088 0.011 1 136 48 48 GLY N N 111.656 0.01 1 137 49 49 GLY H H 7.501 0.001 1 138 49 49 GLY CA C 43.606 0.011 1 139 49 49 GLY N N 109.001 0.01 1 140 50 50 ILE H H 8.795 0.001 1 141 50 50 ILE CA C 64.074 0.011 1 142 50 50 ILE N N 123.232 0.01 1 143 51 51 GLY H H 7.782 0.001 1 144 51 51 GLY N N 103.351 0.01 1 145 52 52 GLY H H 6.904 0.001 1 146 52 52 GLY CA C 44.15 0.011 1 147 52 52 GLY N N 105.902 0.01 1 148 53 53 PHE H H 8.24 0.001 1 149 53 53 PHE CA C 56.435 0.011 1 150 53 53 PHE N N 118.675 0.01 1 151 54 54 ILE H H 8.998 0.001 1 152 54 54 ILE CA C 59.654 0.011 1 153 54 54 ILE N N 112.997 0.01 1 154 55 55 LYS H H 8.538 0.001 1 155 55 55 LYS CA C 56.152 0.011 1 156 55 55 LYS N N 123.875 0.01 1 157 56 56 VAL H H 8.966 0.001 1 158 56 56 VAL CA C 58.024 0.011 1 159 56 56 VAL N N 115.537 0.01 1 160 57 57 ARG H H 8.845 0.001 1 161 57 57 ARG CA C 55.559 0.011 1 162 57 57 ARG N N 118.936 0.01 1 163 58 58 GLN H H 9.666 0.001 1 164 58 58 GLN CA C 55.785 0.011 1 165 58 58 GLN N N 123.853 0.01 1 166 59 59 TYR H H 9.159 0.001 1 167 59 59 TYR CA C 57.314 0.011 1 168 59 59 TYR N N 129.164 0.01 1 169 60 60 ASP H H 8.919 0.001 1 170 60 60 ASP CA C 53.77 0.011 1 171 60 60 ASP N N 121.091 0.01 1 172 61 61 GLN H H 8.986 0.001 1 173 61 61 GLN CA C 56.289 0.011 1 174 61 61 GLN N N 114.245 0.01 1 175 62 62 ILE H H 8.767 0.001 1 176 62 62 ILE CA C 55.239 0.011 1 177 62 62 ILE N N 122.206 0.01 1 178 63 63 PRO CA C 61.853 0.011 6 179 64 64 ILE H H 8.838 0.001 6 180 64 64 ILE CA C 59.551 0.011 6 181 64 64 ILE N N 123.18 0.01 6 182 65 65 GLU H H 8.273 0.001 6 183 65 65 GLU CA C 54.216 0.011 6 184 65 65 GLU N N 125.432 0.01 6 185 66 66 ILE H H 9.147 0.001 6 186 66 66 ILE CA C 60.32 0.011 6 187 66 66 ILE N N 125.006 0.01 6 188 67 67 ALA H H 9.012 0.001 6 189 67 67 ALA CA C 53.222 0.011 6 190 67 67 ALA N N 131.092 0.01 6 191 68 68 GLY H H 8.677 0.001 6 192 68 68 GLY CA C 45.412 0.011 6 193 68 68 GLY N N 103.047 0.01 6 194 69 69 HIS H H 8.305 0.001 6 195 69 69 HIS CA C 54.524 0.011 6 196 69 69 HIS N N 119.449 0.01 6 197 70 70 LYS H H 8.986 0.001 6 198 70 70 LYS CA C 57.74 0.011 6 199 70 70 LYS N N 125.534 0.01 6 200 71 71 ALA H H 8.808 0.001 6 201 71 71 ALA CA C 50.792 0.011 6 202 71 71 ALA N N 126.334 0.01 6 203 72 72 ILE H H 8.463 0.001 6 204 72 72 ILE CA C 60.001 0.011 6 205 72 72 ILE N N 119.464 0.01 6 206 73 73 GLY H H 8.449 0.001 6 207 73 73 GLY CA C 46.018 0.011 6 208 73 73 GLY N N 112.24 0.01 6 209 74 74 THR H H 8.73 0.001 6 210 74 74 THR CA C 63.457 0.011 6 211 74 74 THR N N 118.53 0.01 6 212 75 75 VAL H H 9.241 0.001 6 213 75 75 VAL CA C 61.458 0.011 6 214 75 75 VAL N N 126.683 0.01 6 215 76 76 LEU H H 8.187 0.001 6 216 76 76 LEU CA C 52.318 0.011 6 217 76 76 LEU N N 125.135 0.01 6 218 77 77 VAL H H 9.104 0.001 6 219 77 77 VAL CA C 59.881 0.011 6 220 77 77 VAL N N 121.368 0.01 6 221 78 78 GLY H H 8.96 0.001 6 222 78 78 GLY CA C 45.825 0.011 6 223 78 78 GLY N N 113.717 0.01 6 224 79 79 PRO CA C 63.266 0.011 6 225 80 80 THR H H 8.324 0.001 6 226 80 80 THR CA C 56.44 0.011 6 227 80 80 THR N N 119.115 0.01 6 228 81 81 PRO CA C 63.963 0.011 6 229 82 82 VAL H H 7.15 0.001 1 230 82 82 VAL CA C 60.069 0.011 1 231 82 82 VAL N N 115.639 0.01 1 232 83 83 ASN H H 8.616 0.001 1 233 83 83 ASN CA C 53.753 0.011 1 234 83 83 ASN N N 121.57 0.01 1 235 84 84 ILE H H 9.418 0.001 1 236 84 84 ILE CA C 59.774 0.011 1 237 84 84 ILE N N 120.807 0.01 1 238 85 85 ILE H H 8.737 0.001 1 239 85 85 ILE CA C 57.852 0.011 1 240 85 85 ILE N N 122.101 0.01 1 241 86 86 GLY H H 8.155 0.001 1 242 86 86 GLY CA C 43.444 0.011 1 243 86 86 GLY N N 113.748 0.01 1 244 87 87 ARG H H 9.391 0.001 1 245 87 87 ARG CA C 61.305 0.011 1 246 87 87 ARG N N 116.763 0.01 1 247 88 88 ASN H H 7.959 0.001 1 248 88 88 ASN CA C 56.963 0.011 1 249 88 88 ASN N N 115.957 0.01 1 250 89 89 LEU H H 6.885 0.001 1 251 89 89 LEU CA C 55.193 0.011 1 252 89 89 LEU N N 116.401 0.01 1 253 90 90 LEU H H 8.276 0.001 6 254 90 90 LEU CA C 57.845 0.011 6 255 90 90 LEU N N 120.103 0.01 6 256 91 91 THR H H 7.85 0.001 6 257 91 91 THR CA C 63.564 0.011 6 258 91 91 THR N N 106.146 0.01 6 259 92 92 GLN H H 6.65 0.001 6 260 92 92 GLN CA C 57.74 0.011 6 261 92 92 GLN N N 120.131 0.01 6 262 93 93 ILE H H 6.932 0.001 6 263 93 93 ILE CA C 60.465 0.011 6 264 93 93 ILE N N 108.593 0.01 6 265 94 94 GLY H H 7.218 0.001 6 266 94 94 GLY CA C 45.951 0.011 6 267 94 94 GLY N N 108.169 0.01 6 268 95 95 ALA H H 7.529 0.001 6 269 95 95 ALA CA C 51.421 0.011 6 270 95 95 ALA N N 120.43 0.01 6 271 96 96 THR H H 8.991 0.001 6 272 96 96 THR CA C 59.365 0.011 6 273 96 96 THR N N 108.994 0.01 6 274 97 97 LEU H H 8.564 0.001 6 275 97 97 LEU CA C 53.349 0.011 6 276 97 97 LEU N N 121.217 0.01 6 277 98 98 ASN H H 8.911 0.001 6 278 98 98 ASN CA C 52.845 0.011 6 279 98 98 ASN N N 121.648 0.01 6 280 99 99 PHE H H 8.005 0.001 6 281 99 99 PHE CA C 58.904 0.011 6 282 99 99 PHE N N 122.07 0.01 6 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details ; A designates that the subunit that contains this residue is bound to the bis-THF side of the inhibitor. B designates that the subunit that contains this residue is bound to the aniline side of the inhibitor. If blank, the assignment to bis-THF or aniline functional group part of the inhibitor is unknown. ; loop_ _Software_label $NMRPipe $NMRDraw $TopSpin $Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HIV-1_Protease, subunit 2' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 GLN CA C 55.469 0.011 6 2 3 3 ILE H H 9.478 0.001 6 3 3 3 ILE CA C 55.481 0.011 6 4 3 3 ILE N N 128.103 0.01 6 5 4 4 THR H H 8.337 0.001 6 6 4 4 THR CA C 60.813 0.011 6 7 4 4 THR N N 115.752 0.01 6 8 5 5 LEU H H 9.125 0.001 6 9 5 5 LEU CA C 54.112 0.011 6 10 5 5 LEU N N 116.926 0.01 6 11 7 7 LYS CA C 53.558 0.011 6 12 8 8 ARG H H 8.791 0.001 6 13 8 8 ARG CA C 56.12 0.011 6 14 8 8 ARG N N 120.691 0.01 6 15 9 9 PRO CA C 61.631 0.011 6 16 10 10 LEU H H 7.642 0.001 6 17 10 10 LEU CA C 53.71 0.011 6 18 10 10 LEU N N 126.507 0.01 6 19 11 11 VAL H H 9.171 0.001 6 20 11 11 VAL N N 115.871 0.01 6 21 12 12 THR H H 8.508 0.001 6 22 12 12 THR N N 116.862 0.01 6 23 13 13 ILE H H 9.315 0.001 6 24 13 13 ILE CA C 57.966 0.011 6 25 13 13 ILE N N 120.729 0.01 6 26 14 14 ARG H H 8.55 0.001 6 27 14 14 ARG N N 119.945 0.01 6 28 15 15 ILE H H 8.944 0.001 6 29 15 15 ILE N N 124.94 0.01 6 30 18 18 GLN H H 8.026 0.001 6 31 18 18 GLN N N 119.999 0.01 6 32 21 21 GLU CA C 54.941 0.011 6 33 22 22 ALA H H 9.254 0.001 1 34 22 22 ALA CA C 50.725 0.011 1 35 22 22 ALA N N 125.738 0.01 1 36 23 23 LEU H H 8.748 0.001 1 37 23 23 LEU CA C 53.711 0.011 1 38 23 23 LEU N N 120.834 0.01 1 39 24 24 LEU H H 8.282 0.001 1 40 24 24 LEU CA C 54.757 0.011 1 41 24 24 LEU N N 122.615 0.01 1 42 25 25 ASP H H 8.67 0.001 1 43 25 25 ASP CA C 53.185 0.011 1 44 25 25 ASP N N 127.008 0.01 1 45 26 26 THR H H 8.418 0.001 1 46 26 26 THR N N 112.633 0.01 1 47 27 27 GLY H H 9.436 0.001 1 48 27 27 GLY CA C 44.992 0.011 1 49 27 27 GLY N N 109.268 0.01 1 50 28 28 ALA H H 6.893 0.001 1 51 28 28 ALA CA C 49.066 0.011 1 52 28 28 ALA N N 124.433 0.01 1 53 29 29 ASP H H 8.538 0.001 1 54 29 29 ASP CA C 58.281 0.011 1 55 29 29 ASP N N 124.466 0.01 1 56 30 30 ASP H H 7.169 0.001 1 57 30 30 ASP CA C 52.867 0.011 1 58 30 30 ASP N N 112.923 0.01 1 59 31 31 THR H H 7.756 0.001 1 60 31 31 THR CA C 63.797 0.011 1 61 31 31 THR N N 119.641 0.01 1 62 32 32 VAL H H 9.081 0.001 1 63 32 32 VAL CA C 59.286 0.011 1 64 32 32 VAL N N 127.94 0.01 1 65 33 33 ILE H H 9.235 0.001 1 66 33 33 ILE CA C 56.795 0.011 1 67 33 33 ILE N N 125.875 0.01 1 68 34 34 GLU H H 8.00 0.001 1 69 34 34 GLU CA C 55.288 0.011 1 70 34 34 GLU N N 120.042 0.01 1 71 35 35 GLU H H 7.231 0.001 1 72 35 35 GLU CA C 58.306 0.011 1 73 35 35 GLU N N 115.093 0.01 1 74 36 36 MET H H 6.964 0.001 1 75 36 36 MET CA C 54.676 0.011 6 76 36 36 MET N N 120.724 0.01 1 77 37 37 ASN H H 8.65 0.001 6 78 37 37 ASN CA C 52.53 0.011 6 79 37 37 ASN N N 118.779 0.01 6 80 38 38 LEU H H 7.396 0.001 6 81 38 38 LEU CA C 51.755 0.011 6 82 38 38 LEU N N 124.814 0.01 6 83 41 41 LYS H H 8.403 0.001 6 84 41 41 LYS CA C 56.202 0.011 6 85 41 41 LYS N N 119.067 0.01 6 86 42 42 TRP H H 7.384 0.001 6 87 42 42 TRP CA C 53.702 0.011 6 88 42 42 TRP N N 117.772 0.01 6 89 43 43 LYS H H 8.222 0.001 6 90 43 43 LYS CA C 52.828 0.011 6 91 43 43 LYS N N 117.808 0.01 6 92 46 46 MET H H 8.437 0.001 1 93 46 46 MET CA C 54.226 0.011 1 94 46 46 MET N N 122.399 0.01 1 95 47 47 ILE H H 8.641 0.001 1 96 47 47 ILE N N 116.257 0.01 1 97 48 48 GLY H H 8.481 0.001 1 98 48 48 GLY CA C 44.594 0.011 1 99 48 48 GLY N N 108.493 0.01 1 100 49 49 GLY H H 7.47 0.001 1 101 49 49 GLY N N 107.031 0.01 1 102 50 50 ILE H H 8.431 0.001 1 103 50 50 ILE N N 126.159 0.01 1 104 52 52 GLY H H 7.234 0.001 1 105 52 52 GLY CA C 44.304 0.011 1 106 52 52 GLY N N 104.823 0.01 1 107 53 53 PHE H H 8.458 0.001 1 108 53 53 PHE CA C 56.223 0.011 1 109 53 53 PHE N N 119.375 0.01 1 110 54 54 ILE H H 8.649 0.001 1 111 54 54 ILE CA C 59.628 0.011 1 112 54 54 ILE N N 111.919 0.01 1 113 55 55 LYS CA C 56.185 0.011 1 114 56 56 VAL H H 8.83 0.001 1 115 56 56 VAL CA C 57.99 0.011 1 116 56 56 VAL N N 115.231 0.01 1 117 57 57 ARG H H 9.053 0.001 1 118 57 57 ARG CA C 55.294 0.011 1 119 57 57 ARG N N 119.325 0.01 1 120 58 58 GLN H H 9.742 0.001 1 121 58 58 GLN CA C 56.026 0.011 1 122 58 58 GLN N N 123.518 0.01 1 123 59 59 TYR H H 9.161 0.001 1 124 59 59 TYR CA C 57.465 0.011 1 125 59 59 TYR N N 129.116 0.01 1 126 60 60 ASP H H 8.988 0.001 1 127 60 60 ASP CA C 53.697 0.011 1 128 60 60 ASP N N 120.616 0.01 1 129 61 61 GLN H H 8.917 0.001 1 130 61 61 GLN CA C 56.271 0.011 1 131 61 61 GLN N N 114.059 0.01 1 132 62 62 ILE H H 8.739 0.001 1 133 62 62 ILE CA C 55.062 0.011 1 134 62 62 ILE N N 122.395 0.01 1 135 63 63 PRO CA C 61.915 0.011 6 136 64 64 ILE H H 8.89 0.001 6 137 64 64 ILE CA C 59.176 0.011 6 138 64 64 ILE N N 123.877 0.01 6 139 65 65 GLU CA C 54.197 0.011 6 140 66 66 ILE H H 9.175 0.001 6 141 66 66 ILE N N 125.009 0.01 6 142 68 68 GLY H H 8.696 0.001 6 143 68 68 GLY N N 103.085 0.01 6 144 72 72 ILE H H 8.462 0.001 6 145 72 72 ILE N N 119.472 0.01 6 146 73 73 GLY H H 8.506 0.001 6 147 73 73 GLY CA C 46.008 0.011 6 148 73 73 GLY N N 112.472 0.01 6 149 74 74 THR H H 8.63 0.001 6 150 74 74 THR CA C 63.562 0.011 6 151 74 74 THR N N 118.796 0.01 6 152 75 75 VAL H H 9.041 0.001 6 153 75 75 VAL CA C 61.674 0.011 6 154 75 75 VAL N N 125.024 0.01 6 155 76 76 LEU H H 8.246 0.001 6 156 76 76 LEU CA C 52.42 0.011 6 157 76 76 LEU N N 125.312 0.01 6 158 77 77 VAL H H 9.121 0.001 6 159 77 77 VAL CA C 59.83 0.011 6 160 77 77 VAL N N 121.92 0.01 6 161 78 78 GLY H H 9.048 0.001 6 162 78 78 GLY CA C 45.856 0.011 6 163 78 78 GLY N N 114.968 0.01 6 164 79 79 PRO CA C 63.336 0.011 6 165 80 80 THR H H 8.33 0.001 6 166 80 80 THR CA C 56.549 0.011 6 167 80 80 THR N N 119.935 0.01 6 168 81 81 PRO CA C 63.995 0.011 6 169 82 82 VAL H H 6.942 0.001 1 170 82 82 VAL CA C 59.458 0.011 1 171 82 82 VAL N N 113.865 0.01 1 172 83 83 ASN H H 8.502 0.001 1 173 83 83 ASN CA C 54.046 0.011 1 174 83 83 ASN N N 122.367 0.01 1 175 84 84 ILE H H 9.728 0.001 1 176 84 84 ILE CA C 61.278 0.011 1 177 84 84 ILE N N 126.48 0.01 1 178 85 85 ILE H H 9.252 0.001 1 179 85 85 ILE CA C 58.213 0.011 1 180 85 85 ILE N N 126.024 0.01 1 181 86 86 GLY H H 8.047 0.001 1 182 86 86 GLY CA C 43.537 0.011 1 183 86 86 GLY N N 112.461 0.01 1 184 87 87 ARG H H 9.218 0.001 1 185 87 87 ARG CA C 61.364 0.011 1 186 87 87 ARG N N 116.957 0.01 1 187 88 88 ASN H H 7.884 0.001 1 188 88 88 ASN CA C 56.79 0.011 1 189 88 88 ASN N N 115.129 0.01 1 190 89 89 LEU H H 6.948 0.001 1 191 89 89 LEU CA C 55.122 0.011 1 192 89 89 LEU N N 115.853 0.01 1 193 92 92 GLN H H 6.701 0.001 6 194 92 92 GLN N N 120.414 0.01 6 195 93 93 ILE H H 6.952 0.001 6 196 93 93 ILE CA C 60.508 0.011 6 197 93 93 ILE N N 108.671 0.01 6 198 94 94 GLY CA C 45.973 0.011 6 199 95 95 ALA H H 7.48 0.001 6 200 95 95 ALA CA C 51.497 0.011 6 201 95 95 ALA N N 120.272 0.01 6 202 96 96 THR H H 8.982 0.001 6 203 96 96 THR CA C 59.408 0.011 6 204 96 96 THR N N 108.976 0.01 6 205 97 97 LEU H H 8.494 0.001 6 206 97 97 LEU CA C 53.223 0.011 6 207 97 97 LEU N N 121.72 0.01 6 208 98 98 ASN H H 8.902 0.001 6 209 98 98 ASN CA C 52.778 0.011 6 210 98 98 ASN N N 121.51 0.01 6 211 99 99 PHE H H 7.966 0.001 6 212 99 99 PHE CA C 58.974 0.011 6 213 99 99 PHE N N 121.618 0.01 6 stop_ save_