data_27377 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments of HIV-1 Protease (Flap + mutant) bound to Darunavir ; _BMRB_accession_number 27377 _BMRB_flat_file_name bmr27377.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" 163 "13C chemical shifts" 178 "15N chemical shifts" 163 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 27378 'HIV-1 Protease Homodimer (WT 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 MD NMR Protease 'Structural Biology' inhibitor 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 10739.7 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; PQITLWKRPIVTIRIGGQLK EALLDTGADDTVIEEMNLPG KWKPKMIVGIGGFVKVRQYD QIPIEIAGHKAIGTVLVGPT PANIIGRNLLTQIGATLNF ; 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 ILE 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 VAL 49 GLY 50 ILE 51 GLY 52 GLY 53 PHE 54 VAL 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 ALA 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]' Darunavir 20 mM 'natural abundance' 'phosphate buffer' 2:1 ratio 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ 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_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 $TOPSPIN $NMRPipe $NMRDraw $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 62.03 0.014 6 2 2 2 GLN H H 8.533 0.002 6 3 2 2 GLN CA C 55.578 0.014 6 4 2 2 GLN N N 120.394 0.017 6 5 3 3 ILE H H 9.414 0.002 6 6 3 3 ILE CA C 60.527 0.014 6 7 3 3 ILE N N 127.791 0.017 6 8 4 4 THR H H 8.335 0.002 6 9 4 4 THR CA C 60.838 0.014 6 10 4 4 THR N N 115.458 0.017 6 11 5 5 LEU H H 9.141 0.002 6 12 5 5 LEU CA C 54.1 0.014 6 13 5 5 LEU N N 116.936 0.017 6 14 6 6 TRP H H 7.329 0.002 6 15 6 6 TRP CA C 59.037 0.014 6 16 6 6 TRP N N 120.782 0.017 6 17 7 7 LYS H H 7.469 0.002 6 18 7 7 LYS CA C 53.533 0.014 6 19 7 7 LYS N N 115.228 0.017 6 20 8 8 ARG H H 8.749 0.002 6 21 8 8 ARG CA C 56.179 0.014 6 22 8 8 ARG N N 120.432 0.017 6 23 9 9 PRO CA C 61.677 0.014 6 24 10 10 ILE H H 7.611 0.002 6 25 10 10 ILE CA C 59.462 0.014 6 26 10 10 ILE N N 126.659 0.017 6 27 11 11 VAL H H 9.11 0.002 6 28 11 11 VAL CA C 58.481 0.014 6 29 11 11 VAL N N 120.09 0.017 6 30 12 12 THR H H 8.486 0.002 6 31 12 12 THR CA C 62.724 0.014 6 32 12 12 THR N N 116.264 0.017 6 33 13 13 ILE H H 9.286 0.002 6 34 13 13 ILE CA C 58.015 0.014 6 35 13 13 ILE N N 120.665 0.017 6 36 14 14 ARG H H 8.593 0.002 6 37 14 14 ARG CA C 54.661 0.014 6 38 14 14 ARG N N 120.529 0.017 6 39 15 15 ILE H H 8.913 0.002 6 40 15 15 ILE CA C 59.171 0.014 6 41 15 15 ILE N N 124.786 0.017 6 42 16 16 GLY H H 9.732 0.002 6 43 16 16 GLY CA C 46.913 0.014 6 44 16 16 GLY N N 118.152 0.017 6 45 17 17 GLY H H 8.77 0.002 6 46 17 17 GLY CA C 45.036 0.014 6 47 17 17 GLY N N 105.423 0.017 6 48 18 18 GLN H H 7.985 0.002 6 49 18 18 GLN CA C 54.275 0.014 6 50 18 18 GLN N N 119.978 0.017 6 51 19 19 LEU H H 8.46 0.002 6 52 19 19 LEU CA C 54.19 0.014 6 53 19 19 LEU N N 123.43 0.017 6 54 20 20 LYS H H 9.001 0.002 6 55 20 20 LYS CA C 54.165 0.014 6 56 20 20 LYS N N 123.395 0.017 6 57 21 21 GLU H H 8.593 0.002 6 58 21 21 GLU CA C 55.142 0.014 6 59 21 21 GLU N N 119.554 0.017 6 60 22 22 ALA H H 9.248 0.002 1 61 22 22 ALA CA C 50.837 0.014 1 62 22 22 ALA N N 123.731 0.017 1 63 24 24 LEU H H 8.407 0.002 1 64 24 24 LEU CA C 55.582 0.014 1 65 24 24 LEU N N 124.603 0.017 1 66 25 25 ASP H H 8.737 0.002 1 67 25 25 ASP CA C 52.297 0.014 1 68 25 25 ASP N N 128.68 0.017 1 69 26 26 THR H H 8.194 0.002 1 70 26 26 THR CA C 65.499 0.014 1 71 26 26 THR N N 110.967 0.017 1 72 27 27 GLY H H 7.906 0.002 1 73 27 27 GLY CA C 45.161 0.014 1 74 27 27 GLY N N 108.871 0.017 1 75 28 28 ALA H H 7.506 0.002 1 76 28 28 ALA CA C 50.098 0.014 1 77 28 28 ALA N N 126.265 0.017 1 78 29 29 ASP H H 8.63 0.002 1 79 29 29 ASP CA C 57.724 0.014 1 80 29 29 ASP N N 125.988 0.017 1 81 30 30 ASP H H 7.626 0.002 1 82 30 30 ASP CA C 52.84 0.014 1 83 30 30 ASP N N 115.925 0.017 1 84 31 31 THR H H 8.295 0.002 1 85 31 31 THR CA C 63.101 0.014 1 86 31 31 THR N N 117.259 0.017 1 87 32 32 VAL H H 8.229 0.002 1 88 32 32 VAL CA C 60.296 0.014 1 89 32 32 VAL N N 127.948 0.017 1 90 33 33 ILE H H 9.213 0.002 1 91 33 33 ILE CA C 57.141 0.014 1 92 33 33 ILE N N 125.259 0.017 1 93 34 34 GLU H H 8.055 0.002 1 94 34 34 GLU CA C 55.321 0.014 1 95 34 34 GLU N N 119.758 0.017 1 96 35 35 GLU H H 7.573 0.002 1 97 35 35 GLU CA C 58.14 0.014 1 98 35 35 GLU N N 115.292 0.017 1 99 36 36 MET H H 7.037 0.002 1 100 36 36 MET CA C 54.689 0.014 1 101 36 36 MET N N 120.415 0.017 1 102 37 37 ASN H H 8.628 0.002 6 103 37 37 ASN CA C 52.683 0.014 6 104 37 37 ASN N N 118.709 0.017 6 105 38 38 LEU H H 7.284 0.002 6 106 38 38 LEU CA C 51.875 0.014 6 107 38 38 LEU N N 124.626 0.017 6 108 39 39 PRO CA C 62.701 0.014 6 109 40 40 GLY H H 8.36 0.002 6 110 40 40 GLY CA C 44.309 0.014 6 111 40 40 GLY N N 106.18 0.017 6 112 41 41 LYS H H 8.395 0.002 6 113 41 41 LYS CA C 56.21 0.014 6 114 41 41 LYS N N 119.226 0.017 6 115 42 42 TRP H H 7.405 0.002 6 116 42 42 TRP CA C 53.874 0.014 6 117 42 42 TRP N N 118.647 0.017 6 118 43 43 LYS H H 8.491 0.002 6 119 43 43 LYS CA C 52.934 0.014 6 120 43 43 LYS N N 118.073 0.017 6 121 44 44 PRO CA C 63.01 0.014 6 122 45 45 LYS H H 8.554 0.002 1 123 45 45 LYS CA C 55.607 0.014 1 124 45 45 LYS N N 122.379 0.017 1 125 46 46 MET H H 8.527 0.002 1 126 46 46 MET CA C 53.741 0.014 1 127 46 46 MET N N 122.574 0.017 1 128 47 47 ILE H H 8.854 0.002 1 129 47 47 ILE CA C 59.172 0.014 1 130 47 47 ILE N N 118.261 0.017 1 131 48 48 VAL H H 8.068 0.002 1 132 48 48 VAL CA C 61.066 0.014 1 133 48 48 VAL N N 121.072 0.017 1 134 49 49 GLY H H 7.643 0.002 1 135 49 49 GLY CA C 43.1 0.014 1 136 49 49 GLY N N 109.155 0.017 1 137 50 50 ILE H H 8.91 0.002 1 138 50 50 ILE CA C 64.812 0.014 1 139 50 50 ILE N N 120.623 0.017 1 140 51 51 GLY H H 8.108 0.002 1 141 51 51 GLY N N 103.614 0.017 1 142 52 52 GLY H H 7.062 0.002 1 143 52 52 GLY CA C 44.133 0.014 1 144 52 52 GLY N N 106.842 0.017 1 145 53 53 PHE H H 8.217 0.002 1 146 53 53 PHE CA C 57.001 0.014 1 147 53 53 PHE N N 118.106 0.017 1 148 54 54 VAL H H 9.072 0.002 1 149 54 54 VAL CA C 60.704 0.014 1 150 54 54 VAL N N 117.424 0.017 1 151 55 55 LYS H H 8.369 0.002 1 152 55 55 LYS CA C 56.249 0.014 1 153 55 55 LYS N N 125.667 0.017 1 154 56 56 VAL H H 9.075 0.002 1 155 56 56 VAL CA C 58.405 0.014 1 156 56 56 VAL N N 116.815 0.017 1 157 57 57 ARG H H 8.699 0.002 1 158 57 57 ARG CA C 55.79 0.014 1 159 57 57 ARG N N 118.532 0.017 1 160 58 58 GLN H H 9.649 0.002 1 161 58 58 GLN CA C 55.862 0.014 1 162 58 58 GLN N N 123.693 0.017 1 163 59 59 TYR H H 9.203 0.002 1 164 59 59 TYR CA C 57.281 0.014 1 165 59 59 TYR N N 129.125 0.017 1 166 60 60 ASP H H 8.862 0.002 1 167 60 60 ASP CA C 53.807 0.014 1 168 60 60 ASP N N 121.154 0.017 1 169 61 61 GLN H H 8.979 0.002 1 170 61 61 GLN CA C 56.294 0.014 1 171 61 61 GLN N N 114.149 0.017 1 172 62 62 ILE H H 8.763 0.002 1 173 62 62 ILE CA C 55.296 0.014 1 174 62 62 ILE N N 122.159 0.017 1 175 63 63 PRO CA C 61.873 0.014 6 176 64 64 ILE H H 8.838 0.002 6 177 64 64 ILE CA C 59.483 0.014 6 178 64 64 ILE N N 123.341 0.017 6 179 65 65 GLU H H 8.288 0.002 6 180 65 65 GLU CA C 54.212 0.014 6 181 65 65 GLU N N 125.49 0.017 6 182 66 66 ILE H H 9.161 0.002 6 183 66 66 ILE CA C 60.307 0.014 6 184 66 66 ILE N N 124.98 0.017 6 185 67 67 ALA H H 9.02 0.002 6 186 67 67 ALA CA C 53.223 0.014 6 187 67 67 ALA N N 131.025 0.017 6 188 68 68 GLY H H 8.673 0.002 6 189 68 68 GLY CA C 45.406 0.014 6 190 68 68 GLY N N 103.011 0.017 6 191 69 69 HIS H H 8.296 0.002 6 192 69 69 HIS CA C 54.516 0.014 6 193 69 69 HIS N N 119.388 0.017 6 194 70 70 LYS H H 8.985 0.002 6 195 70 70 LYS CA C 57.713 0.014 6 196 70 70 LYS N N 125.434 0.017 6 197 71 71 ALA H H 8.806 0.002 6 198 71 71 ALA CA C 50.801 0.014 6 199 71 71 ALA N N 126.505 0.017 6 200 72 72 ILE H H 8.482 0.002 6 201 72 72 ILE CA C 60.018 0.014 6 202 72 72 ILE N N 119.345 0.017 6 203 73 73 GLY H H 8.459 0.002 6 204 73 73 GLY CA C 45.994 0.014 6 205 73 73 GLY N N 112.343 0.017 6 206 74 74 THR H H 8.709 0.002 6 207 74 74 THR CA C 63.436 0.014 6 208 74 74 THR N N 118.55 0.017 6 209 75 75 VAL H H 9.26 0.002 6 210 75 75 VAL CA C 61.437 0.014 6 211 75 75 VAL N N 126.911 0.017 6 212 76 76 LEU H H 8.36 0.002 6 213 76 76 LEU CA C 52.226 0.014 6 214 76 76 LEU N N 125.157 0.017 6 215 77 77 VAL H H 9.179 0.002 6 216 77 77 VAL CA C 59.853 0.014 6 217 77 77 VAL N N 121.731 0.017 6 218 78 78 GLY H H 8.941 0.002 6 219 78 78 GLY CA C 45.62 0.014 6 220 78 78 GLY N N 115.694 0.017 6 221 79 79 PRO CA C 63.043 0.014 6 222 80 80 THR H H 7.727 0.002 6 223 80 80 THR CA C 56.557 0.014 6 224 80 80 THR N N 119.799 0.017 6 225 81 81 PRO CA C 63.604 0.014 6 226 82 82 ALA H H 7.473 0.002 1 227 82 82 ALA CA C 51.156 0.014 1 228 82 82 ALA N N 119.603 0.017 1 229 83 83 ASN H H 8.616 0.002 1 230 83 83 ASN CA C 53.601 0.014 1 231 83 83 ASN N N 121.203 0.017 1 232 84 84 ILE H H 9.47 0.002 1 233 84 84 ILE CA C 59.577 0.014 1 234 84 84 ILE N N 120.557 0.017 1 235 85 85 ILE H H 8.764 0.002 1 236 85 85 ILE CA C 57.796 0.014 1 237 85 85 ILE N N 121.904 0.017 1 238 86 86 GLY H H 8.132 0.002 1 239 86 86 GLY CA C 43.48 0.014 1 240 86 86 GLY N N 113.749 0.017 1 241 87 87 ARG H H 9.378 0.002 1 242 87 87 ARG CA C 61.283 0.014 1 243 87 87 ARG N N 116.792 0.017 1 244 88 88 ASN H H 7.998 0.002 1 245 88 88 ASN CA C 56.956 0.014 1 246 88 88 ASN N N 115.886 0.017 1 247 89 89 LEU H H 6.92 0.002 1 248 89 89 LEU CA C 55.2 0.014 1 249 89 89 LEU N N 116.568 0.017 1 250 90 90 LEU H H 8.251 0.002 6 251 90 90 LEU CA C 57.853 0.014 6 252 90 90 LEU N N 120.345 0.017 6 253 91 91 THR H H 7.853 0.002 6 254 91 91 THR CA C 63.556 0.014 6 255 91 91 THR N N 106.22 0.017 6 256 92 92 GLN H H 6.68 0.002 6 257 92 92 GLN CA C 57.835 0.014 6 258 92 92 GLN N N 120.052 0.017 6 259 93 93 ILE H H 6.938 0.002 6 260 93 93 ILE CA C 60.436 0.014 6 261 93 93 ILE N N 108.65 0.017 6 262 94 94 GLY H H 7.217 0.002 6 263 94 94 GLY CA C 45.955 0.014 6 264 94 94 GLY N N 108.139 0.017 6 265 95 95 ALA H H 7.485 0.002 6 266 95 95 ALA CA C 51.49 0.014 6 267 95 95 ALA N N 120.376 0.017 6 268 96 96 THR H H 9.013 0.002 6 269 96 96 THR CA C 59.452 0.014 6 270 96 96 THR N N 108.952 0.017 6 271 97 97 LEU H H 8.544 0.002 6 272 97 97 LEU CA C 53.326 0.014 6 273 97 97 LEU N N 121.333 0.017 6 274 98 98 ASN H H 8.926 0.002 6 275 98 98 ASN CA C 52.844 0.014 6 276 98 98 ASN N N 121.734 0.017 6 277 99 99 PHE H H 8.022 0.002 6 278 99 99 PHE CA C 58.954 0.014 6 279 99 99 PHE N N 122.135 0.017 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 $TOPSPIN $NMRPipe $NMRDraw $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 55.52 0.014 6 2 3 3 ILE H H 9.459 0.002 6 3 3 3 ILE CA C 55.481 0.014 6 4 3 3 ILE N N 127.724 0.017 6 5 8 8 ARG H H 8.803 0.002 6 6 8 8 ARG CA C 56.175 0.014 6 7 8 8 ARG N N 120.992 0.017 6 8 9 9 PRO CA C 61.675 0.014 6 9 10 10 ILE H H 7.594 0.002 6 10 10 10 ILE CA C 59.207 0.014 6 11 10 10 ILE N N 126.87 0.017 6 12 11 11 VAL H H 9.168 0.002 6 13 11 11 VAL CA C 58.412 0.014 6 14 11 11 VAL N N 119.997 0.017 6 15 12 12 THR H H 8.515 0.002 6 16 12 12 THR CA C 62.727 0.014 6 17 12 12 THR N N 116.357 0.017 6 18 13 13 ILE H H 9.265 0.002 6 19 13 13 ILE CA C 57.967 0.014 6 20 13 13 ILE N N 120.862 0.017 6 21 14 14 ARG H H 8.548 0.002 6 22 14 14 ARG CA C 54.628 0.014 6 23 14 14 ARG N N 121.102 0.017 6 24 15 15 ILE H H 8.932 0.002 6 25 15 15 ILE CA C 59.172 0.014 6 26 15 15 ILE N N 124.854 0.017 6 27 17 17 GLY CA C 45.024 0.014 6 28 18 18 GLN H H 8.033 0.002 6 29 18 18 GLN CA C 54.354 0.014 6 30 18 18 GLN N N 120.018 0.017 6 31 22 22 ALA H H 9.238 0.002 1 32 22 22 ALA CA C 50.821 0.014 1 33 22 22 ALA N N 123.589 0.017 1 34 23 23 LEU H H 8.58 0.002 1 35 23 23 LEU CA C 53.632 0.014 1 36 23 23 LEU N N 119.767 0.017 1 37 24 24 LEU H H 8.301 0.002 1 38 24 24 LEU CA C 54.729 0.014 1 39 24 24 LEU N N 121.664 0.017 1 40 25 25 ASP H H 8.76 0.002 1 41 25 25 ASP CA C 53.082 0.014 1 42 25 25 ASP N N 126.955 0.017 1 43 26 26 THR H H 8.383 0.002 1 44 26 26 THR CA C 64.691 0.014 1 45 26 26 THR N N 112.668 0.017 1 46 27 27 GLY H H 9.357 0.002 1 47 27 27 GLY CA C 44.956 0.014 1 48 27 27 GLY N N 109.178 0.017 1 49 28 28 ALA H H 6.89 0.002 1 50 28 28 ALA CA C 49.174 0.014 1 51 28 28 ALA N N 124.298 0.017 1 52 29 29 ASP H H 8.437 0.002 1 53 29 29 ASP CA C 58.258 0.014 1 54 29 29 ASP N N 124.127 0.017 1 55 30 30 ASP H H 7.138 0.002 1 56 30 30 ASP CA C 52.368 0.014 1 57 30 30 ASP N N 113.082 0.017 1 58 31 31 THR H H 7.773 0.002 1 59 31 31 THR CA C 63.83 0.014 1 60 31 31 THR N N 119.52 0.017 1 61 32 32 VAL H H 9.101 0.002 1 62 32 32 VAL CA C 59.669 0.014 1 63 32 32 VAL N N 128.175 0.017 1 64 33 33 ILE H H 9.193 0.002 1 65 33 33 ILE CA C 56.924 0.014 1 66 33 33 ILE N N 125.749 0.017 1 67 34 34 GLU H H 7.943 0.002 1 68 34 34 GLU CA C 55.286 0.014 1 69 34 34 GLU N N 119.702 0.017 1 70 35 35 GLU H H 7.091 0.002 1 71 35 35 GLU CA C 58.305 0.014 1 72 35 35 GLU N N 115.405 0.017 1 73 36 36 MET H H 6.963 0.002 1 74 36 36 MET CA C 54.705 0.014 1 75 36 36 MET N N 120.597 0.017 1 76 37 37 ASN H H 8.641 0.002 6 77 37 37 ASN CA C 52.617 0.014 6 78 37 37 ASN N N 118.909 0.017 6 79 38 38 LEU H H 7.43 0.002 6 80 38 38 LEU CA C 51.765 0.014 6 81 38 38 LEU N N 124.991 0.017 6 82 40 40 GLY H H 8.37 0.002 6 83 40 40 GLY N N 106.012 0.017 6 84 41 41 LYS H H 8.405 0.002 6 85 41 41 LYS CA C 56.15 0.014 6 86 41 41 LYS N N 119.339 0.017 6 87 42 42 TRP H H 7.368 0.002 6 88 42 42 TRP CA C 53.715 0.014 6 89 42 42 TRP N N 117.918 0.017 6 90 43 43 LYS H H 8.321 0.002 6 91 43 43 LYS CA C 52.86 0.014 6 92 43 43 LYS N N 117.931 0.017 6 93 44 44 PRO CA C 63.198 0.014 6 94 45 45 LYS H H 8.595 0.002 1 95 45 45 LYS CA C 55.213 0.014 1 96 45 45 LYS N N 122.259 0.017 1 97 46 46 MET H H 8.389 0.002 1 98 46 46 MET CA C 54.199 0.014 1 99 46 46 MET N N 121.854 0.017 1 100 47 47 ILE H H 8.781 0.002 1 101 47 47 ILE CA C 59.702 0.014 1 102 47 47 ILE N N 118.373 0.017 1 103 48 48 VAL H H 8.412 0.002 1 104 48 48 VAL CA C 61.012 0.014 1 105 48 48 VAL N N 121.117 0.017 1 106 49 49 GLY H H 7.757 0.002 1 107 49 49 GLY CA C 44.895 0.014 1 108 49 49 GLY N N 111.623 0.017 1 109 50 50 ILE H H 8.134 0.002 1 110 50 50 ILE CA C 64.634 0.014 1 111 50 50 ILE N N 123.378 0.017 1 112 51 51 GLY CA C 43.632 0.014 1 113 52 52 GLY H H 7.297 0.002 1 114 52 52 GLY CA C 44.515 0.014 1 115 52 52 GLY N N 105.352 0.017 1 116 53 53 PHE H H 8.034 0.002 1 117 53 53 PHE CA C 56.141 0.014 1 118 53 53 PHE N N 117.894 0.017 1 119 54 54 VAL H H 8.942 0.002 1 120 54 54 VAL CA C 61.344 0.014 1 121 54 54 VAL N N 119.873 0.017 1 122 55 55 LYS H H 8.62 0.002 1 123 55 55 LYS CA C 56.817 0.014 1 124 55 55 LYS N N 127.969 0.017 1 125 56 56 VAL H H 8.782 0.002 1 126 56 56 VAL CA C 58.274 0.014 1 127 56 56 VAL N N 116.245 0.017 1 128 57 57 ARG H H 9.033 0.002 1 129 57 57 ARG CA C 55.366 0.014 1 130 57 57 ARG N N 119.467 0.017 1 131 58 58 GLN H H 9.745 0.002 1 132 58 58 GLN CA C 56.055 0.014 1 133 58 58 GLN N N 123.551 0.017 1 134 59 59 TYR H H 9.214 0.002 1 135 59 59 TYR CA C 57.419 0.014 1 136 59 59 TYR N N 129.134 0.017 1 137 60 60 ASP H H 8.954 0.002 1 138 60 60 ASP CA C 53.707 0.014 1 139 60 60 ASP N N 120.572 0.017 1 140 61 61 GLN H H 8.916 0.002 1 141 61 61 GLN CA C 56.276 0.014 1 142 61 61 GLN N N 113.985 0.017 1 143 62 62 ILE H H 8.732 0.002 1 144 62 62 ILE CA C 55.265 0.014 1 145 62 62 ILE N N 122.333 0.017 1 146 63 63 PRO CA C 61.927 0.014 6 147 64 64 ILE H H 8.861 0.002 6 148 64 64 ILE CA C 59.21 0.014 6 149 64 64 ILE N N 123.77 0.017 6 150 65 65 GLU H H 8.266 0.002 6 151 65 65 GLU N N 125.557 0.017 6 152 66 66 ILE H H 9.21 0.002 6 153 66 66 ILE N N 125.237 0.017 6 154 71 71 ALA CA C 50.799 0.014 6 155 72 72 ILE H H 8.44 0.002 6 156 72 72 ILE CA C 59.99 0.014 6 157 72 72 ILE N N 119.489 0.017 6 158 73 73 GLY H H 8.46 0.002 6 159 73 73 GLY CA C 46.045 0.014 6 160 73 73 GLY N N 112.594 0.017 6 161 74 74 THR H H 8.612 0.002 6 162 74 74 THR CA C 63.752 0.014 6 163 74 74 THR N N 118.691 0.017 6 164 75 75 VAL H H 9.036 0.002 6 165 75 75 VAL CA C 61.47 0.014 6 166 75 75 VAL N N 124.348 0.017 6 167 76 76 LEU H H 8.402 0.002 6 168 76 76 LEU CA C 52.445 0.014 6 169 76 76 LEU N N 125.425 0.017 6 170 77 77 VAL H H 9.253 0.002 6 171 77 77 VAL CA C 59.92 0.014 6 172 77 77 VAL N N 121.455 0.017 6 173 78 78 GLY H H 8.784 0.002 6 174 78 78 GLY CA C 45.626 0.014 6 175 78 78 GLY N N 113.541 0.017 6 176 79 79 PRO CA C 62.794 0.014 6 177 80 80 THR H H 8.109 0.002 6 178 80 80 THR CA C 56.689 0.014 6 179 80 80 THR N N 118.195 0.017 6 180 81 81 PRO CA C 63.267 0.014 6 181 82 82 ALA H H 7.346 0.002 1 182 82 82 ALA CA C 51.078 0.014 1 183 82 82 ALA N N 120.243 0.017 1 184 83 83 ASN H H 8.641 0.002 1 185 83 83 ASN CA C 53.667 0.014 1 186 83 83 ASN N N 119.865 0.017 1 187 84 84 ILE H H 9.653 0.002 1 188 84 84 ILE CA C 61.337 0.014 1 189 84 84 ILE N N 127.537 0.017 1 190 85 85 ILE H H 9.295 0.002 1 191 85 85 ILE CA C 58.245 0.014 1 192 85 85 ILE N N 125.928 0.017 1 193 86 86 GLY H H 8.088 0.002 1 194 86 86 GLY CA C 43.455 0.014 1 195 86 86 GLY N N 112.631 0.017 1 196 87 87 ARG H H 9.179 0.002 1 197 87 87 ARG CA C 61.313 0.014 1 198 87 87 ARG N N 116.848 0.017 1 199 88 88 ASN H H 7.893 0.002 1 200 88 88 ASN CA C 56.786 0.014 1 201 88 88 ASN N N 115.103 0.017 1 202 89 89 LEU H H 6.96 0.002 1 203 89 89 LEU CA C 55.219 0.014 1 204 89 89 LEU N N 115.95 0.017 1 205 90 90 LEU H H 8.358 0.002 6 206 90 90 LEU CA C 57.832 0.014 6 207 90 90 LEU N N 120.153 0.017 6 208 91 91 THR H H 7.803 0.002 6 209 91 91 THR CA C 63.519 0.014 6 210 91 91 THR N N 105.928 0.017 6 211 93 93 ILE H H 6.953 0.002 6 212 93 93 ILE CA C 60.443 0.014 6 213 93 93 ILE N N 108.694 0.017 6 214 94 94 GLY CA C 45.994 0.014 6 215 95 95 ALA H H 7.437 0.002 6 216 95 95 ALA CA C 51.519 0.014 6 217 95 95 ALA N N 120.254 0.017 6 218 96 96 THR CA C 59.425 0.014 6 219 97 97 LEU H H 8.500 0.002 6 220 97 97 LEU CA C 53.241 0.014 6 221 97 97 LEU N N 121.512 0.017 6 222 98 98 ASN CA C 52.742 0.014 6 223 99 99 PHE H H 7.992 0.002 6 224 99 99 PHE CA C 58.986 0.014 6 225 99 99 PHE N N 121.891 0.017 6 stop_ save_