data_4225 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of Escherichia coli glutaredoxin3-glutathione mixed disulfide complex ; _BMRB_accession_number 4225 _BMRB_flat_file_name bmr4225.str _Entry_type original _Submission_date 1998-08-17 _Accession_date 1998-08-17 _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 Nordstrand K. . . 2 Aslund F. . . 3 Holmgren A. . . 4 Otting G. . . 5 Berndt K. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 501 "15N chemical shifts" 87 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-28 update BMRB 'Updating non-standard residue' 2000-03-09 original author . stop_ _Original_release_date 1998-08-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Nordstrand, K., Aslund, F., Holmgren, A., Otting, G., and Berndt, K.D., "NMR Structure of Escherichia coli Glutaredoxin 3-glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism," J. Mol. Biol. 286, 541-552 (1999). ; _Citation_title ; NMR Structure of Escherichia coli Glutaredoxin 3-glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99141205 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nordstrand K. . . 2 Aslund F. . . 3 Holmgren A. . . 4 Otting G. . . 5 Berndt K. D. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 286 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 541 _Page_last 552 _Year 1999 _Details . loop_ _Keyword 'electron transport' oxidoreductase thiol-disulfide thioltransferase 'thioredoxin superfamily' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full ; Bartels, C. et al. J. Biomol. NMR 5, 1-10 (1995) ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 . . . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref2 _Saveframe_category citation _Citation_full ; Guntert, P. et al. J. Biomol. NMR 2, 619-629 (1992) ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 . . . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_Grx3 _Saveframe_category molecular_system _Mol_system_name 'Glutaredoxin 3 system' _Abbreviation_common Grx3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Glutaredoxin 3' $Glutaredoxin_3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Glutaredoxin_3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Glutaredoxin 3' _Name_variant 'C14S, C65Y' _Abbreviation_common Grx3 _Molecular_mass . _Mol_thiol_state . _Details ; The molecule is a mixed disulfide between Grx3 and glutathione (heteroatom name GSH in the PDB data base). In the present study, Grx3 contains the mutations C14S/C65Y and the mixed disulfide is referred to as Grx3-SG. Grx3, glutaredoxin 3 -SG, disulfide bonded glutathione (PDB hetero atom name: GSH) ; ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; ANVEIYTKETCPYSHRAKAL LSSKGVSFQELPIDGNAAKR EEMIKRSGRTTVPQIFIDAQ HIGGYDDLYALDARGGLDPL LKX ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASN 3 VAL 4 GLU 5 ILE 6 TYR 7 THR 8 LYS 9 GLU 10 THR 11 CYS 12 PRO 13 TYR 14 SER 15 HIS 16 ARG 17 ALA 18 LYS 19 ALA 20 LEU 21 LEU 22 SER 23 SER 24 LYS 25 GLY 26 VAL 27 SER 28 PHE 29 GLN 30 GLU 31 LEU 32 PRO 33 ILE 34 ASP 35 GLY 36 ASN 37 ALA 38 ALA 39 LYS 40 ARG 41 GLU 42 GLU 43 MET 44 ILE 45 LYS 46 ARG 47 SER 48 GLY 49 ARG 50 THR 51 THR 52 VAL 53 PRO 54 GLN 55 ILE 56 PHE 57 ILE 58 ASP 59 ALA 60 GLN 61 HIS 62 ILE 63 GLY 64 GLY 65 TYR 66 ASP 67 ASP 68 LEU 69 TYR 70 ALA 71 LEU 72 ASP 73 ALA 74 ARG 75 GLY 76 GLY 77 LEU 78 ASP 79 PRO 80 LEU 81 LEU 82 LYS 83 GSH stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_GSH _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common GLUTATHIONE _BMRB_code GSH _PDB_code GSH _Standard_residue_derivative . _Molecular_mass 307.323 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? CA1 CA1 C . 0 . ? C1 C1 C . 0 . ? O11 O11 O . 0 . ? O12 O12 O . 0 . ? CB1 CB1 C . 0 . ? CG1 CG1 C . 0 . ? CD1 CD1 C . 0 . ? OE1 OE1 O . 0 . ? N2 N2 N . 0 . ? CA2 CA2 C . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? CB2 CB2 C . 0 . ? SG2 SG2 S . 0 . ? N3 N3 N . 0 . ? CA3 CA3 C . 0 . ? C3 C3 C . 0 . ? O31 O31 O . 0 . ? O32 O32 O . 0 . ? HN11 HN11 H . 0 . ? HN12 HN12 H . 0 . ? HA1 HA1 H . 0 . ? H12 H12 H . 0 . ? HB12 HB12 H . 0 . ? HB13 HB13 H . 0 . ? HG12 HG12 H . 0 . ? HG13 HG13 H . 0 . ? HN2 HN2 H . 0 . ? HA2 HA2 H . 0 . ? HB22 HB22 H . 0 . ? HB23 HB23 H . 0 . ? HSG HSG H . 0 . ? HN3 HN3 H . 0 . ? HA31 HA31 H . 0 . ? HA32 HA32 H . 0 . ? H32 H32 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 CA1 ? ? SING N1 HN11 ? ? SING N1 HN12 ? ? SING CA1 C1 ? ? SING CA1 CB1 ? ? SING CA1 HA1 ? ? DOUB C1 O11 ? ? SING C1 O12 ? ? SING O12 H12 ? ? SING CB1 CG1 ? ? SING CB1 HB12 ? ? SING CB1 HB13 ? ? SING CG1 CD1 ? ? SING CG1 HG12 ? ? SING CG1 HG13 ? ? DOUB CD1 OE1 ? ? SING CD1 N2 ? ? SING N2 CA2 ? ? SING N2 HN2 ? ? SING CA2 C2 ? ? SING CA2 CB2 ? ? SING CA2 HA2 ? ? DOUB C2 O2 ? ? SING C2 N3 ? ? SING CB2 SG2 ? ? SING CB2 HB22 ? ? SING CB2 HB23 ? ? SING SG2 HSG ? ? SING N3 CA3 ? ? SING N3 HN3 ? ? SING CA3 C3 ? ? SING CA3 HA31 ? ? SING CA3 HA32 ? ? DOUB C3 O31 ? ? SING C3 O32 ? ? SING O32 H32 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Glutaredoxin_3 'Escherichia coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $Glutaredoxin_3 'recombinant technology' . Escherichia coli BL21(DE3) plasmid pET-24D 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 $Glutaredoxin_3 2.8 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Glutaredoxin_3 5.0 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_PROSA _Saveframe_category software _Name PROSA _Version 3.6 loop_ _Task 'spectral FT-transformations; baseline correction' stop_ _Details . _Citation_label $ref2 save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'spectral analysis' stop_ _Details . _Citation_label $ref1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model . _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details ; DQF-COSY 3QF-COSY small flip angle COSY TOCSY NOESY omega1-decoupled NOESY 2D HNHB 15N-HSQC NOESY-15N-HSQC ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.0 0.1 n/a pressure 1 . atm temperature 301 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Glutaredoxin 3' _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 ALA HA H 4.42 . 1 2 . 1 ALA HB H 1.48 . 1 3 . 2 ASN H H 9.38 . 1 4 . 2 ASN HA H 4.97 . 1 5 . 2 ASN HB2 H 2.82 . 1 6 . 2 ASN HB3 H 2.97 . 1 7 . 2 ASN HD21 H 7.60 . 1 8 . 2 ASN HD22 H 6.83 . 1 9 . 2 ASN N N 121.2 . 1 10 . 2 ASN ND2 N 112.1 . 1 11 . 3 VAL H H 9.24 . 1 12 . 3 VAL HA H 4.96 . 1 13 . 3 VAL HB H 2.22 . 1 14 . 3 VAL HG1 H 0.86 . 1 15 . 3 VAL HG2 H 0.92 . 1 16 . 3 VAL N N 129.5 . 1 17 . 4 GLU H H 9.32 . 1 18 . 4 GLU HA H 5.33 . 1 19 . 4 GLU HB2 H 2.01 . 1 20 . 4 GLU HB3 H 1.95 . 1 21 . 4 GLU HG2 H 2.06 . 1 22 . 4 GLU HG3 H 2.06 . 1 23 . 4 GLU N N 127.0 . 1 24 . 5 ILE H H 8.62 . 1 25 . 5 ILE HA H 5.49 . 1 26 . 5 ILE HB H 1.42 . 1 27 . 5 ILE HG12 H 1.40 . 2 28 . 5 ILE HG13 H 0.91 . 2 29 . 5 ILE HG2 H 0.64 . 1 30 . 5 ILE HD1 H 0.40 . 1 31 . 5 ILE N N 118.2 . 1 32 . 6 TYR H H 9.08 . 1 33 . 6 TYR HA H 5.51 . 1 34 . 6 TYR HB2 H 2.94 . 1 35 . 6 TYR HB3 H 3.11 . 1 36 . 6 TYR HD1 H 7.27 . 1 37 . 6 TYR HD2 H 7.27 . 1 38 . 6 TYR HE1 H 6.55 . 1 39 . 6 TYR HE2 H 6.55 . 1 40 . 6 TYR N N 129.4 . 1 41 . 7 THR H H 7.71 . 1 42 . 7 THR HA H 4.72 . 1 43 . 7 THR HB H 4.04 . 1 44 . 7 THR HG2 H 1.02 . 1 45 . 7 THR N N 108.9 . 1 46 . 8 LYS H H 7.07 . 1 47 . 8 LYS HA H 5.10 . 1 48 . 8 LYS HB2 H 1.77 . 1 49 . 8 LYS HB3 H 1.62 . 1 50 . 8 LYS HG2 H 1.45 . 1 51 . 8 LYS HG3 H 1.45 . 1 52 . 8 LYS HE2 H 2.97 . 1 53 . 8 LYS HE3 H 2.97 . 1 54 . 8 LYS N N 114.6 . 1 55 . 9 GLU H H 10.64 . 1 56 . 9 GLU HA H 4.17 . 1 57 . 9 GLU HB2 H 2.11 . 2 58 . 9 GLU HB3 H 2.18 . 2 59 . 9 GLU HG2 H 2.41 . 2 60 . 9 GLU HG3 H 2.43 . 2 61 . 9 GLU N N 128.6 . 1 62 . 10 THR H H 7.55 . 1 63 . 10 THR HA H 4.39 . 1 64 . 10 THR HB H 4.66 . 1 65 . 10 THR HG2 H 1.30 . 1 66 . 10 THR N N 104.6 . 1 67 . 11 CYS H H 7.42 . 1 68 . 11 CYS HA H 5.55 . 1 69 . 11 CYS HB2 H 3.18 . 1 70 . 11 CYS HB3 H 3.18 . 1 71 . 11 CYS N N 118.7 . 1 72 . 12 PRO HA H 4.38 . 1 73 . 12 PRO HB2 H 1.48 . 1 74 . 12 PRO HB3 H 2.28 . 1 75 . 12 PRO HG2 H 2.02 . 2 76 . 12 PRO HG3 H 1.84 . 2 77 . 12 PRO HD2 H 4.38 . 2 78 . 12 PRO HD3 H 4.03 . 2 79 . 13 TYR H H 6.61 . 1 80 . 13 TYR HA H 3.63 . 1 81 . 13 TYR HB2 H 3.17 . 1 82 . 13 TYR HB3 H 2.89 . 1 83 . 13 TYR HD1 H 7.14 . 1 84 . 13 TYR HD2 H 7.14 . 1 85 . 13 TYR HE1 H 7.02 . 1 86 . 13 TYR HE2 H 7.02 . 1 87 . 13 TYR N N 112.5 . 1 88 . 14 SER H H 7.40 . 1 89 . 14 SER HA H 3.97 . 1 90 . 14 SER HB2 H 3.58 . 1 91 . 14 SER HB3 H 4.32 . 1 92 . 14 SER HG H 5.54 . 1 93 . 14 SER N N 113.5 . 1 94 . 15 HIS H H 7.05 . 1 95 . 15 HIS HA H 4.17 . 1 96 . 15 HIS HB2 H 3.18 . 1 97 . 15 HIS HB3 H 3.18 . 1 98 . 15 HIS HD2 H 7.01 . 1 99 . 15 HIS HE1 H 7.98 . 1 100 . 15 HIS N N 118.8 . 1 101 . 16 ARG H H 8.18 . 1 102 . 16 ARG HA H 3.95 . 1 103 . 16 ARG HB2 H 0.89 . 1 104 . 16 ARG HB3 H 1.22 . 1 105 . 16 ARG HG2 H 1.59 . 1 106 . 16 ARG HG3 H 1.43 . 1 107 . 16 ARG HD2 H 2.62 . 2 108 . 16 ARG HD3 H 2.55 . 2 109 . 16 ARG HE H 6.83 . 1 110 . 16 ARG N N 118.1 . 1 111 . 16 ARG NE N 83.6 . 1 112 . 17 ALA H H 7.70 . 1 113 . 17 ALA HA H 4.18 . 1 114 . 17 ALA HB H 1.56 . 1 115 . 17 ALA N N 121.8 . 1 116 . 18 LYS H H 7.77 . 1 117 . 18 LYS HA H 3.34 . 1 118 . 18 LYS HB2 H 1.88 . 1 119 . 18 LYS HB3 H 1.88 . 1 120 . 18 LYS HG2 H 1.62 . 2 121 . 18 LYS HG3 H 0.91 . 2 122 . 18 LYS HD2 H 1.96 . 1 123 . 18 LYS HD3 H 1.96 . 1 124 . 18 LYS HE2 H 2.92 . 2 125 . 18 LYS HE3 H 3.15 . 2 126 . 18 LYS N N 116.6 . 1 127 . 19 ALA H H 8.12 . 1 128 . 19 ALA HA H 4.18 . 1 129 . 19 ALA HB H 1.49 . 1 130 . 19 ALA N N 120.4 . 1 131 . 20 LEU H H 7.89 . 1 132 . 20 LEU HA H 4.25 . 1 133 . 20 LEU HB2 H 2.03 . 1 134 . 20 LEU HB3 H 1.95 . 1 135 . 20 LEU HG H 1.64 . 1 136 . 20 LEU HD1 H 1.03 . 1 137 . 20 LEU HD2 H 0.77 . 1 138 . 20 LEU N N 121.6 . 1 139 . 21 LEU H H 7.92 . 1 140 . 21 LEU HA H 3.83 . 1 141 . 21 LEU HB2 H 1.84 . 1 142 . 21 LEU HB3 H 1.25 . 1 143 . 21 LEU HG H 1.75 . 1 144 . 21 LEU HD1 H 0.34 . 1 145 . 21 LEU HD2 H 0.73 . 1 146 . 21 LEU N N 119.0 . 1 147 . 22 SER H H 9.13 . 1 148 . 22 SER HA H 4.52 . 1 149 . 22 SER HB2 H 4.09 . 2 150 . 22 SER HB3 H 4.12 . 2 151 . 22 SER N N 115.4 . 1 152 . 23 SER H H 8.44 . 1 153 . 23 SER HA H 4.38 . 1 154 . 23 SER HB2 H 4.12 . 2 155 . 23 SER HB3 H 4.16 . 2 156 . 23 SER N N 119.7 . 1 157 . 24 LYS H H 7.44 . 1 158 . 24 LYS HA H 4.42 . 1 159 . 24 LYS HB2 H 2.01 . 1 160 . 24 LYS HB3 H 2.08 . 1 161 . 24 LYS HG2 H 1.32 . 1 162 . 24 LYS HG3 H 1.71 . 1 163 . 24 LYS HD2 H 1.57 . 1 164 . 24 LYS HD3 H 1.57 . 1 165 . 24 LYS HE2 H 2.71 . 2 166 . 24 LYS HE3 H 2.67 . 2 167 . 24 LYS N N 119.2 . 1 168 . 25 GLY H H 8.11 . 1 169 . 25 GLY HA2 H 3.88 . 2 170 . 25 GLY HA3 H 4.10 . 2 171 . 25 GLY N N 107.3 . 1 172 . 26 VAL H H 7.29 . 1 173 . 26 VAL HA H 4.27 . 1 174 . 26 VAL HB H 2.20 . 1 175 . 26 VAL HG1 H 1.04 . 1 176 . 26 VAL HG2 H 0.99 . 1 177 . 26 VAL N N 116.6 . 1 178 . 27 SER H H 8.58 . 1 179 . 27 SER HA H 4.43 . 1 180 . 27 SER HB2 H 3.81 . 1 181 . 27 SER HB3 H 3.81 . 1 182 . 27 SER N N 121.2 . 1 183 . 28 PHE H H 7.52 . 1 184 . 28 PHE HA H 5.10 . 1 185 . 28 PHE HB2 H 2.72 . 1 186 . 28 PHE HB3 H 2.72 . 1 187 . 28 PHE HD1 H 6.82 . 1 188 . 28 PHE HD2 H 6.82 . 1 189 . 28 PHE HE1 H 7.32 . 1 190 . 28 PHE HE2 H 7.32 . 1 191 . 28 PHE HZ H 7.33 . 1 192 . 28 PHE N N 118.2 . 1 193 . 29 GLN H H 9.18 . 1 194 . 29 GLN HA H 4.58 . 1 195 . 29 GLN HB2 H 2.12 . 1 196 . 29 GLN HB3 H 2.05 . 1 197 . 29 GLN HG2 H 2.30 . 1 198 . 29 GLN HG3 H 2.30 . 1 199 . 29 GLN HE21 H 7.44 . 1 200 . 29 GLN HE22 H 6.90 . 1 201 . 29 GLN N N 120.7 . 1 202 . 29 GLN NE2 N 112.0 . 1 203 . 30 GLU H H 9.01 . 1 204 . 30 GLU HA H 4.84 . 1 205 . 30 GLU HB2 H 1.96 . 1 206 . 30 GLU HB3 H 2.11 . 1 207 . 30 GLU HG2 H 2.25 . 1 208 . 30 GLU HG3 H 2.25 . 1 209 . 30 GLU N N 127.9 . 1 210 . 31 LEU H H 9.08 . 1 211 . 31 LEU HA H 4.85 . 1 212 . 31 LEU HB2 H 1.07 . 1 213 . 31 LEU HB3 H 0.81 . 1 214 . 31 LEU HG H 1.21 . 1 215 . 31 LEU HD1 H 0.27 . 1 216 . 31 LEU HD2 H 0.67 . 1 217 . 31 LEU N N 129.4 . 1 218 . 32 PRO HA H 4.86 . 1 219 . 32 PRO HB2 H 2.07 . 2 220 . 32 PRO HB3 H 2.41 . 2 221 . 32 PRO HG2 H 2.17 . 2 222 . 32 PRO HG3 H 1.84 . 2 223 . 32 PRO HD2 H 3.77 . 1 224 . 32 PRO HD3 H 3.58 . 1 225 . 33 ILE H H 9.01 . 1 226 . 33 ILE HA H 4.79 . 1 227 . 33 ILE HB H 2.18 . 1 228 . 33 ILE HG12 H 1.34 . 1 229 . 33 ILE HG13 H 1.15 . 1 230 . 33 ILE HG2 H 1.16 . 1 231 . 33 ILE HD1 H 0.86 . 1 232 . 33 ILE N N 114.0 . 1 233 . 34 ASP H H 9.30 . 1 234 . 34 ASP HA H 4.24 . 1 235 . 34 ASP HB2 H 2.56 . 1 236 . 34 ASP HB3 H 2.56 . 1 237 . 34 ASP N N 122.3 . 1 238 . 35 GLY H H 9.26 . 1 239 . 35 GLY HA2 H 3.96 . 1 240 . 35 GLY HA3 H 3.96 . 1 241 . 35 GLY N N 113.0 . 1 242 . 36 ASN H H 7.79 . 1 243 . 36 ASN HA H 4.98 . 1 244 . 36 ASN HB2 H 2.41 . 2 245 . 36 ASN HB3 H 2.97 . 2 246 . 36 ASN HD21 H 7.91 . 1 247 . 36 ASN HD22 H 7.04 . 1 248 . 36 ASN N N 118.2 . 1 249 . 36 ASN ND2 N 112.5 . 1 250 . 37 ALA H H 8.80 . 1 251 . 37 ALA HA H 4.12 . 1 252 . 37 ALA HB H 1.50 . 1 253 . 37 ALA N N 127.4 . 1 254 . 38 ALA H H 8.40 . 1 255 . 38 ALA HA H 4.24 . 1 256 . 38 ALA HB H 1.52 . 1 257 . 38 ALA N N 120.4 . 1 258 . 39 LYS H H 7.84 . 1 259 . 39 LYS HA H 4.20 . 1 260 . 39 LYS HB2 H 1.84 . 2 261 . 39 LYS HB3 H 1.91 . 2 262 . 39 LYS HG2 H 1.58 . 1 263 . 39 LYS HG3 H 1.58 . 1 264 . 39 LYS HD2 H 1.72 . 1 265 . 39 LYS HD3 H 1.72 . 1 266 . 39 LYS HE2 H 2.98 . 1 267 . 39 LYS HE3 H 2.98 . 1 268 . 39 LYS N N 120.7 . 1 269 . 40 ARG H H 8.00 . 1 270 . 40 ARG HA H 3.88 . 1 271 . 40 ARG HB2 H 1.98 . 1 272 . 40 ARG HB3 H 2.08 . 1 273 . 40 ARG HG2 H 1.54 . 2 274 . 40 ARG HG3 H 1.42 . 2 275 . 40 ARG HD2 H 3.22 . 1 276 . 40 ARG HD3 H 3.22 . 1 277 . 40 ARG HE H 7.65 . 1 278 . 40 ARG N N 119.7 . 1 279 . 40 ARG NE N 85.1 . 1 280 . 41 GLU H H 8.23 . 1 281 . 41 GLU HA H 3.92 . 1 282 . 41 GLU HB2 H 2.09 . 2 283 . 41 GLU HB3 H 2.14 . 2 284 . 41 GLU HG2 H 2.37 . 2 285 . 41 GLU HG3 H 2.29 . 2 286 . 41 GLU N N 117.9 . 1 287 . 42 GLU H H 7.88 . 1 288 . 42 GLU HA H 3.95 . 1 289 . 42 GLU HB2 H 2.27 . 1 290 . 42 GLU HB3 H 2.36 . 1 291 . 42 GLU HG2 H 1.98 . 1 292 . 42 GLU HG3 H 1.98 . 1 293 . 42 GLU N N 120.8 . 1 294 . 43 MET H H 8.02 . 1 295 . 43 MET HA H 2.80 . 1 296 . 43 MET HB2 H 1.40 . 1 297 . 43 MET HB3 H 2.33 . 1 298 . 43 MET HG2 H 1.59 . 1 299 . 43 MET HG3 H 1.59 . 1 300 . 43 MET HE H 1.68 . 1 301 . 43 MET N N 119.6 . 1 302 . 44 ILE H H 8.35 . 1 303 . 44 ILE HA H 4.02 . 1 304 . 44 ILE HB H 1.75 . 1 305 . 44 ILE HG12 H 1.08 . 2 306 . 44 ILE HG13 H 1.78 . 2 307 . 44 ILE HG2 H 0.69 . 1 308 . 44 ILE HD1 H 0.73 . 1 309 . 44 ILE N N 123.8 . 1 310 . 45 LYS H H 8.45 . 1 311 . 45 LYS HA H 3.94 . 1 312 . 45 LYS HB2 H 1.88 . 1 313 . 45 LYS HB3 H 1.88 . 1 314 . 45 LYS HG2 H 1.51 . 2 315 . 45 LYS HG3 H 1.39 . 2 316 . 45 LYS HD2 H 1.63 . 1 317 . 45 LYS HD3 H 1.63 . 1 318 . 45 LYS HE2 H 2.95 . 1 319 . 45 LYS HE3 H 2.95 . 1 320 . 45 LYS N N 121.9 . 1 321 . 46 ARG H H 8.30 . 1 322 . 46 ARG HA H 4.04 . 1 323 . 46 ARG HB2 H 1.79 . 2 324 . 46 ARG HB3 H 1.88 . 2 325 . 46 ARG HG2 H 1.39 . 2 326 . 46 ARG HG3 H 1.51 . 2 327 . 46 ARG HD2 H 2.61 . 2 328 . 46 ARG HD3 H 2.99 . 2 329 . 46 ARG HE H 6.11 . 1 330 . 46 ARG N N 115.1 . 1 331 . 46 ARG NE N 82.3 . 1 332 . 47 SER H H 8.20 . 1 333 . 47 SER HA H 3.61 . 1 334 . 47 SER HB2 H 3.46 . 1 335 . 47 SER HB3 H 3.46 . 1 336 . 47 SER HG H 4.81 . 1 337 . 47 SER N N 110.0 . 1 338 . 48 GLY H H 8.50 . 1 339 . 48 GLY HA2 H 3.84 . 2 340 . 48 GLY HA3 H 4.10 . 2 341 . 48 GLY N N 112.0 . 1 342 . 49 ARG H H 8.36 . 1 343 . 49 ARG HA H 4.77 . 1 344 . 49 ARG HB2 H 1.61 . 1 345 . 49 ARG HB3 H 1.89 . 1 346 . 49 ARG HG2 H 1.64 . 1 347 . 49 ARG HG3 H 1.72 . 1 348 . 49 ARG HD2 H 3.23 . 1 349 . 49 ARG HD3 H 3.34 . 1 350 . 49 ARG HE H 7.45 . 1 351 . 49 ARG N N 119.7 . 1 352 . 49 ARG NE N 84.1 . 1 353 . 50 THR H H 8.14 . 1 354 . 50 THR HA H 4.31 . 1 355 . 50 THR HB H 4.40 . 1 356 . 50 THR HG2 H 1.07 . 1 357 . 50 THR N N 101.8 . 1 358 . 51 THR H H 6.89 . 1 359 . 51 THR HA H 4.77 . 1 360 . 51 THR HB H 4.00 . 1 361 . 51 THR HG2 H 0.91 . 1 362 . 51 THR N N 108.3 . 1 363 . 52 VAL H H 8.63 . 1 364 . 52 VAL HA H 4.58 . 1 365 . 52 VAL HB H 1.94 . 1 366 . 52 VAL HG1 H 1.05 . 1 367 . 52 VAL HG2 H 1.11 . 1 368 . 52 VAL N N 115.0 . 1 369 . 53 PRO HA H 5.37 . 1 370 . 53 PRO HB2 H 2.02 . 2 371 . 53 PRO HB3 H 2.32 . 2 372 . 53 PRO HG2 H 1.84 . 1 373 . 53 PRO HG3 H 1.84 . 1 374 . 53 PRO HD2 H 3.16 . 2 375 . 53 PRO HD3 H 4.26 . 2 376 . 54 GLN H H 7.33 . 1 377 . 54 GLN HA H 4.94 . 1 378 . 54 GLN HB2 H 1.83 . 1 379 . 54 GLN HB3 H 2.11 . 1 380 . 54 GLN HG2 H 2.24 . 2 381 . 54 GLN HG3 H 3.14 . 2 382 . 54 GLN HE21 H 7.95 . 1 383 . 54 GLN HE22 H 6.06 . 1 384 . 54 GLN N N 112.5 . 1 385 . 54 GLN NE2 N 114.0 . 1 386 . 55 ILE H H 9.05 . 1 387 . 55 ILE HA H 5.17 . 1 388 . 55 ILE HB H 1.50 . 1 389 . 55 ILE HG12 H 1.45 . 2 390 . 55 ILE HG13 H 1.00 . 2 391 . 55 ILE HG2 H 0.76 . 1 392 . 55 ILE HD1 H 0.80 . 1 393 . 55 ILE N N 123.7 . 1 394 . 56 PHE H H 9.44 . 1 395 . 56 PHE HA H 5.40 . 1 396 . 56 PHE HB2 H 3.06 . 1 397 . 56 PHE HB3 H 2.69 . 1 398 . 56 PHE HD1 H 7.11 . 1 399 . 56 PHE HD2 H 7.11 . 1 400 . 56 PHE HE1 H 7.24 . 1 401 . 56 PHE HE2 H 7.24 . 1 402 . 56 PHE HZ H 6.51 . 1 403 . 56 PHE N N 126.9 . 1 404 . 57 ILE H H 8.95 . 1 405 . 57 ILE HA H 4.75 . 1 406 . 57 ILE HB H 1.62 . 1 407 . 57 ILE HG12 H 0.97 . 1 408 . 57 ILE HG13 H 1.49 . 1 409 . 57 ILE HG2 H 0.77 . 1 410 . 57 ILE HD1 H 0.61 . 1 411 . 57 ILE N N 119.7 . 1 412 . 58 ASP H H 9.96 . 1 413 . 58 ASP HA H 4.56 . 1 414 . 58 ASP HB2 H 2.78 . 1 415 . 58 ASP HB3 H 3.02 . 1 416 . 58 ASP N N 131.2 . 1 417 . 59 ALA H H 9.34 . 1 418 . 59 ALA HA H 3.76 . 1 419 . 59 ALA HB H 1.64 . 1 420 . 59 ALA N N 114.0 . 1 421 . 60 GLN H H 8.35 . 1 422 . 60 GLN HA H 4.59 . 1 423 . 60 GLN HB2 H 2.20 . 1 424 . 60 GLN HB3 H 2.20 . 1 425 . 60 GLN HG2 H 2.41 . 1 426 . 60 GLN HG3 H 2.35 . 1 427 . 60 GLN HE21 H 7.55 . 1 428 . 60 GLN HE22 H 6.86 . 1 429 . 60 GLN N N 120.8 . 1 430 . 60 GLN NE2 N 111.9 . 1 431 . 61 HIS H H 9.26 . 1 432 . 61 HIS HA H 3.91 . 1 433 . 61 HIS HB2 H 3.03 . 2 434 . 61 HIS HB3 H 3.12 . 2 435 . 61 HIS HD2 H 5.69 . 1 436 . 61 HIS HE1 H 7.34 . 1 437 . 61 HIS N N 125.9 . 1 438 . 62 ILE H H 8.42 . 1 439 . 62 ILE HA H 3.90 . 1 440 . 62 ILE HB H 1.58 . 1 441 . 62 ILE HG12 H 1.50 . 1 442 . 62 ILE HG13 H 0.95 . 1 443 . 62 ILE HG2 H 0.55 . 1 444 . 62 ILE HD1 H 0.50 . 1 445 . 62 ILE N N 128.8 . 1 446 . 63 GLY H H 6.17 . 1 447 . 63 GLY HA2 H 4.63 . 2 448 . 63 GLY HA3 H 3.14 . 2 449 . 63 GLY N N 102.8 . 1 450 . 64 GLY H H 8.84 . 1 451 . 64 GLY HA2 H 4.62 . 2 452 . 64 GLY HA3 H 3.69 . 2 453 . 64 GLY N N 108.9 . 1 454 . 65 TYR H H 9.76 . 1 455 . 65 TYR HA H 3.90 . 1 456 . 65 TYR HB2 H 3.27 . 1 457 . 65 TYR HB3 H 3.48 . 1 458 . 65 TYR HD1 H 6.97 . 1 459 . 65 TYR HD2 H 6.97 . 1 460 . 65 TYR HE1 H 6.66 . 1 461 . 65 TYR HE2 H 6.66 . 1 462 . 65 TYR N N 122.8 . 1 463 . 66 ASP H H 9.86 . 1 464 . 66 ASP HA H 3.94 . 1 465 . 66 ASP HB2 H 2.44 . 1 466 . 66 ASP HB3 H 2.61 . 1 467 . 66 ASP N N 119.7 . 1 468 . 67 ASP H H 7.17 . 1 469 . 67 ASP HA H 4.28 . 1 470 . 67 ASP HB2 H 2.50 . 1 471 . 67 ASP HB3 H 2.60 . 1 472 . 67 ASP N N 117.7 . 1 473 . 68 LEU H H 8.08 . 1 474 . 68 LEU HA H 3.65 . 1 475 . 68 LEU HB2 H 1.29 . 1 476 . 68 LEU HB3 H 2.03 . 1 477 . 68 LEU HG H 1.55 . 1 478 . 68 LEU HD1 H 0.82 . 1 479 . 68 LEU HD2 H 0.91 . 1 480 . 68 LEU N N 123.4 . 1 481 . 69 TYR H H 8.97 . 1 482 . 69 TYR HA H 3.62 . 1 483 . 69 TYR HB2 H 2.27 . 1 484 . 69 TYR HB3 H 2.59 . 1 485 . 69 TYR HD1 H 6.99 . 1 486 . 69 TYR HD2 H 6.99 . 1 487 . 69 TYR HE1 H 6.80 . 1 488 . 69 TYR HE2 H 6.80 . 1 489 . 69 TYR N N 118.7 . 1 490 . 70 ALA H H 7.91 . 1 491 . 70 ALA HA H 3.92 . 1 492 . 70 ALA HB H 1.46 . 1 493 . 70 ALA N N 120.1 . 1 494 . 71 LEU H H 7.72 . 1 495 . 71 LEU HA H 3.94 . 1 496 . 71 LEU HB2 H 1.53 . 1 497 . 71 LEU HB3 H 1.78 . 1 498 . 71 LEU HG H 1.13 . 1 499 . 71 LEU HD1 H 0.76 . 1 500 . 71 LEU HD2 H 0.82 . 1 501 . 71 LEU N N 118.8 . 1 502 . 72 ASP H H 8.03 . 1 503 . 72 ASP HA H 4.36 . 1 504 . 72 ASP HB2 H 2.44 . 1 505 . 72 ASP HB3 H 2.48 . 1 506 . 72 ASP N N 118.6 . 1 507 . 73 ALA H H 8.57 . 1 508 . 73 ALA HA H 3.93 . 1 509 . 73 ALA HB H 1.20 . 1 510 . 73 ALA N N 122.3 . 1 511 . 74 ARG H H 7.23 . 1 512 . 74 ARG HA H 4.63 . 1 513 . 74 ARG HB2 H 1.78 . 1 514 . 74 ARG HB3 H 2.01 . 1 515 . 74 ARG HG2 H 1.98 . 2 516 . 74 ARG HG3 H 1.52 . 2 517 . 74 ARG HD2 H 3.14 . 1 518 . 74 ARG HD3 H 3.14 . 1 519 . 74 ARG HE H 7.32 . 1 520 . 74 ARG N N 112.5 . 1 521 . 74 ARG NE N 84.7 . 1 522 . 75 GLY H H 8.18 . 1 523 . 75 GLY HA2 H 4.02 . 2 524 . 75 GLY HA3 H 4.12 . 2 525 . 75 GLY N N 110.5 . 1 526 . 76 GLY H H 8.34 . 1 527 . 76 GLY HA2 H 4.23 . 1 528 . 76 GLY HA3 H 3.43 . 1 529 . 76 GLY N N 104.1 . 1 530 . 77 LEU H H 7.93 . 1 531 . 77 LEU HA H 4.44 . 1 532 . 77 LEU HB2 H 0.98 . 1 533 . 77 LEU HB3 H 2.09 . 1 534 . 77 LEU HG H 1.44 . 1 535 . 77 LEU HD1 H 0.75 . 1 536 . 77 LEU HD2 H 0.80 . 1 537 . 77 LEU N N 121.8 . 1 538 . 78 ASP H H 8.62 . 1 539 . 78 ASP HA H 4.37 . 1 540 . 78 ASP HB2 H 2.56 . 1 541 . 78 ASP HB3 H 2.60 . 1 542 . 78 ASP N N 119.7 . 1 543 . 79 PRO HA H 4.31 . 1 544 . 79 PRO HB2 H 1.72 . 1 545 . 79 PRO HB3 H 2.36 . 1 546 . 79 PRO HG2 H 2.00 . 1 547 . 79 PRO HG3 H 2.00 . 1 548 . 79 PRO HD2 H 3.30 . 1 549 . 79 PRO HD3 H 3.52 . 1 550 . 80 LEU H H 7.43 . 1 551 . 80 LEU HA H 4.24 . 1 552 . 80 LEU HB2 H 1.50 . 2 553 . 80 LEU HB3 H 1.98 . 2 554 . 80 LEU HG H 1.89 . 1 555 . 80 LEU HD1 H 0.90 . 1 556 . 80 LEU HD2 H 0.84 . 1 557 . 80 LEU N N 113.5 . 1 558 . 81 LEU H H 7.39 . 1 559 . 81 LEU HA H 4.25 . 1 560 . 81 LEU HB2 H 1.84 . 1 561 . 81 LEU HB3 H 1.65 . 1 562 . 81 LEU HG H 1.79 . 1 563 . 81 LEU HD1 H 0.68 . 2 564 . 81 LEU HD2 H 0.79 . 2 565 . 81 LEU N N 116.0 . 1 566 . 82 LYS H H 7.05 . 1 567 . 82 LYS HA H 4.06 . 1 568 . 82 LYS HB2 H 1.74 . 2 569 . 82 LYS HB3 H 1.81 . 2 570 . 82 LYS HG2 H 1.43 . 1 571 . 82 LYS HG3 H 1.43 . 1 572 . 82 LYS HD2 H 1.67 . 1 573 . 82 LYS HD3 H 1.67 . 1 574 . 82 LYS HE2 H 2.98 . 1 575 . 82 LYS HE3 H 2.98 . 1 576 . 82 LYS N N 124.3 . 1 577 . 83 GSH HA1 H 3.32 . 1 578 . 83 GSH HB11 H 1.90 . 1 579 . 83 GSH HB12 H 0.65 . 1 580 . 83 GSH HG11 H 2.67 . 1 581 . 83 GSH HG12 H 2.35 . 1 582 . 83 GSH HN2 H 9.58 . 1 583 . 83 GSH HA2 H 5.00 . 1 584 . 83 GSH HB21 H 2.97 . 1 585 . 83 GSH HB22 H 4.04 . 1 586 . 83 GSH HN3 H 8.65 . 1 587 . 83 GSH HA31 H 3.60 . 2 588 . 83 GSH HA32 H 4.00 . 2 stop_ save_