data_2396 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy ; _BMRB_accession_number 2396 _BMRB_flat_file_name bmr2396.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Penington Christopher J. . 2 Rule Gordon S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 18 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-16 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Penington, Christopher J., Rule, Gordon S., "Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy," Biochemistry 31 (11), 2912-2920 (1992). ; _Citation_title ; Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Penington Christopher J. . 2 Rule Gordon S. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 31 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2912 _Page_last 2920 _Year 1992 _Details . save_ ################################## # Molecular system description # ################################## save_system_glutathione_transferase _Saveframe_category molecular_system _Mol_system_name 'glutathione transferase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'glutathione transferase' $glutathione_transferase stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_glutathione_transferase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'glutathione transferase' _Name_variant 'class Mu' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 218 _Mol_residue_sequence ; MPMTLGYWNIRGLAHSIRLL LEYTDSSYEEKKYTMGDAPD YDRSQWLNEKFKLGLDFPNL PYLIDGTHKITQSNAILRYI ARKHNLCGESEKEQIREDIL ENQFMDSRMQLAKLCYDPDF EKLKPEYLQALPEMLKLYSQ FLGKQPWFLGDKITFVDFIA YDVLERNQVFEPSCLDAFPN LKDFISRFEGLEKISAYMKS SRFLPRPVFTKMAVWGNK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 MET 4 THR 5 LEU 6 GLY 7 TYR 8 TRP 9 ASN 10 ILE 11 ARG 12 GLY 13 LEU 14 ALA 15 HIS 16 SER 17 ILE 18 ARG 19 LEU 20 LEU 21 LEU 22 GLU 23 TYR 24 THR 25 ASP 26 SER 27 SER 28 TYR 29 GLU 30 GLU 31 LYS 32 LYS 33 TYR 34 THR 35 MET 36 GLY 37 ASP 38 ALA 39 PRO 40 ASP 41 TYR 42 ASP 43 ARG 44 SER 45 GLN 46 TRP 47 LEU 48 ASN 49 GLU 50 LYS 51 PHE 52 LYS 53 LEU 54 GLY 55 LEU 56 ASP 57 PHE 58 PRO 59 ASN 60 LEU 61 PRO 62 TYR 63 LEU 64 ILE 65 ASP 66 GLY 67 THR 68 HIS 69 LYS 70 ILE 71 THR 72 GLN 73 SER 74 ASN 75 ALA 76 ILE 77 LEU 78 ARG 79 TYR 80 ILE 81 ALA 82 ARG 83 LYS 84 HIS 85 ASN 86 LEU 87 CYS 88 GLY 89 GLU 90 SER 91 GLU 92 LYS 93 GLU 94 GLN 95 ILE 96 ARG 97 GLU 98 ASP 99 ILE 100 LEU 101 GLU 102 ASN 103 GLN 104 PHE 105 MET 106 ASP 107 SER 108 ARG 109 MET 110 GLN 111 LEU 112 ALA 113 LYS 114 LEU 115 CYS 116 TYR 117 ASP 118 PRO 119 ASP 120 PHE 121 GLU 122 LYS 123 LEU 124 LYS 125 PRO 126 GLU 127 TYR 128 LEU 129 GLN 130 ALA 131 LEU 132 PRO 133 GLU 134 MET 135 LEU 136 LYS 137 LEU 138 TYR 139 SER 140 GLN 141 PHE 142 LEU 143 GLY 144 LYS 145 GLN 146 PRO 147 TRP 148 PHE 149 LEU 150 GLY 151 ASP 152 LYS 153 ILE 154 THR 155 PHE 156 VAL 157 ASP 158 PHE 159 ILE 160 ALA 161 TYR 162 ASP 163 VAL 164 LEU 165 GLU 166 ARG 167 ASN 168 GLN 169 VAL 170 PHE 171 GLU 172 PRO 173 SER 174 CYS 175 LEU 176 ASP 177 ALA 178 PHE 179 PRO 180 ASN 181 LEU 182 LYS 183 ASP 184 PHE 185 ILE 186 SER 187 ARG 188 PHE 189 GLU 190 GLY 191 LEU 192 GLU 193 LYS 194 ILE 195 SER 196 ALA 197 TYR 198 MET 199 LYS 200 SER 201 SER 202 ARG 203 PHE 204 LEU 205 PRO 206 ARG 207 PRO 208 VAL 209 PHE 210 THR 211 LYS 212 MET 213 ALA 214 VAL 215 TRP 216 GLY 217 ASN 218 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 PDB 1HNA "Crystal Structure Of Human Class Mu Glutathione Transferase Gstm2-2: Effects Of Lattice Packing On Conformational Heterogeneity" 99.54 217 99.54 100.00 1.48e-157 PDB 1HNB "Crystal Structure Of Human Class Mu Glutathione Transferase Gstm2-2: Effects Of Lattice Packing On Conformational Heterogeneity" 99.54 217 99.54 100.00 1.48e-157 PDB 1HNC "Crystal Structure Of Human Class Mu Glutathione Transferase Gstm2-2: Effects Of Lattice Packing On Conformational Heterogeneity" 99.54 217 99.54 100.00 1.48e-157 PDB 1XW5 "Human Glutathione S-transferase M2-2 (e.c.2.5.1.18) Complexed With Glutathione, Monoclinic Crystal Form" 99.54 217 100.00 100.00 1.07e-158 PDB 1YKC "Human Glutathione S-transferase M2-2 (e.c.2.5.1.18) Complexed With Glutathione-disulfide" 99.54 217 100.00 100.00 1.07e-158 PDB 2AB6 "Human Glutathione S-Transferase M2-2 (E.C.2.5.1.18) Complexed With S-Methylglutathione" 99.54 217 100.00 100.00 1.07e-158 PDB 2C4J "Human Glutathione-S-Transferase M2-2 T210s Mutant In Complex With Glutathione-Styrene Oxide Conjugate" 100.00 218 99.54 100.00 3.89e-159 PDB 2GTU "Ligand-Free Human Glutathione S-Transferase M2-2 (E.C.2.5.1.18), Monoclinic Crystal Form" 99.54 217 100.00 100.00 1.07e-158 PDB 3GTU "Ligand-Free Heterodimeric Human Glutathione S-Transferase M2-3 (Ec 2.5.1.18), Monoclinic Crystal Form" 99.54 217 100.00 100.00 1.07e-158 PDB 3GUR "Crystal Structure Of Mu Class Glutathione S-Transferase (Gstm2-2) In Complex With Glutathione And 6-(7-Nitro-2,1,3-Benzoxadiazo" 99.54 217 100.00 100.00 1.07e-158 DBJ BAG61446 "unnamed protein product [Homo sapiens]" 86.70 191 99.47 99.47 1.58e-135 GB AAA60963 "glutathione transferase [Homo sapiens]" 100.00 218 100.00 100.00 1.10e-159 GB AAI05039 "Glutathione S-transferase mu 2 (muscle) [Homo sapiens]" 100.00 218 100.00 100.00 1.10e-159 GB AAI05067 "Glutathione S-transferase mu 2 (muscle) [Homo sapiens]" 100.00 218 100.00 100.00 1.10e-159 GB AAI10381 "Glutathione S-transferase mu 2 (muscle) [Homo sapiens]" 100.00 218 99.54 99.54 1.53e-158 GB AAV38746 "glutathione S-transferase M2 (muscle) [synthetic construct]" 100.00 219 100.00 100.00 1.56e-159 REF NP_000839 "glutathione S-transferase Mu 2 isoform 1 [Homo sapiens]" 100.00 218 100.00 100.00 1.10e-159 REF NP_001135840 "glutathione S-transferase Mu 2 isoform 2 [Homo sapiens]" 86.70 191 100.00 100.00 2.43e-136 REF XP_004026326 "PREDICTED: glutathione S-transferase Mu 2 isoform 1 [Gorilla gorilla gorilla]" 100.00 218 98.62 99.54 1.49e-157 REF XP_004026327 "PREDICTED: glutathione S-transferase Mu 2 isoform 2 [Gorilla gorilla gorilla]" 100.00 218 97.71 99.08 1.06e-155 REF XP_009428156 "PREDICTED: glutathione S-transferase Mu 2 isoform X1 [Pan troglodytes]" 72.94 174 97.48 97.48 1.31e-106 SP P28161 "RecName: Full=Glutathione S-transferase Mu 2; AltName: Full=GST class-mu 2; AltName: Full=GSTM2-2" 100.00 218 100.00 100.00 1.10e-159 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Tissue $glutathione_transferase human 9606 Eukaryota Metazoa Homo sapiens generic muscle 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 $glutathione_transferase 'not available' . Escherichia coli N4830 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label HOD H . . ppm 4.8 . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'glutathione transferase' _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 . 7 TYR HE1 H 6.73 . 1 2 . 7 TYR HE2 H 6.73 . 1 3 . 23 TYR HE1 H 6.75 . 1 4 . 23 TYR HE2 H 6.75 . 1 5 . 28 TYR HE1 H 6.6 . 1 6 . 28 TYR HE2 H 6.6 . 1 7 . 33 TYR HE1 H 6.62 . 1 8 . 33 TYR HE2 H 6.62 . 1 9 . 41 TYR HE1 H 6.68 . 1 10 . 41 TYR HE2 H 6.68 . 1 11 . 116 TYR HE1 H 6.33 . 1 12 . 116 TYR HE2 H 6.33 . 1 13 . 127 TYR HE1 H 6.45 . 1 14 . 127 TYR HE2 H 6.45 . 1 15 . 138 TYR HE1 H 5.68 . 1 16 . 138 TYR HE2 H 5.68 . 1 17 . 197 TYR HE1 H 6.82 . 1 18 . 197 TYR HE2 H 6.82 . 1 stop_ save_