data_4991 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Identification of a novel archaebacterial thioredoxin: Determination of function through structure. ; _BMRB_accession_number 4991 _BMRB_flat_file_name bmr4991.str _Entry_type original _Submission_date 2001-04-17 _Accession_date 2001-04-18 _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 Bhattacharyya Sudeepa . . 2 Habibi-Nazhad Bahram . . 3 Amegbey Godwin . . 4 Slupsky Carolyn M. . 5 Yee Adelinda . . 6 Arrowsmith Cheryl . . 7 Wishart David S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 382 "13C chemical shifts" 144 "15N chemical shifts" 78 "coupling constants" 57 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification of a Novel Archaebacterial Thioredoxin: Determination of Function through Structure ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21937742 _PubMed_ID 11939770 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhattacharyya Sudeepa . . 2 Habibi-Nazhad Bahram . . 3 Amegbey Godwin . . 4 Slupsky Carolyn M. . 5 Yee Adelinda . . 6 Arrowsmith Cheryl . . 7 Wishart David S. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 15 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4760 _Page_last 4770 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_MtH895 _Saveframe_category molecular_system _Mol_system_name 'thioredoxin like protein' _Abbreviation_common MtH895 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MtH895 $MtH895 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'catalyse cellular redox reactions' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MtH895 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'thioredoxin from Methanobacterium thermoautotrophicum delta H' _Abbreviation_common MtH895 _Molecular_mass 8500 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 77 _Mol_residue_sequence ; MMKIQIYGTGCANCQMLEKN AREAVKELGIDAEFEKIKEM DQILEAGLTALPGLAVDGEL KIMGRVASKEEIKKILS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 MET 3 LYS 4 ILE 5 GLN 6 ILE 7 TYR 8 GLY 9 THR 10 GLY 11 CYS 12 ALA 13 ASN 14 CYS 15 GLN 16 MET 17 LEU 18 GLU 19 LYS 20 ASN 21 ALA 22 ARG 23 GLU 24 ALA 25 VAL 26 LYS 27 GLU 28 LEU 29 GLY 30 ILE 31 ASP 32 ALA 33 GLU 34 PHE 35 GLU 36 LYS 37 ILE 38 LYS 39 GLU 40 MET 41 ASP 42 GLN 43 ILE 44 LEU 45 GLU 46 ALA 47 GLY 48 LEU 49 THR 50 ALA 51 LEU 52 PRO 53 GLY 54 LEU 55 ALA 56 VAL 57 ASP 58 GLY 59 GLU 60 LEU 61 LYS 62 ILE 63 MET 64 GLY 65 ARG 66 VAL 67 ALA 68 SER 69 LYS 70 GLU 71 GLU 72 ILE 73 LYS 74 LYS 75 ILE 76 LEU 77 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-21 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 1ILO "Nmr Structure Of A Thioredoxin, Mth895, From The Archeon Methanobacterium Thermoautotrophicum Strain Delta H." 100.00 77 100.00 100.00 1.86e-45 DBJ BAM70061 "conserved hypothetical protein [Methanothermobacter thermautotrophicus CaT2]" 98.70 76 98.68 98.68 1.87e-43 GB AAB85393 "conserved protein [Methanothermobacter thermautotrophicus str. Delta H]" 100.00 77 100.00 100.00 1.86e-45 REF NP_276032 "hypothetical protein MTH895 [Methanothermobacter thermautotrophicus str. Delta H]" 100.00 77 100.00 100.00 1.86e-45 REF WP_010876528 "hypothetical protein [Methanothermobacter thermautotrophicus]" 100.00 77 100.00 100.00 1.86e-45 SP O26981 "RecName: Full=Thioredoxin [Methanothermobacter thermautotrophicus str. Delta H]" 100.00 77 100.00 100.00 1.86e-45 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 $MtH895 'Methanothermobacter thermautotrophicus' 145262 Archaea Euryarchaeota Methanothermobacter thermautotrophicus 'delta H' 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 $MtH895 'recombinant technology' . . . . . 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 $MtH895 1.0 mM '[U-13C; U-15N]' stop_ 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_ ####################### # Sample conditions # ####################### save_NMR-condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.20 0.02 M pH 7.0 0.3 n/a temperature 298 2 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $NMR-condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MtH895 _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 MET H H 8.18 0.05 1 2 . 1 MET HA H 4.43 0.05 1 3 . 1 MET HB2 H 1.87 0.05 1 4 . 1 MET HB3 H 1.87 0.05 1 5 . 1 MET HG2 H 2.34 0.05 2 6 . 1 MET HG3 H 2.26 0.05 2 7 . 1 MET CA C 55.10 0.05 1 8 . 1 MET CB C 33.29 0.05 1 9 . 1 MET N N 123.41 0.05 1 10 . 2 MET H H 8.17 0.05 1 11 . 2 MET HA H 4.56 0.05 1 12 . 2 MET HB2 H 2.00 0.05 2 13 . 2 MET HB3 H 1.85 0.05 2 14 . 2 MET HG2 H 2.41 0.05 2 15 . 2 MET HG3 H 2.16 0.05 2 16 . 2 MET CA C 56.06 0.05 1 17 . 2 MET CB C 35.10 0.05 1 18 . 2 MET N N 125.47 0.05 1 19 . 3 LYS H H 8.85 0.05 1 20 . 3 LYS HA H 4.85 0.05 1 21 . 3 LYS HB2 H 1.69 0.05 2 22 . 3 LYS HB3 H 1.58 0.05 2 23 . 3 LYS HG2 H 1.29 0.05 2 24 . 3 LYS HG3 H 1.17 0.05 2 25 . 3 LYS HE2 H 2.80 0.05 1 26 . 3 LYS CA C 54.52 0.05 1 27 . 3 LYS CB C 33.95 0.05 1 28 . 3 LYS N N 125.73 0.05 1 29 . 4 ILE H H 8.73 0.05 1 30 . 4 ILE HA H 4.66 0.05 1 31 . 4 ILE HB H 0.92 0.05 1 32 . 4 ILE HG12 H 0.70 0.05 2 33 . 4 ILE HD1 H 0.43 0.05 1 34 . 4 ILE CA C 59.73 0.05 1 35 . 4 ILE CB C 38.47 0.05 1 36 . 4 ILE N N 126.88 0.05 1 37 . 5 GLN H H 8.62 0.05 1 38 . 5 GLN HA H 5.05 0.05 1 39 . 5 GLN HB2 H 1.93 0.05 2 40 . 5 GLN HB3 H 1.14 0.05 2 41 . 5 GLN HG2 H 2.27 0.05 2 42 . 5 GLN HG3 H 2.07 0.05 2 43 . 5 GLN HE21 H 7.55 0.05 2 44 . 5 GLN HE22 H 6.22 0.05 2 45 . 5 GLN CA C 54.92 0.05 1 46 . 5 GLN CB C 31.07 0.05 1 47 . 5 GLN N N 125.91 0.05 1 48 . 5 GLN NE2 N 111.17 0.05 1 49 . 6 ILE H H 8.71 0.05 1 50 . 6 ILE HA H 4.94 0.05 1 51 . 6 ILE HB H 1.90 0.05 1 52 . 6 ILE HG12 H 1.46 0.05 2 53 . 6 ILE HG13 H 1.45 0.05 2 54 . 6 ILE HG2 H 0.93 0.05 1 55 . 6 ILE CA C 58.49 0.05 1 56 . 6 ILE CB C 38.62 0.05 1 57 . 6 ILE N N 122.25 0.05 1 58 . 7 TYR H H 9.32 0.05 1 59 . 7 TYR HA H 5.27 0.05 1 60 . 7 TYR HB2 H 2.62 0.05 1 61 . 7 TYR HB3 H 2.50 0.05 1 62 . 7 TYR HD1 H 6.72 0.05 1 63 . 7 TYR HD2 H 6.72 0.05 1 64 . 7 TYR HE1 H 6.55 0.05 1 65 . 7 TYR HE2 H 6.55 0.05 1 66 . 7 TYR CA C 56.49 0.05 1 67 . 7 TYR CB C 42.03 0.05 1 68 . 7 TYR N N 128.52 0.05 1 69 . 8 GLY H H 8.37 0.05 1 70 . 8 GLY HA2 H 5.00 0.05 2 71 . 8 GLY HA3 H 3.90 0.05 2 72 . 8 GLY CA C 45.71 0.05 1 73 . 8 GLY N N 106.40 0.05 1 74 . 9 THR H H 8.99 0.05 1 75 . 9 THR HA H 4.64 0.05 1 76 . 9 THR HB H 4.46 0.05 1 77 . 9 THR HG2 H 1.18 0.05 1 78 . 9 THR CA C 62.12 0.05 1 79 . 9 THR CB C 69.15 0.05 1 80 . 9 THR N N 108.87 0.05 1 81 . 10 GLY HA2 H 4.28 0.05 2 82 . 10 GLY HA3 H 3.87 0.05 2 83 . 10 GLY CA C 45.74 0.05 1 84 . 11 CYS H H 7.35 0.05 1 85 . 11 CYS HA H 4.67 0.05 1 86 . 11 CYS HB2 H 3.41 0.05 2 87 . 11 CYS HB3 H 2.93 0.05 2 88 . 11 CYS N N 114.50 0.05 1 89 . 12 ALA HA H 4.55 0.05 1 90 . 12 ALA HB H 0.82 0.05 1 91 . 12 ALA CA C 51.72 0.05 1 92 . 12 ALA CB C 22.20 0.05 1 93 . 13 ASN H H 8.77 0.05 1 94 . 13 ASN HA H 4.53 0.05 1 95 . 13 ASN HB2 H 3.11 0.05 1 96 . 13 ASN HB3 H 2.23 0.05 1 97 . 13 ASN HD21 H 7.78 0.05 2 98 . 13 ASN HD22 H 7.06 0.05 2 99 . 13 ASN CA C 55.90 0.05 1 100 . 13 ASN CB C 37.49 0.05 1 101 . 13 ASN N N 118.50 0.05 1 102 . 13 ASN ND2 N 112.84 0.05 1 103 . 14 CYS H H 9.01 0.05 1 104 . 14 CYS HA H 3.82 0.05 1 105 . 14 CYS HB2 H 3.37 0.05 1 106 . 14 CYS HB3 H 3.05 0.05 1 107 . 14 CYS CA C 63.99 0.05 1 108 . 14 CYS CB C 27.07 0.05 1 109 . 14 CYS N N 125.95 0.05 1 110 . 15 GLN H H 8.40 0.05 1 111 . 15 GLN HA H 4.06 0.05 1 112 . 15 GLN HB2 H 2.06 0.05 2 113 . 15 GLN HB3 H 2.00 0.05 2 114 . 15 GLN HG2 H 2.34 0.05 2 115 . 15 GLN HG3 H 2.33 0.05 2 116 . 15 GLN HE21 H 7.21 0.05 2 117 . 15 GLN HE22 H 6.82 0.05 2 118 . 15 GLN CA C 58.97 0.05 1 119 . 15 GLN CB C 28.57 0.05 1 120 . 15 GLN N N 118.87 0.05 1 121 . 15 GLN NE2 N 111.70 0.05 1 122 . 16 MET H H 8.07 0.05 1 123 . 16 MET HA H 4.24 0.05 1 124 . 16 MET HB2 H 2.08 0.05 2 125 . 16 MET HB3 H 1.94 0.05 2 126 . 16 MET HG2 H 2.63 0.05 2 127 . 16 MET HG3 H 2.22 0.05 2 128 . 16 MET CA C 58.26 0.05 1 129 . 16 MET CB C 32.81 0.05 1 130 . 16 MET N N 120.48 0.05 1 131 . 17 LEU H H 8.18 0.05 1 132 . 17 LEU HA H 4.05 0.05 1 133 . 17 LEU HB2 H 2.07 0.05 1 134 . 17 LEU HB3 H 1.55 0.05 1 135 . 17 LEU HG H 1.16 0.05 1 136 . 17 LEU CA C 58.26 0.05 1 137 . 17 LEU CB C 42.33 0.05 1 138 . 17 LEU N N 119.70 0.05 1 139 . 18 GLU H H 8.14 0.05 1 140 . 18 GLU HA H 3.68 0.05 1 141 . 18 GLU HB2 H 2.07 0.05 2 142 . 18 GLU HB3 H 1.97 0.05 2 143 . 18 GLU CA C 60.06 0.05 1 144 . 18 GLU CB C 29.28 0.05 1 145 . 18 GLU N N 117.32 0.05 1 146 . 19 LYS H H 8.08 0.05 1 147 . 19 LYS HA H 3.83 0.05 1 148 . 19 LYS HB2 H 1.93 0.05 2 149 . 19 LYS HB3 H 1.89 0.05 2 150 . 19 LYS HG2 H 1.47 0.05 2 151 . 19 LYS HG3 H 1.34 0.05 2 152 . 19 LYS HD2 H 1.67 0.05 2 153 . 19 LYS HD3 H 1.65 0.05 2 154 . 19 LYS CA C 58.19 0.05 1 155 . 19 LYS CB C 32.43 0.05 1 156 . 19 LYS N N 120.30 0.05 1 157 . 20 ASN H H 8.48 0.05 1 158 . 20 ASN HA H 4.32 0.05 1 159 . 20 ASN HB2 H 2.91 0.05 1 160 . 20 ASN HB3 H 2.33 0.05 1 161 . 20 ASN HD21 H 7.80 0.05 1 162 . 20 ASN HD22 H 6.84 0.05 1 163 . 20 ASN CA C 55.54 0.05 1 164 . 20 ASN CB C 37.29 0.05 1 165 . 20 ASN N N 118.48 0.05 1 166 . 20 ASN ND2 N 109.23 0.05 1 167 . 21 ALA H H 8.49 0.05 1 168 . 21 ALA HA H 4.14 0.05 1 169 . 21 ALA HB H 1.57 0.05 1 170 . 21 ALA CA C 55.37 0.05 1 171 . 21 ALA CB C 18.50 0.05 1 172 . 21 ALA N N 122.58 0.05 1 173 . 22 ARG H H 8.85 0.05 1 174 . 22 ARG HA H 3.93 0.05 1 175 . 22 ARG HB2 H 1.77 0.05 2 176 . 22 ARG HB3 H 1.55 0.05 2 177 . 22 ARG HD2 H 0.64 0.05 4 178 . 22 ARG CA C 60.05 0.05 1 179 . 22 ARG CB C 29.75 0.05 1 180 . 22 ARG N N 118.82 0.05 1 181 . 23 GLU H H 8.37 0.05 1 182 . 23 GLU HA H 4.04 0.05 1 183 . 23 GLU HB2 H 2.12 0.05 2 184 . 23 GLU HB3 H 1.98 0.05 2 185 . 23 GLU HG2 H 2.54 0.05 2 186 . 23 GLU HG3 H 2.27 0.05 2 187 . 23 GLU CA C 59.52 0.05 1 188 . 23 GLU CB C 29.91 0.05 1 189 . 23 GLU N N 120.08 0.05 1 190 . 24 ALA H H 8.17 0.05 1 191 . 24 ALA HA H 3.72 0.05 1 192 . 24 ALA HB H 1.51 0.05 1 193 . 24 ALA CA C 55.85 0.05 1 194 . 24 ALA CB C 19.39 0.05 1 195 . 24 ALA N N 121.70 0.05 1 196 . 25 VAL H H 8.07 0.05 1 197 . 25 VAL HA H 3.50 0.05 1 198 . 25 VAL HB H 2.39 0.05 1 199 . 25 VAL HG1 H 1.06 0.05 2 200 . 25 VAL HG2 H 1.07 0.05 2 201 . 25 VAL CA C 66.86 0.05 1 202 . 25 VAL CB C 31.92 0.05 1 203 . 25 VAL N N 114.86 0.05 1 204 . 26 LYS H H 7.79 0.05 1 205 . 26 LYS HA H 4.19 0.05 1 206 . 26 LYS HB2 H 2.01 0.05 1 207 . 26 LYS HG2 H 1.55 0.05 2 208 . 26 LYS HG3 H 1.42 0.05 2 209 . 26 LYS HD2 H 1.72 0.05 1 210 . 26 LYS HD3 H 1.72 0.05 1 211 . 26 LYS HE2 H 2.98 0.05 2 212 . 26 LYS CA C 59.17 0.05 1 213 . 26 LYS CB C 32.39 0.05 1 214 . 26 LYS N N 120.33 0.05 1 215 . 27 GLU H H 8.22 0.05 1 216 . 27 GLU HA H 4.01 0.05 1 217 . 27 GLU HB2 H 1.98 0.05 1 218 . 27 GLU HG2 H 2.68 0.05 1 219 . 27 GLU HG3 H 2.23 0.05 1 220 . 27 GLU CA C 59.28 0.05 1 221 . 27 GLU CB C 29.61 0.05 1 222 . 27 GLU N N 118.86 0.05 1 223 . 28 LEU H H 7.89 0.05 1 224 . 28 LEU HA H 4.31 0.05 1 225 . 28 LEU HB2 H 1.82 0.05 2 226 . 28 LEU HG H 1.55 0.05 2 227 . 28 LEU HD1 H 0.89 0.05 2 228 . 28 LEU CA C 55.48 0.05 1 229 . 28 LEU CB C 43.76 0.05 1 230 . 28 LEU N N 116.97 0.05 1 231 . 29 GLY H H 7.94 0.05 1 232 . 29 GLY HA2 H 3.96 0.05 2 233 . 29 GLY HA3 H 3.93 0.05 2 234 . 29 GLY CA C 46.45 0.05 1 235 . 29 GLY N N 108.64 0.05 1 236 . 30 ILE H H 7.23 0.05 1 237 . 30 ILE HA H 4.26 0.05 1 238 . 30 ILE HB H 1.78 0.05 1 239 . 30 ILE HG12 H 1.41 0.05 2 240 . 30 ILE HG13 H 0.89 0.05 2 241 . 30 ILE HG2 H 1.02 0.05 1 242 . 30 ILE CA C 60.24 0.05 1 243 . 30 ILE CB C 40.99 0.05 1 244 . 30 ILE N N 116.07 0.05 1 245 . 31 ASP H H 8.44 0.05 1 246 . 31 ASP HA H 4.79 0.05 1 247 . 31 ASP HB2 H 2.67 0.05 2 248 . 31 ASP HB3 H 2.56 0.05 2 249 . 31 ASP CA C 53.67 0.05 1 250 . 31 ASP CB C 41.50 0.05 1 251 . 31 ASP N N 124.62 0.05 1 252 . 32 ALA H H 8.07 0.05 1 253 . 32 ALA HA H 5.07 0.05 1 254 . 32 ALA HB H 0.94 0.05 1 255 . 32 ALA CA C 50.69 0.05 1 256 . 32 ALA CB C 23.11 0.05 1 257 . 32 ALA N N 124.68 0.05 1 258 . 33 GLU H H 8.50 0.05 1 259 . 33 GLU HA H 4.61 0.05 1 260 . 33 GLU HB2 H 1.83 0.05 1 261 . 33 GLU HG2 H 2.23 0.05 1 262 . 33 GLU HG3 H 2.07 0.05 1 263 . 33 GLU CA C 54.44 0.05 1 264 . 33 GLU CB C 32.63 0.05 1 265 . 33 GLU N N 120.83 0.05 1 266 . 34 PHE H H 8.85 0.05 1 267 . 34 PHE HA H 5.23 0.05 1 268 . 34 PHE HB2 H 2.96 0.05 3 269 . 34 PHE HB3 H 2.55 0.05 3 270 . 34 PHE HD1 H 7.08 0.05 1 271 . 34 PHE HD2 H 7.08 0.05 1 272 . 34 PHE HE1 H 7.14 0.05 1 273 . 34 PHE HE2 H 7.14 0.05 1 274 . 34 PHE HZ H 6.92 0.05 1 275 . 34 PHE CA C 57.32 0.05 1 276 . 34 PHE CB C 41.95 0.05 1 277 . 34 PHE N N 122.56 0.05 1 278 . 35 GLU H H 9.08 0.05 1 279 . 35 GLU HA H 4.59 0.05 1 280 . 35 GLU HB2 H 1.82 0.05 2 281 . 35 GLU HB3 H 1.80 0.05 2 282 . 35 GLU HG2 H 2.09 0.05 1 283 . 35 GLU HG3 H 1.96 0.05 1 284 . 35 GLU CA C 54.82 0.05 1 285 . 35 GLU CB C 33.58 0.05 1 286 . 35 GLU N N 124.20 0.05 1 287 . 36 LYS H H 8.80 0.05 1 288 . 36 LYS HA H 4.83 0.05 1 289 . 36 LYS HB2 H 1.67 0.05 2 290 . 36 LYS HG2 H 1.33 0.05 2 291 . 36 LYS HE2 H 2.87 0.05 1 292 . 36 LYS CA C 55.52 0.05 1 293 . 36 LYS CB C 32.26 0.05 1 294 . 36 LYS N N 125.84 0.05 1 295 . 37 ILE H H 8.54 0.05 1 296 . 37 ILE HA H 4.23 0.05 1 297 . 37 ILE HB H 1.38 0.05 1 298 . 37 ILE HG12 H 0.89 0.05 2 299 . 37 ILE HD1 H 0.35 0.05 1 300 . 37 ILE CA C 61.26 0.05 1 301 . 37 ILE CB C 37.85 0.05 1 302 . 37 ILE N N 127.75 0.05 1 303 . 38 LYS H H 8.32 0.05 1 304 . 38 LYS HA H 5.19 0.05 1 305 . 38 LYS HB2 H 1.77 0.05 1 306 . 38 LYS HB3 H 1.74 0.05 1 307 . 38 LYS HG2 H 1.26 0.05 2 308 . 38 LYS HE2 H 2.91 0.05 2 309 . 38 LYS CA C 55.18 0.05 1 310 . 38 LYS CB C 35.24 0.05 1 311 . 38 LYS N N 123.69 0.05 1 312 . 39 GLU H H 7.48 0.05 1 313 . 39 GLU HA H 3.68 0.05 1 314 . 39 GLU HB2 H 1.96 0.05 1 315 . 39 GLU HG2 H 2.42 0.05 2 316 . 39 GLU HG3 H 2.23 0.05 2 317 . 39 GLU CA C 57.47 0.05 1 318 . 39 GLU CB C 30.77 0.05 1 319 . 39 GLU N N 119.78 0.05 1 320 . 40 MET HA H 4.34 0.05 1 321 . 40 MET CA C 57.47 0.05 1 322 . 40 MET CB C 30.77 0.05 1 323 . 41 ASP H H 9.02 0.05 1 324 . 41 ASP HA H 4.30 0.05 1 325 . 41 ASP HB2 H 2.68 0.05 1 326 . 41 ASP HB3 H 2.62 0.05 1 327 . 41 ASP CA C 57.47 0.05 1 328 . 41 ASP CB C 39.34 0.05 1 329 . 41 ASP N N 117.05 0.05 1 330 . 42 GLN H H 7.19 0.05 1 331 . 42 GLN HA H 4.13 0.05 1 332 . 42 GLN HB2 H 2.12 0.05 2 333 . 42 GLN HB3 H 2.11 0.05 2 334 . 42 GLN HG2 H 2.44 0.05 2 335 . 42 GLN HG3 H 2.41 0.05 2 336 . 42 GLN HE21 H 7.74 0.05 1 337 . 42 GLN HE22 H 6.88 0.05 1 338 . 42 GLN CA C 58.44 0.05 1 339 . 42 GLN CB C 29.71 0.05 1 340 . 42 GLN N N 119.19 0.05 1 341 . 42 GLN NE2 N 112.82 0.05 1 342 . 43 ILE H H 8.07 0.05 1 343 . 43 ILE HA H 3.52 0.05 1 344 . 43 ILE HB H 2.12 0.05 1 345 . 43 ILE HG12 H 0.97 0.05 2 346 . 43 ILE HG13 H 0.96 0.05 2 347 . 43 ILE HD1 H 0.86 0.05 4 348 . 43 ILE CA C 66.27 0.05 1 349 . 43 ILE CB C 38.50 0.05 1 350 . 43 ILE N N 118.18 0.05 1 351 . 44 LEU H H 8.41 0.05 1 352 . 44 LEU HA H 4.09 0.05 1 353 . 44 LEU HB2 H 1.80 0.05 1 354 . 44 LEU HB3 H 1.47 0.05 1 355 . 44 LEU HG H 0.85 0.05 1 356 . 44 LEU CA C 57.68 0.05 1 357 . 44 LEU CB C 41.31 0.05 1 358 . 44 LEU N N 118.18 0.05 1 359 . 45 GLU H H 7.91 0.05 1 360 . 45 GLU HA H 3.99 0.05 1 361 . 45 GLU HB2 H 2.15 0.05 1 362 . 45 GLU HB3 H 2.06 0.05 1 363 . 45 GLU HG2 H 2.39 0.05 1 364 . 45 GLU HG3 H 2.28 0.05 1 365 . 45 GLU CA C 59.01 0.05 1 366 . 45 GLU CB C 29.53 0.05 1 367 . 45 GLU N N 121.46 0.05 1 368 . 46 ALA H H 7.37 0.05 1 369 . 46 ALA HA H 4.25 0.05 1 370 . 46 ALA HB H 1.32 0.05 1 371 . 46 ALA CA C 52.64 0.05 1 372 . 46 ALA CB C 18.98 0.05 1 373 . 46 ALA N N 119.26 0.05 1 374 . 47 GLY H H 7.67 0.05 1 375 . 47 GLY HA2 H 4.02 0.05 1 376 . 47 GLY HA3 H 3.64 0.05 1 377 . 47 GLY CA C 45.23 0.05 1 378 . 47 GLY N N 104.24 0.05 1 379 . 48 LEU H H 6.91 0.05 1 380 . 48 LEU HA H 4.25 0.05 1 381 . 48 LEU HB2 H 1.50 0.05 1 382 . 48 LEU HB3 H 1.38 0.05 1 383 . 48 LEU HG H 0.41 0.05 1 384 . 48 LEU CA C 56.80 0.05 1 385 . 48 LEU CB C 41.52 0.05 1 386 . 48 LEU N N 120.48 0.05 1 387 . 49 THR H H 7.72 0.05 1 388 . 49 THR HA H 4.26 0.05 1 389 . 49 THR HB H 4.39 0.05 1 390 . 49 THR CA C 61.03 0.05 1 391 . 49 THR CB C 68.97 0.05 1 392 . 49 THR N N 110.40 0.05 1 393 . 50 ALA H H 7.54 0.05 1 394 . 50 ALA HA H 4.39 0.05 1 395 . 50 ALA HB H 1.32 0.05 1 396 . 50 ALA CA C 51.50 0.05 1 397 . 50 ALA CB C 44.68 0.05 1 398 . 50 ALA N N 123.58 0.05 1 399 . 51 LEU H H 8.17 0.05 1 400 . 51 LEU HA H 4.54 0.05 1 401 . 51 LEU HB2 H 1.68 0.05 2 402 . 51 LEU HB3 H 1.39 0.05 2 403 . 51 LEU HG H 1.49 0.05 1 404 . 51 LEU HD1 H 0.95 0.05 2 405 . 51 LEU CB C 44.68 0.05 1 406 . 51 LEU N N 116.95 0.05 1 407 . 52 PRO HA H 4.89 0.05 1 408 . 52 PRO HB2 H 2.30 0.05 1 409 . 52 PRO HB3 H 2.05 0.05 1 410 . 52 PRO HG2 H 1.98 0.05 1 411 . 52 PRO HG3 H 1.91 0.05 1 412 . 52 PRO HD2 H 3.87 0.05 2 413 . 52 PRO HD3 H 3.70 0.05 2 414 . 52 PRO CA C 62.38 0.05 1 415 . 52 PRO CB C 35.99 0.05 1 416 . 53 GLY H H 9.07 0.05 1 417 . 53 GLY HA2 H 5.20 0.05 1 418 . 53 GLY HA3 H 3.71 0.05 1 419 . 53 GLY CA C 45.30 0.05 1 420 . 53 GLY N N 103.96 0.05 1 421 . 54 LEU H H 9.11 0.05 1 422 . 54 LEU HA H 5.79 0.05 1 423 . 54 LEU HB2 H 1.66 0.05 2 424 . 54 LEU HB3 H 1.62 0.05 2 425 . 54 LEU HD1 H 0.81 0.05 4 426 . 54 LEU CA C 54.56 0.05 1 427 . 54 LEU CB C 47.03 0.05 1 428 . 54 LEU N N 122.90 0.05 1 429 . 55 ALA H H 9.84 0.05 1 430 . 55 ALA HA H 5.39 0.05 1 431 . 55 ALA HB H 1.52 0.05 1 432 . 55 ALA CA C 50.49 0.05 1 433 . 55 ALA CB C 24.01 0.05 1 434 . 55 ALA N N 131.69 0.05 1 435 . 56 VAL H H 8.31 0.05 1 436 . 56 VAL HA H 4.57 0.05 1 437 . 56 VAL HB H 1.81 0.05 1 438 . 56 VAL HG1 H 0.89 0.05 1 439 . 56 VAL HG2 H 0.76 0.05 1 440 . 56 VAL CA C 60.13 0.05 1 441 . 56 VAL CB C 34.04 0.05 1 442 . 56 VAL N N 119.12 0.05 1 443 . 57 ASP H H 10.17 0.05 1 444 . 57 ASP HA H 4.44 0.05 1 445 . 57 ASP HB2 H 2.99 0.05 1 446 . 57 ASP HB3 H 2.66 0.05 1 447 . 57 ASP CA C 56.16 0.05 1 448 . 57 ASP CB C 40.05 0.05 1 449 . 57 ASP N N 130.69 0.05 1 450 . 58 GLY H H 8.98 0.05 1 451 . 58 GLY HA2 H 4.20 0.05 2 452 . 58 GLY HA3 H 3.54 0.05 2 453 . 58 GLY CA C 45.31 0.05 1 454 . 58 GLY N N 103.37 0.05 1 455 . 59 GLU H H 7.91 0.05 1 456 . 59 GLU HA H 4.61 0.05 1 457 . 59 GLU HB2 H 2.08 0.05 1 458 . 59 GLU HB3 H 1.98 0.05 1 459 . 59 GLU HG2 H 2.41 0.05 1 460 . 59 GLU HG3 H 2.28 0.05 1 461 . 59 GLU CA C 54.65 0.05 1 462 . 59 GLU CB C 31.08 0.05 1 463 . 59 GLU N N 121.63 0.05 1 464 . 60 LEU H H 8.96 0.05 1 465 . 60 LEU HA H 4.07 0.05 1 466 . 60 LEU HB2 H 1.63 0.05 2 467 . 60 LEU HD1 H 0.78 0.05 2 468 . 60 LEU CA C 56.82 0.05 1 469 . 60 LEU CB C 42.15 0.05 1 470 . 60 LEU N N 129.66 0.05 1 471 . 61 LYS H H 9.08 0.05 1 472 . 61 LYS HA H 4.73 0.05 1 473 . 61 LYS HB2 H 1.91 0.05 1 474 . 61 LYS HB3 H 1.71 0.05 1 475 . 61 LYS CA C 54.90 0.05 1 476 . 61 LYS CB C 35.62 0.05 1 477 . 61 LYS N N 122.44 0.05 1 478 . 62 ILE H H 7.73 0.05 1 479 . 62 ILE HA H 4.35 0.05 1 480 . 62 ILE HB H 1.76 0.05 1 481 . 62 ILE HG12 H 1.32 0.05 1 482 . 62 ILE HG13 H 0.84 0.05 1 483 . 62 ILE HG2 H 1.14 0.05 1 484 . 62 ILE HD1 H 0.72 0.05 1 485 . 62 ILE CA C 59.42 0.05 1 486 . 62 ILE CB C 42.21 0.05 1 487 . 62 ILE N N 117.86 0.05 1 488 . 63 MET H H 8.94 0.05 1 489 . 63 MET HA H 4.98 0.05 1 490 . 63 MET HB2 H 2.13 0.05 1 491 . 63 MET HB3 H 1.94 0.05 1 492 . 63 MET HG2 H 2.46 0.05 2 493 . 63 MET HG3 H 2.27 0.05 2 494 . 63 MET CA C 55.65 0.05 1 495 . 63 MET CB C 36.01 0.05 1 496 . 63 MET N N 125.24 0.05 1 497 . 64 GLY H H 8.79 0.05 1 498 . 64 GLY HA2 H 3.94 0.05 2 499 . 64 GLY HA3 H 3.43 0.05 1 500 . 64 GLY CA C 46.38 0.05 1 501 . 64 GLY N N 111.58 0.05 1 502 . 65 ARG H H 7.17 0.05 1 503 . 65 ARG HA H 4.62 0.05 1 504 . 65 ARG HB2 H 1.83 0.05 2 505 . 65 ARG HB3 H 1.65 0.05 2 506 . 65 ARG HG2 H 1.22 0.05 2 507 . 65 ARG HG3 H 1.03 0.05 2 508 . 65 ARG HD2 H 3.10 0.05 1 509 . 65 ARG CA C 53.88 0.05 1 510 . 65 ARG CB C 32.09 0.05 1 511 . 65 ARG N N 112.57 0.05 1 512 . 66 VAL H H 8.39 0.05 1 513 . 66 VAL HA H 3.74 0.05 1 514 . 66 VAL HB H 1.98 0.05 1 515 . 66 VAL HG1 H 0.98 0.05 1 516 . 66 VAL HG2 H 0.73 0.05 1 517 . 66 VAL CA C 62.22 0.05 1 518 . 66 VAL CB C 31.50 0.05 1 519 . 66 VAL N N 117.34 0.05 1 520 . 67 ALA H H 6.01 0.05 1 521 . 67 ALA HA H 4.49 0.05 1 522 . 67 ALA HB H 1.20 0.05 1 523 . 67 ALA CA C 50.74 0.05 1 524 . 67 ALA CB C 21.41 0.05 1 525 . 67 ALA N N 128.70 0.05 1 526 . 68 SER H H 8.82 0.05 1 527 . 68 SER HA H 4.29 0.05 1 528 . 68 SER HB2 H 4.42 0.05 1 529 . 68 SER CA C 57.27 0.05 1 530 . 68 SER CB C 65.30 0.05 1 531 . 68 SER N N 117.13 0.05 1 532 . 69 LYS H H 9.12 0.05 1 533 . 69 LYS HA H 3.75 0.05 1 534 . 69 LYS HG2 H 1.62 0.05 2 535 . 69 LYS CA C 60.63 0.05 1 536 . 69 LYS CB C 31.54 0.05 1 537 . 69 LYS N N 121.03 0.05 1 538 . 70 GLU H H 8.72 0.05 1 539 . 70 GLU HA H 3.82 0.05 1 540 . 70 GLU HB2 H 1.97 0.05 1 541 . 70 GLU HG2 H 2.42 0.05 1 542 . 70 GLU HG3 H 2.29 0.05 1 543 . 70 GLU CA C 60.40 0.05 1 544 . 70 GLU CB C 29.03 0.05 1 545 . 70 GLU N N 117.40 0.05 1 546 . 71 GLU H H 8.01 0.05 1 547 . 71 GLU HA H 3.93 0.05 1 548 . 71 GLU HB2 H 1.97 0.05 2 549 . 71 GLU HB3 H 1.96 0.05 2 550 . 71 GLU HG2 H 2.41 0.05 1 551 . 71 GLU HG3 H 2.18 0.05 1 552 . 71 GLU CA C 59.49 0.05 1 553 . 71 GLU CB C 29.92 0.05 1 554 . 71 GLU N N 121.14 0.05 1 555 . 72 ILE H H 8.19 0.05 1 556 . 72 ILE HA H 3.50 0.05 1 557 . 72 ILE HB H 1.68 0.05 1 558 . 72 ILE HG2 H 0.75 0.05 1 559 . 72 ILE HD1 H 0.51 0.05 1 560 . 72 ILE CA C 65.39 0.05 1 561 . 72 ILE CB C 37.81 0.05 1 562 . 72 ILE N N 119.50 0.05 1 563 . 73 LYS H H 8.61 0.05 1 564 . 73 LYS HA H 3.73 0.05 1 565 . 73 LYS HB2 H 1.88 0.05 1 566 . 73 LYS HB3 H 1.88 0.05 1 567 . 73 LYS HG2 H 1.23 0.05 2 568 . 73 LYS CA C 60.96 0.05 1 569 . 73 LYS CB C 32.25 0.05 1 570 . 73 LYS N N 118.99 0.05 1 571 . 74 LYS H H 7.36 0.05 1 572 . 74 LYS HA H 4.03 0.05 1 573 . 74 LYS HB2 H 1.96 0.05 1 574 . 74 LYS HB3 H 1.68 0.05 1 575 . 74 LYS HG2 H 1.44 0.05 1 576 . 74 LYS HD2 H 1.57 0.05 1 577 . 74 LYS HE2 H 2.95 0.05 1 578 . 74 LYS CA C 59.14 0.05 1 579 . 74 LYS CB C 32.10 0.05 1 580 . 74 LYS N N 117.43 0.05 1 581 . 75 ILE H H 7.66 0.05 1 582 . 75 ILE HA H 3.92 0.05 1 583 . 75 ILE HB H 2.07 0.05 1 584 . 75 ILE HG12 H 1.23 0.05 1 585 . 75 ILE HG13 H 0.75 0.05 1 586 . 75 ILE HG2 H 0.87 0.05 1 587 . 75 ILE CA C 63.94 0.05 1 588 . 75 ILE CB C 38.45 0.05 1 589 . 75 ILE N N 118.82 0.05 1 590 . 76 LEU H H 7.54 0.05 1 591 . 76 LEU HA H 4.24 0.05 1 592 . 76 LEU HB2 H 1.86 0.05 2 593 . 76 LEU HB3 H 1.84 0.05 2 594 . 76 LEU HG H 1.57 0.05 1 595 . 76 LEU HD1 H 0.74 0.05 2 596 . 76 LEU CA C 55.05 0.05 1 597 . 76 LEU CB C 42.49 0.05 1 598 . 76 LEU N N 118.18 0.05 1 599 . 77 SER H H 7.24 0.05 1 600 . 77 SER HA H 4.29 0.05 1 601 . 77 SER HB2 H 3.89 0.05 2 602 . 77 SER CA C 60.44 0.05 1 603 . 77 SER CB C 65.27 0.05 1 604 . 77 SER N N 119.27 0.05 1 stop_ save_ ######################## # Coupling constants # ######################## save_MtH895_J_values _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $NMR-condition _Spectrometer_frequency_1H 500 _Mol_system_component_name MtH895 _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 1 MET H 1 MET HA 6.9 . . . 2 3JHNHA 2 MET H 2 MET HA 5.7 . . . 3 3JHNHA 3 LYS H 3 LYS HA 8.4 . . . 4 3JHNHA 4 ILE H 4 ILE HA 8.5 . . . 5 3JHNHA 5 GLN H 5 GLN HA 8.5 . . . 6 3JHNHA 6 ILE H 6 ILE HA 8.9 . . . 7 3JHNHA 7 TYR H 7 TYR HA 8.5 . . . 8 3JHNHA 13 ASN H 13 ASN HA 5.4 . . . 9 3JHNHA 14 CYS H 14 CYS HA 4.3 . . . 10 3JHNHA 15 GLN H 15 GLN HA 4.6 . . . 11 3JHNHA 18 GLU H 18 GLU HA 3.6 . . . 12 3JHNHA 20 ASN H 20 ASN HA 3.3 . . . 13 3JHNHA 21 ALA H 21 ALA HA 4.3 . . . 14 3JHNHA 22 ARG H 22 ARG HA 3.9 . . . 15 3JHNHA 23 GLU H 23 GLU HA 4.7 . . . 16 3JHNHA 24 ALA H 24 ALA HA 3.2 . . . 17 3JHNHA 25 VAL H 25 VAL HA 3.8 . . . 18 3JHNHA 26 LYS H 26 LYS HA 4.0 . . . 19 3JHNHA 27 GLU H 27 GLU HA 4.7 . . . 20 3JHNHA 28 LEU H 28 LEU HA 6.3 . . . 21 3JHNHA 30 ILE H 30 ILE HA 8.6 . . . 22 3JHNHA 31 ASP H 31 ASP HA 7.6 . . . 23 3JHNHA 32 ALA H 32 ALA HA 8.5 . . . 24 3JHNHA 33 GLU H 33 GLU HA 9.1 . . . 25 3JHNHA 34 PHE H 34 PHE HA 8.4 . . . 26 3JHNHA 35 GLU H 35 GLU HA 9.1 . . . 27 3JHNHA 36 LYS H 36 LYS HA 8.3 . . . 28 3JHNHA 37 ILE H 37 ILE HA 9.0 . . . 29 3JHNHA 38 LYS H 38 LYS HA 9.7 . . . 30 3JHNHA 39 GLU H 39 GLU HA 6.3 . . . 31 3JHNHA 41 ASP H 41 ASP HA 3.6 . . . 32 3JHNHA 42 GLN H 42 GLN HA 6.3 . . . 33 3JHNHA 43 ILE H 43 ILE HA 4.6 . . . 34 3JHNHA 44 LEU H 44 LEU HA 3.9 . . . 35 3JHNHA 48 LEU H 48 LEU HA 6.1 . . . 36 3JHNHA 49 THR H 49 THR HA 10.4 . . . 37 3JHNHA 50 ALA H 50 ALA HA 6.1 . . . 38 3JHNHA 51 LEU H 51 LEU HA 8.3 . . . 39 3JHNHA 54 LEU H 54 LEU HA 7.9 . . . 40 3JHNHA 55 ALA H 55 ALA HA 8.6 . . . 41 3JHNHA 56 VAL H 56 VAL HA 8.6 . . . 42 3JHNHA 57 ASP H 57 ASP HA 6.5 . . . 43 3JHNHA 60 LEU H 60 LEU HA 3.8 . . . 44 3JHNHA 61 LYS H 61 LYS HA 9.7 . . . 45 3JHNHA 62 ILE H 62 ILE HA 8.2 . . . 46 3JHNHA 63 MET H 63 MET HA 7.9 . . . 47 3JHNHA 65 ARG H 65 ARG HA 6.4 . . . 48 3JHNHA 66 VAL H 66 VAL HA 7.9 . . . 49 3JHNHA 67 ALA H 67 ALA HA 7.1 . . . 50 3JHNHA 68 SER H 68 SER HA 5.3 . . . 51 3JHNHA 69 LYS H 69 LYS HA 3.1 . . . 52 3JHNHA 70 GLU H 70 GLU HA 3.6 . . . 53 3JHNHA 73 LYS H 73 LYS HA 3.1 . . . 54 3JHNHA 74 LYS H 74 LYS HA 5.1 . . . 55 3JHNHA 75 ILE H 75 ILE HA 5.4 . . . 56 3JHNHA 76 LEU H 76 LEU HA 7.1 . . . 57 3JHNHA 77 SER H 77 SER HA 7.3 . . . stop_ save_