data_4042 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific Assignment of the 1H and 15N Nuclear Magnetic Resonance Spectra of the Reduced Recombinant High-potential Iron-sulfur Protein I from Ectothiorhodospira halophila ; _BMRB_accession_number 4042 _BMRB_flat_file_name bmr4042.str _Entry_type update _Submission_date 1997-07-02 _Accession_date 1997-07-02 _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 Bertini Ivano . . 2 Felli Isabella Caterina . 3 Kastrau Dieter H.W. . 4 Luchinat Claudio . . 5 Piccioli Mario . . 6 Viezzoli Maria Silvia . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 373 "15N chemical shifts" 66 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-10 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Bertini, I., Felli, I. C., Kastrau, D. H.W., Luchinat, C., Piccioli, M., and Viezzoli, M. S., "Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high potential iron-sulfur protein I from Ectothiorhodospira halophila," European Journal of Biochemistry 225, 703-714 (1994). ; _Citation_title ; Sequence-specific assignment of the 1H and 15N Nuclear Magnetic Resonance Spectra of the Reduced Recombinant High-potential Iron-sulfur Protein I from Ectothiorhodospira halophila ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 95045521 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini Ivano . . 2 Felli Isabella Caterina . 3 Kastrau Dieter H.W. . 4 Luchinat Claudio . . 5 Piccioli Mario . . 6 Viezzoli Maria Silvia . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European Journal of Biochemistry' _Journal_volume 225 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 703 _Page_last 714 _Year 1994 _Details . loop_ _Keyword 'Ectothiorhodospira halophila' '[Fe4S4]2+ cluster' 'HiPIP (high-potential iron-sulfur protein) I' NMR 'Nuclear Magnetic Resonance' stop_ save_ ################################## # Molecular system description # ################################## save_HiPIP_I _Saveframe_category molecular_system _Mol_system_name 'high-potential iron-sulfur protein I' _Abbreviation_common HiPIP_I _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'high-potential iron-sulfur protein I' $HiPIP_I_peptide iron-sulfur_center $entity_SF4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HiPIP_I_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'high-potential iron-sulfur protein I' _Abbreviation_common HiPIP_I _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; ASEPRAEDGHAHDYVNEAAD ASGHPRYQEGQLCENCAFWG EAVQDGWGRCTHPDFDEVLV KAEGWCSVYAPAS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 SER 3 3 GLU 4 4 PRO 5 5 ARG 6 6 ALA 7 7 GLU 8 8 ASP 9 9 GLY 10 10 HIS 11 11 ALA 12 12 HIS 13 13 ASP 14 14 TYR 15 15 VAL 16 16 ASN 17 17 GLU 18 18 ALA 19 19 ALA 20 20 ASP 21 21 ALA 22 22 SER 23 23 GLY 24 24 HIS 25 25 PRO 26 26 ARG 27 27 TYR 28 28 GLN 29 29 GLU 30 30 GLY 31 31 GLN 32 32 LEU 33 33 CYS 34 34 GLU 35 35 ASN 36 36 CYS 37 37 ALA 38 38 PHE 39 39 TRP 40 40 GLY 41 41 GLU 42 42 ALA 43 43 VAL 44 44 GLN 45 45 ASP 46 46 GLY 47 47 TRP 48 48 GLY 49 49 ARG 50 50 CYS 51 51 THR 52 52 HIS 53 53 PRO 54 54 ASP 55 55 PHE 56 56 ASP 57 57 GLU 58 58 VAL 59 59 LEU 60 60 VAL 61 61 LYS 62 62 ALA 63 63 GLU 64 64 GLY 65 65 TRP 66 66 CYS 67 67 SER 68 68 VAL 69 69 TYR 70 70 ALA 71 71 PRO 72 72 ALA 73 73 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-03 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 1PIH "The Three Dimensional Structure Of The Paramagnetic Protein Hipip I From E.Halophila Through Nuclear Magnetic Resonance" 100.00 73 100.00 100.00 1.13e-45 PDB 1PIJ "The Three Dimensional Structure Of The Paramagnetic Protein Hipip I From E.Halophila Through Nuclear Magnetic Resonance" 100.00 73 100.00 100.00 1.13e-45 PDB 2HIP "The Molecular Structure Of The High Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Halophila Determined At 2.5-" 97.26 72 100.00 100.00 1.33e-44 SP P04168 "RecName: Full=High-potential iron-sulfur protein isozyme I; AltName: Full=HiPIP 1; AltName: Full=High-redox-potential ferredoxi" 97.26 71 100.00 100.00 1.87e-44 stop_ save_ ############# # Ligands # ############# save_SF4 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'IRON/SULFUR CLUSTER' _BMRB_code SF4 _PDB_code SF4 _Molecular_mass 351.640 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? FE3 FE3 FE . 0 . ? FE4 FE4 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? S3 S3 S . 0 . ? S4 S4 S . 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 FE1 S2 ? ? SING FE1 S3 ? ? SING FE1 S4 ? ? SING FE2 S1 ? ? SING FE2 S3 ? ? SING FE2 S4 ? ? SING FE3 S1 ? ? SING FE3 S2 ? ? SING FE3 S4 ? ? SING FE4 S1 ? ? SING FE4 S2 ? ? SING FE4 S3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $HiPIP_I_peptide 'E. halophila' 1053 Eubacteria . Ectothiorhodospira halophila 'Wild-type does not contain Ala1 and Ser2' 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 $HiPIP_I_peptide 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $HiPIP_I_peptide 6 mM . . . 'sodium isoascorbate buffer' . mM .15 6 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH . . n/a temperature 288 . K stop_ save_ save_sample_conditions_two _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH . . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 DSS H 1 'methyl protons' ppm 4.93 . . . . . $entry_citation $entry_citation (NH4)2SO4 N 15 nitrogen ppm 21.6 . . . . . $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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'high-potential iron-sulfur protein I' _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 4.10 . 1 2 . 1 ALA HB H 1.50 . 1 3 . 2 SER H H 8.71 . 1 4 . 2 SER HA H 4.38 . 1 5 . 2 SER HB2 H 3.78 . 2 6 . 2 SER HB3 H 3.74 . 2 7 . 3 GLU H H 8.65 . 1 8 . 3 GLU HA H 4.45 . 1 9 . 3 GLU HB2 H 1.74 . 1 10 . 3 GLU HB3 H 1.74 . 1 11 . 3 GLU HG2 H 2.25 . 1 12 . 3 GLU HG3 H 2.25 . 1 13 . 4 PRO HA H 4.32 . 1 14 . 4 PRO HB2 H 1.86 . 2 15 . 4 PRO HB3 H 2.24 . 2 16 . 4 PRO HG2 H 2.09 . 2 17 . 4 PRO HG3 H 1.98 . 2 18 . 4 PRO HD2 H 3.88 . 2 19 . 4 PRO HD3 H 3.75 . 2 20 . 5 ARG H H 8.15 . 1 21 . 5 ARG HA H 4.05 . 1 22 . 5 ARG HB2 H 1.15 . 2 23 . 5 ARG HB3 H 1.28 . 2 24 . 5 ARG HG2 H 0.16 . 2 25 . 5 ARG HG3 H 1.16 . 2 26 . 5 ARG HD2 H 1.69 . 2 27 . 5 ARG HD3 H 2.25 . 2 28 . 5 ARG HE H 5.97 . 1 29 . 5 ARG HH11 H 6.52 . 4 30 . 5 ARG HH12 H 6.52 . 4 31 . 5 ARG HH21 H 6.34 . 4 32 . 5 ARG HH22 H 6.34 . 4 33 . 6 ALA H H 9.54 . 1 34 . 6 ALA HA H 3.78 . 1 35 . 6 ALA HB H 1.16 . 1 36 . 7 GLU H H 8.91 . 1 37 . 7 GLU HA H 4.74 . 1 38 . 7 GLU HB2 H 2.28 . 2 39 . 7 GLU HB3 H 2.05 . 2 40 . 7 GLU HG2 H 2.53 . 1 41 . 7 GLU HG3 H 2.45 . 2 42 . 8 ASP H H 9.08 . 1 43 . 8 ASP HA H 4.76 . 1 44 . 8 ASP HB2 H 2.83 . 2 45 . 8 ASP HB3 H 2.74 . 2 46 . 9 GLY H H 10.48 . 1 47 . 9 GLY HA2 H 3.69 . 2 48 . 9 GLY HA3 H 4.33 . 2 49 . 10 HIS H H 8.50 . 1 50 . 10 HIS HB2 H 3.99 . 2 51 . 10 HIS HB3 H 2.75 . 2 52 . 10 HIS HD2 H 6.56 . 1 53 . 10 HIS HE1 H 8.61 . 1 54 . 11 ALA H H 7.14 . 1 55 . 11 ALA HA H 4.14 . 1 56 . 11 ALA HB H 0.94 . 1 57 . 12 HIS H H 9.18 . 1 58 . 12 HIS HA H 4.20 . 1 59 . 12 HIS HB2 H 3.77 . 2 60 . 12 HIS HB3 H 3.48 . 2 61 . 12 HIS HD2 H 7.05 . 1 62 . 12 HIS HE1 H 8.69 . 1 63 . 13 ASP H H 9.03 . 1 64 . 13 ASP HA H 4.26 . 1 65 . 13 ASP HB2 H 3.15 . 2 66 . 13 ASP HB3 H 3.00 . 2 67 . 14 TYR H H 7.75 . 1 68 . 14 TYR HA H 4.90 . 1 69 . 14 TYR HB2 H 4.09 . 2 70 . 14 TYR HB3 H 2.75 . 2 71 . 14 TYR HD1 H 7.13 . 1 72 . 14 TYR HD2 H 7.13 . 1 73 . 14 TYR HE1 H 6.43 . 1 74 . 14 TYR HE2 H 6.43 . 1 75 . 14 TYR HH H 9.43 . 1 76 . 15 VAL H H 8.60 . 1 77 . 15 VAL HA H 4.39 . 1 78 . 15 VAL HB H 2.14 . 1 79 . 15 VAL HG1 H 0.83 . 1 80 . 15 VAL HG2 H 0.83 . 1 81 . 16 ASN H H 8.31 . 1 82 . 16 ASN HA H 4.38 . 1 83 . 16 ASN HB2 H 2.80 . 2 84 . 16 ASN HB3 H 2.55 . 2 85 . 16 ASN HD21 H 7.91 . 2 86 . 16 ASN HD22 H 7.46 . 2 87 . 17 GLU H H 7.83 . 1 88 . 17 GLU HA H 4.39 . 1 89 . 17 GLU HB2 H 1.94 . 2 90 . 17 GLU HB3 H 1.76 . 2 91 . 17 GLU HG2 H 2.28 . 1 92 . 17 GLU HG3 H 2.21 . 2 93 . 18 ALA H H 8.84 . 1 94 . 18 ALA HA H 3.81 . 1 95 . 18 ALA HB H 1.57 . 1 96 . 19 ALA H H 8.42 . 1 97 . 19 ALA HA H 3.85 . 1 98 . 19 ALA HB H 1.33 . 1 99 . 20 ASP H H 8.54 . 1 100 . 20 ASP HA H 4.41 . 1 101 . 20 ASP HB2 H 2.91 . 2 102 . 20 ASP HB3 H 2.77 . 2 103 . 21 ALA H H 8.25 . 1 104 . 21 ALA HA H 4.04 . 1 105 . 21 ALA HB H 0.71 . 1 106 . 22 SER H H 6.80 . 1 107 . 22 SER HA H 3.47 . 1 108 . 22 SER HB2 H 3.78 . 2 109 . 22 SER HB3 H 3.64 . 2 110 . 23 GLY H H 8.64 . 1 111 . 23 GLY HA2 H 3.93 . 2 112 . 23 GLY HA3 H 3.87 . 2 113 . 24 HIS H H 8.63 . 1 114 . 24 HIS HA H 4.62 . 1 115 . 24 HIS HB2 H 3.32 . 2 116 . 24 HIS HB3 H 3.18 . 2 117 . 24 HIS HD2 H 7.29 . 1 118 . 24 HIS HE1 H 8.15 . 1 119 . 25 PRO HA H 4.41 . 1 120 . 25 PRO HB2 H 2.42 . 2 121 . 25 PRO HB3 H 1.98 . 2 122 . 25 PRO HG2 H 3.72 . 1 123 . 25 PRO HG3 H 3.72 . 1 124 . 25 PRO HD2 H 2.80 . 2 125 . 25 PRO HD3 H 2.78 . 2 126 . 26 ARG H H 10.58 . 1 127 . 26 ARG HB2 H 2.40 . 2 128 . 26 ARG HB3 H 2.33 . 2 129 . 26 ARG HG2 H 1.91 . 2 130 . 26 ARG HG3 H 2.00 . 2 131 . 26 ARG HD2 H 3.49 . 2 132 . 26 ARG HD3 H 3.41 . 2 133 . 26 ARG HE H 7.49 . 1 134 . 27 TYR H H 7.78 . 1 135 . 27 TYR HA H 3.83 . 1 136 . 27 TYR HB2 H 2.40 . 2 137 . 27 TYR HB3 H 1.70 . 2 138 . 27 TYR HD1 H 5.42 . 1 139 . 27 TYR HD2 H 5.42 . 1 140 . 27 TYR HE1 H 6.19 . 1 141 . 27 TYR HE2 H 6.19 . 1 142 . 28 GLN H H 5.79 . 1 143 . 28 GLN HA H 3.94 . 1 144 . 28 GLN HB2 H 2.14 . 2 145 . 28 GLN HB3 H 1.44 . 2 146 . 28 GLN HG2 H 1.73 . 1 147 . 28 GLN HG3 H 1.73 . 1 148 . 28 GLN HE21 H 6.84 . 2 149 . 28 GLN HE22 H 7.56 . 2 150 . 29 GLU H H 8.20 . 1 151 . 29 GLU HA H 3.62 . 1 152 . 29 GLU HB2 H 1.82 . 2 153 . 29 GLU HB3 H 2.26 . 2 154 . 29 GLU HG2 H 2.26 . 1 155 . 29 GLU HG3 H 1.88 . 2 156 . 30 GLY H H 8.45 . 1 157 . 30 GLY HA2 H 3.44 . 2 158 . 30 GLY HA3 H 4.36 . 2 159 . 31 GLN H H 7.41 . 1 160 . 31 GLN HA H 4.16 . 1 161 . 31 GLN HB2 H 1.89 . 2 162 . 31 GLN HB3 H 0.40 . 2 163 . 31 GLN HG2 H 2.23 . 1 164 . 31 GLN HG3 H 2.23 . 1 165 . 31 GLN HE21 H 6.48 . 2 166 . 31 GLN HE22 H 7.63 . 2 167 . 32 LEU H H 8.47 . 1 168 . 32 LEU HA H 5.90 . 1 169 . 32 LEU HB2 H 1.43 . 2 170 . 32 LEU HB3 H 1.63 . 2 171 . 32 LEU HG H 2.29 . 1 172 . 32 LEU HD1 H 1.02 . 2 173 . 32 LEU HD2 H 0.82 . 2 174 . 34 GLU H H 7.93 . 1 175 . 34 GLU HA H 2.20 . 1 176 . 34 GLU HB2 H 1.44 . 2 177 . 34 GLU HB3 H 1.16 . 2 178 . 34 GLU HG2 H 1.68 . 1 179 . 34 GLU HG3 H 1.68 . 1 180 . 35 ASN H H 8.16 . 1 181 . 35 ASN HA H 4.91 . 1 182 . 35 ASN HB2 H 3.40 . 2 183 . 35 ASN HB3 H 2.54 . 2 184 . 35 ASN HD21 H 8.16 . 2 185 . 35 ASN HD22 H 7.16 . 2 186 . 37 ALA H H 9.44 . 1 187 . 37 ALA HA H 4.25 . 1 188 . 37 ALA HB H 0.96 . 1 189 . 38 PHE HE1 H 7.18 . 1 190 . 38 PHE HE2 H 7.18 . 1 191 . 39 TRP HB2 H 3.28 . 1 192 . 39 TRP HB3 H 3.28 . 1 193 . 39 TRP HD1 H 7.04 . 1 194 . 39 TRP HE1 H 9.91 . 1 195 . 39 TRP HE3 H 7.20 . 1 196 . 39 TRP HZ2 H 7.20 . 3 197 . 39 TRP HZ3 H 6.66 . 3 198 . 39 TRP HH2 H 6.66 . 1 199 . 40 GLY H H 9.15 . 1 200 . 40 GLY HA2 H 4.14 . 2 201 . 40 GLY HA3 H 3.19 . 2 202 . 41 GLU H H 6.18 . 1 203 . 41 GLU HA H 4.13 . 1 204 . 41 GLU HB2 H 2.05 . 2 205 . 41 GLU HB3 H 1.97 . 2 206 . 41 GLU HG2 H 2.13 . 1 207 . 41 GLU HG3 H 1.97 . 2 208 . 42 ALA H H 8.61 . 1 209 . 42 ALA HA H 4.37 . 1 210 . 42 ALA HB H 1.60 . 1 211 . 43 VAL H H 8.94 . 1 212 . 43 VAL HA H 4.31 . 1 213 . 43 VAL HB H 1.92 . 1 214 . 43 VAL HG1 H 0.92 . 2 215 . 43 VAL HG2 H 0.86 . 2 216 . 44 GLN H H 7.99 . 1 217 . 44 GLN HA H 4.57 . 1 218 . 44 GLN HB2 H 2.12 . 2 219 . 44 GLN HB3 H 2.11 . 2 220 . 44 GLN HG2 H 2.34 . 2 221 . 44 GLN HG3 H 2.30 . 2 222 . 44 GLN HE21 H 7.60 . 2 223 . 44 GLN HE22 H 6.89 . 2 224 . 45 ASP H H 9.21 . 1 225 . 45 ASP HA H 4.53 . 1 226 . 45 ASP HB2 H 3.15 . 2 227 . 45 ASP HB3 H 2.87 . 2 228 . 46 GLY H H 8.76 . 1 229 . 46 GLY HA2 H 4.30 . 2 230 . 46 GLY HA3 H 3.77 . 2 231 . 47 TRP H H 8.26 . 1 232 . 47 TRP HA H 5.49 . 1 233 . 47 TRP HB2 H 3.16 . 2 234 . 47 TRP HB3 H 3.30 . 2 235 . 47 TRP HD1 H 7.22 . 1 236 . 47 TRP HE1 H 10.33 . 1 237 . 47 TRP HE3 H 7.33 . 1 238 . 47 TRP HZ2 H 7.45 . 3 239 . 47 TRP HZ3 H 7.46 . 3 240 . 47 TRP HH2 H 7.33 . 1 241 . 48 GLY H H 10.38 . 1 242 . 48 GLY HA2 H 3.30 . 2 243 . 48 GLY HA3 H 4.36 . 2 244 . 49 ARG H H 7.47 . 1 245 . 49 ARG HA H 4.20 . 1 246 . 49 ARG HB2 H 1.27 . 2 247 . 49 ARG HB3 H 1.47 . 2 248 . 49 ARG HG2 H 1.27 . 2 249 . 49 ARG HG3 H 1.36 . 2 250 . 49 ARG HD2 H 3.02 . 1 251 . 49 ARG HD3 H 3.02 . 1 252 . 49 ARG HE H 7.44 . 1 253 . 49 ARG HH11 H 6.68 . 4 254 . 49 ARG HH12 H 6.68 . 4 255 . 49 ARG HH21 H 6.87 . 4 256 . 49 ARG HH22 H 6.87 . 4 257 . 50 CYS H H 8.88 . 1 258 . 50 CYS HA H 4.17 . 1 259 . 51 THR H H 9.87 . 1 260 . 51 THR HA H 4.68 . 1 261 . 51 THR HB H 4.46 . 1 262 . 51 THR HG2 H 1.21 . 1 263 . 52 HIS HA H 4.10 . 1 264 . 53 PRO HA H 4.29 . 1 265 . 53 PRO HB2 H 1.80 . 2 266 . 53 PRO HB3 H 2.32 . 2 267 . 53 PRO HG2 H 1.69 . 2 268 . 53 PRO HG3 H 1.84 . 2 269 . 53 PRO HD2 H 3.45 . 2 270 . 53 PRO HD3 H 1.80 . 2 271 . 54 ASP HB2 H 2.98 . 2 272 . 54 ASP HB3 H 2.65 . 2 273 . 55 PHE H H 8.32 . 1 274 . 55 PHE HA H 4.63 . 1 275 . 55 PHE HB2 H 2.97 . 2 276 . 55 PHE HB3 H 2.69 . 2 277 . 55 PHE HD1 H 7.05 . 1 278 . 55 PHE HD2 H 7.05 . 1 279 . 55 PHE HE1 H 7.90 . 1 280 . 55 PHE HE2 H 7.90 . 1 281 . 55 PHE HZ H 8.37 . 1 282 . 57 GLU H H 8.38 . 1 283 . 57 GLU HA H 4.07 . 1 284 . 57 GLU HB2 H 1.99 . 2 285 . 57 GLU HB3 H 2.36 . 2 286 . 57 GLU HG2 H 2.36 . 1 287 . 57 GLU HG3 H 2.25 . 2 288 . 58 VAL H H 7.21 . 1 289 . 58 VAL HA H 4.88 . 1 290 . 58 VAL HB H 1.79 . 1 291 . 58 VAL HG1 H 0.52 . 2 292 . 58 VAL HG2 H 0.20 . 2 293 . 59 LEU H H 8.46 . 1 294 . 59 LEU HA H 4.91 . 1 295 . 59 LEU HB2 H 1.44 . 2 296 . 59 LEU HB3 H 1.60 . 2 297 . 59 LEU HG H 1.73 . 1 298 . 59 LEU HD1 H 0.66 . 2 299 . 59 LEU HD2 H 0.56 . 2 300 . 60 VAL H H 8.90 . 1 301 . 60 VAL HA H 5.02 . 1 302 . 60 VAL HG1 H 0.55 . 2 303 . 60 VAL HG2 H 0.21 . 2 304 . 61 LYS H H 8.46 . 1 305 . 61 LYS HA H 3.79 . 1 306 . 61 LYS HB2 H 1.10 . 2 307 . 61 LYS HB3 H 1.73 . 2 308 . 61 LYS HG2 H 0.27 . 2 309 . 61 LYS HG3 H 0.92 . 2 310 . 61 LYS HD2 H 1.17 . 2 311 . 61 LYS HD3 H 0.98 . 2 312 . 61 LYS HE2 H 2.67 . 2 313 . 61 LYS HE3 H 2.64 . 2 314 . 62 ALA H H 8.35 . 1 315 . 62 ALA HA H 3.41 . 1 316 . 62 ALA HB H 1.21 . 1 317 . 63 GLU H H 6.71 . 1 318 . 63 GLU HA H 4.60 . 1 319 . 63 GLU HB2 H 1.90 . 2 320 . 63 GLU HB3 H 2.39 . 2 321 . 63 GLU HG2 H 2.38 . 1 322 . 63 GLU HG3 H 2.27 . 2 323 . 64 GLY H H 7.93 . 1 324 . 64 GLY HA2 H 4.01 . 2 325 . 64 GLY HA3 H 3.93 . 2 326 . 65 TRP HB2 H 3.92 . 2 327 . 65 TRP HB3 H 2.79 . 2 328 . 65 TRP HD1 H 6.98 . 1 329 . 65 TRP HE1 H 9.99 . 1 330 . 65 TRP HE3 H 6.91 . 1 331 . 65 TRP HZ2 H 7.10 . 3 332 . 65 TRP HZ3 H 6.38 . 3 333 . 66 CYS HA H 7.83 . 1 334 . 66 CYS HB2 H 11.05 . 2 335 . 66 CYS HB3 H 6.00 . 2 336 . 67 SER H H 8.34 . 1 337 . 67 SER HA H 3.62 . 1 338 . 67 SER HB2 H 4.10 . 2 339 . 67 SER HB3 H 3.31 . 2 340 . 68 VAL H H 7.78 . 1 341 . 68 VAL HA H 4.22 . 1 342 . 68 VAL HB H 1.67 . 1 343 . 68 VAL HG1 H 0.09 . 2 344 . 68 VAL HG2 H -0.47 . 2 345 . 69 TYR HB2 H 2.95 . 2 346 . 69 TYR HB3 H 2.68 . 2 347 . 69 TYR HD1 H 6.82 . 1 348 . 69 TYR HD2 H 6.82 . 1 349 . 69 TYR HE1 H 6.44 . 3 350 . 69 TYR HE2 H 7.40 . 3 351 . 69 TYR HH H 8.80 . 1 352 . 70 ALA H H 6.44 . 1 353 . 70 ALA HA H 4.52 . 1 354 . 70 ALA HB H 1.05 . 1 355 . 71 PRO HA H 4.44 . 1 356 . 71 PRO HB2 H 2.38 . 2 357 . 71 PRO HB3 H 2.06 . 2 358 . 71 PRO HG2 H 2.16 . 1 359 . 71 PRO HG3 H 2.16 . 1 360 . 71 PRO HD2 H 3.62 . 2 361 . 71 PRO HD3 H 3.67 . 2 362 . 72 ALA H H 8.28 . 1 363 . 72 ALA HA H 4.03 . 1 364 . 72 ALA HB H 1.21 . 1 365 . 73 SER H H 8.07 . 1 366 . 73 SER HA H 4.24 . 1 367 . 73 SER HB2 H 3.83 . 1 368 . 73 SER HB3 H 3.83 . 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_two _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'high-potential iron-sulfur protein I' _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 . 3 GLU N N 124.55 . 1 2 . 5 ARG N N 119.38 . 1 3 . 5 ARG NE N 84.8 . 1 4 . 6 ALA N N 127.14 . 1 5 . 7 GLU N N 122.34 . 1 6 . 8 ASP N N 122.30 . 1 7 . 9 GLY N N 120.65 . 1 8 . 10 HIS N N 119.61 . 1 9 . 11 ALA N N 111.18 . 1 10 . 12 HIS N N 118.95 . 1 11 . 13 ASP N N 111.00 . 1 12 . 14 TYR N N 114.72 . 1 13 . 15 VAL N N 124.58 . 1 14 . 16 ASN N N 117.38 . 1 15 . 16 ASN ND2 N 114.24 . 1 16 . 17 GLU N N 117.18 . 1 17 . 18 ALA N N 128.49 . 1 18 . 19 ALA N N 114.57 . 1 19 . 20 ASP N N 118.16 . 1 20 . 21 ALA N N 124.44 . 1 21 . 22 SER N N 111.43 . 1 22 . 23 GLY N N 112.31 . 1 23 . 24 HIS N N 126.27 . 1 24 . 26 ARG N N 118.67 . 1 25 . 26 ARG NE N 84.9 . 1 26 . 27 TYR N N 121.69 . 1 27 . 28 GLN N N 125.11 . 1 28 . 28 GLN NE2 N 112.16 . 1 29 . 29 GLU N N 121.81 . 1 30 . 30 GLY N N 114.94 . 1 31 . 31 GLN N N 122.30 . 1 32 . 31 GLN NE2 N 108.20 . 1 33 . 32 LEU N N 123.55 . 1 34 . 33 CYS H H 9.28 . 1 35 . 33 CYS HB2 H 16.93 . 2 36 . 33 CYS HB3 H 7.72 . 2 37 . 33 CYS N N 128.93 . 1 38 . 34 GLU N N 109.28 . 1 39 . 35 ASN N N 116.75 . 1 40 . 35 ASN ND2 N 115.96 . 1 41 . 37 ALA N N 138.97 . 1 42 . 40 GLY N N 118.99 . 1 43 . 41 GLU N N 114.33 . 1 44 . 42 ALA N N 123.61 . 1 45 . 43 VAL N N 120.70 . 1 46 . 44 GLN N N 116.89 . 1 47 . 44 GLN NE2 N 111.89 . 1 48 . 45 ASP N N 121.47 . 1 49 . 46 GLY N N 106.99 . 1 50 . 47 TRP N N 121.69 . 1 51 . 48 GLY N N 112.24 . 1 52 . 49 ARG N N 116.71 . 1 53 . 49 ARG NE N 84.2 . 1 54 . 50 CYS HB2 H 14.33 . 2 55 . 50 CYS HB3 H 4.70 . 2 56 . 50 CYS N N 137.27 . 1 57 . 51 THR N N 126.14 . 1 58 . 55 PHE N N 119.03 . 1 59 . 57 GLU N N 115.87 . 1 60 . 58 VAL N N 109.64 . 1 61 . 59 LEU N N 119.44 . 1 62 . 60 VAL N N 114.26 . 1 63 . 61 LYS N N 125.28 . 1 64 . 62 ALA N N 126.01 . 1 65 . 63 GLU N N 109.46 . 1 66 . 64 GLY N N 111.10 . 1 67 . 67 SER N N 113.80 . 1 68 . 68 VAL N N 142.76 . 1 69 . 70 ALA N N 142.69 . 1 70 . 72 ALA N N 125.38 . 1 71 . 73 SER N N 119.78 . 1 stop_ save_