data_4229 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Artificial Fe8S8 ferredoxin: the D13C variant of Bacillus schlegelii Fe7S8 ferredoxin ; _BMRB_accession_number 4229 _BMRB_flat_file_name bmr4229.str _Entry_type original _Submission_date 1998-08-20 _Accession_date 1998-08-20 _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 Aono S. . . 2 Bentrop D. . . 3 Bertini I. . . 4 Cosenza G. . . 5 Luchinat C. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 516 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-01 original BMRB . stop_ _Original_release_date 1998-08-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of an artficial Fe8S8 ferredoxin: the D13C variant of Bacillus schlegelii Fe7S8 ferredoxin" ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99089613 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Aono S. . . 2 Bentrop D. . . 3 Bertini I. . . 4 Cosenza G. . . 5 Luchinat C. . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European Journal of Biochemistry' _Journal_volume 258 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 502 _Page_last 514 _Year 1998 _Details . loop_ _Keyword 'electron transport' 'iron-sulfur protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_Fe8S8_Fd _Saveframe_category molecular_system _Mol_system_name 'Fe8S8 Fd' _Abbreviation_common Fd _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Fe8S8 Fd' $Fe8S8_Fd 'FeS4, cluster 1' $entity_SF4 'FeS4, cluster 2' $entity_SF4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' loop_ _Biological_function 'The exact physiological function of the wild-type protein is not known.' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Fe8S8_Fd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ferredoxin _Name_variant D13C _Abbreviation_common Fd _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 77 _Mol_residue_sequence ; AYVITEPCIGTKCASCVEVC PVDCIHEGEDQYYIDPDVCI DCGACEAVCPVSAIYHEDFV PEEWKSYIQKNRDFFKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 TYR 3 3 VAL 4 4 ILE 5 5 THR 6 6 GLU 7 7 PRO 8 8 CYS 9 9 ILE 10 10 GLY 11 11 THR 12 12 LYS 13 13 CYS 14 14 ALA 15 15 SER 16 16 CYS 17 17 VAL 18 18 GLU 19 19 VAL 20 20 CYS 21 21 PRO 22 22 VAL 23 23 ASP 24 24 CYS 25 25 ILE 26 26 HIS 27 27 GLU 28 28 GLY 29 29 GLU 30 30 ASP 31 31 GLN 32 32 TYR 33 33 TYR 34 34 ILE 35 35 ASP 36 36 PRO 37 37 ASP 38 38 VAL 39 39 CYS 40 40 ILE 41 41 ASP 42 42 CYS 43 43 GLY 44 44 ALA 45 45 CYS 46 46 GLU 47 47 ALA 48 48 VAL 49 49 CYS 50 50 PRO 51 51 VAL 52 52 SER 53 53 ALA 54 54 ILE 55 55 TYR 56 56 HIS 57 57 GLU 58 58 ASP 59 59 PHE 60 60 VAL 61 61 PRO 62 62 GLU 63 63 GLU 64 64 TRP 65 65 LYS 66 66 SER 67 67 TYR 68 68 ILE 69 69 GLN 70 70 LYS 71 71 ASN 72 72 ARG 73 73 ASP 74 74 PHE 75 75 PHE 76 76 LYS 77 77 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 _ATCC_number $Fe8S8_Fd . 1484 Eubacteria . Bacillus schlegelii 43741 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 $Fe8S8_Fd 'recombinant technology' 'Escherichia coli' Escherichia coli 'JM 109' plasmid 'pKKFd D13C' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The sample was exchanged into D2O solution by ultrafiltration (Centrikon-3 tube) before the spectra were collected. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Fe8S8_Fd . mM 2 3.3 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_1D-NOE_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1D-NOE _Sample_label $sample_1 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' 20 . mM pH 6.5 0.1 n/a pressure 1 . atm temperature 300 0.5 K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 6.5 0.1 n/a pressure 1 . atm temperature 282 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 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_one _Saveframe_category assigned_chemical_shifts _Details ; A second set of slightly shifted resonances corresponding to a thermodynamically less stable conformational species was observed for a total of 34 amino acids (3,5-7,9,17-19,21,23,25-28,30,31, 33-35,47,48,54-59,63,64,67,71-74). Several unassogned signals were also observed. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Fe8S8 Fd' _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 4.13 0.02 1 2 . 1 ALA HB H 1.55 0.02 1 3 . 2 TYR HA H 5.06 0.02 1 4 . 2 TYR HB2 H 2.51 0.02 2 5 . 2 TYR HB3 H 3.38 0.02 2 6 . 2 TYR HD2 H 6.63 0.02 3 7 . 2 TYR HE1 H 7.10 0.02 3 8 . 3 VAL H H 8.93 0.02 1 9 . 3 VAL HA H 4.11 0.02 1 10 . 3 VAL HB H 1.91 0.02 2 11 . 3 VAL HG1 H 0.87 0.02 2 12 . 4 ILE H H 7.51 0.02 1 13 . 4 ILE HA H 4.42 0.02 1 14 . 4 ILE HB H 2.66 0.02 2 15 . 5 THR H H 8.54 0.02 1 16 . 5 THR HA H 4.06 0.02 1 17 . 5 THR HB H 3.29 0.02 2 18 . 5 THR HG2 H 1.35 0.02 1 19 . 6 GLU HA H 3.32 0.02 1 20 . 6 GLU HB2 H 0.742 0.02 2 21 . 6 GLU HG2 H 2.181 0.02 2 22 . 6 GLU HG3 H 1.932 0.02 2 23 . 7 PRO HA H 4.33 0.02 1 24 . 7 PRO HB2 H 2.31 0.02 1 25 . 7 PRO HB3 H 1.17 0.02 1 26 . 7 PRO HG2 H 1.93 0.02 2 27 . 7 PRO HD2 H 2.85 0.02 2 28 . 8 CYS H H 7.32 0.02 1 29 . 8 CYS HA H 5.48 0.02 1 30 . 8 CYS HB2 H 8.481 0.02 2 31 . 8 CYS HB3 H 10.12 0.02 2 32 . 9 ILE H H 7.93 0.02 1 33 . 9 ILE HA H 4.26 0.02 2 34 . 9 ILE HB H 1.94 0.02 2 35 . 9 ILE HG12 H 1.52 0.02 2 36 . 9 ILE HG13 H 1.04 0.02 2 37 . 9 ILE HG2 H 0.93 0.02 1 38 . 9 ILE HD1 H 0.78 0.02 1 39 . 10 GLY H H 9.13 0.02 1 40 . 10 GLY HA2 H 4.34 0.02 2 41 . 10 GLY HA3 H 3.66 0.02 2 42 . 11 THR H H 8.83 0.02 1 43 . 11 THR HA H 4.17 0.02 1 44 . 11 THR HB H 3.84 0.02 2 45 . 11 THR HG2 H 0.90 0.02 1 46 . 12 LYS HB2 H 1.54 0.02 2 47 . 12 LYS HB3 H 1.46 0.02 2 48 . 12 LYS HG2 H 1.72 0.02 2 49 . 12 LYS HG3 H 1.90 0.02 2 50 . 12 LYS HD2 H 3.01 0.02 2 51 . 12 LYS HE2 H 3.76 0.02 2 52 . 12 LYS HZ H 7.10 0.02 2 53 . 13 CYS HA H 9.66 0.02 1 54 . 13 CYS HB2 H 10.00 0.02 2 55 . 13 CYS HB3 H 16.10 0.02 2 56 . 14 ALA HA H 3.00 0.02 2 57 . 15 SER H H 7.48 0.02 2 58 . 15 SER HA H 4.17 0.02 2 59 . 15 SER HB2 H 4.031 0.02 2 60 . 15 SER HB3 H 3.842 0.02 2 61 . 16 CYS HA H 6.72 0.02 2 62 . 16 CYS HB2 H 15.90 0.02 2 63 . 16 CYS HB3 H 4.232 0.02 2 64 . 17 VAL HA H 4.92 0.02 2 65 . 17 VAL HB H 2.85 0.02 2 66 . 17 VAL HG1 H 1.03 0.02 2 67 . 17 VAL HG2 H 0.91 0.02 2 68 . 18 GLU H H 6.97 0.02 2 69 . 18 GLU HA H 4.10 0.02 2 70 . 18 GLU HB2 H 2.101 0.02 2 71 . 18 GLU HG2 H 2.34 0.02 2 72 . 18 GLU HG3 H 2.26 0.02 2 73 . 19 VAL H H 6.68 0.02 2 74 . 19 VAL HA H 4.46 0.02 2 75 . 19 VAL HB H 2.15 0.02 2 76 . 19 VAL HG1 H 0.71 0.02 2 77 . 19 VAL HG2 H 0.26 0.02 2 78 . 20 CYS H H 7.12 0.02 2 79 . 20 CYS HA H 4.98 0.02 2 80 . 20 CYS HB2 H 5.481 0.02 2 81 . 20 CYS HB3 H 11.06 0.02 2 82 . 21 PRO HA H 5.11 0.02 2 83 . 21 PRO HB2 H 2.362 0.02 2 84 . 21 PRO HG2 H 1.58 0.02 2 85 . 21 PRO HD2 H 3.60 0.02 2 86 . 23 ASP H H 7.45 0.02 2 87 . 23 ASP HA H 4.38 0.02 2 88 . 23 ASP HB2 H 2.94 0.02 2 89 . 23 ASP HB3 H 2.53 0.02 2 90 . 24 CYS HA H 6.20 0.02 2 91 . 24 CYS HB2 H 4.96 0.02 2 92 . 24 CYS HB3 H 2.30 0.02 2 93 . 25 ILE H H 8.00 0.02 2 94 . 25 ILE HA H 5.28 0.02 2 95 . 25 ILE HB H 1.82 0.02 2 96 . 25 ILE HG2 H 0.99 0.02 1 97 . 26 HIS H H 9.77 0.02 2 98 . 26 HIS HA H 5.08 0.02 2 99 . 26 HIS HB2 H 3.191 0.02 2 100 . 26 HIS HB3 H 3.662 0.02 2 101 . 26 HIS HD1 H 7.26 0.02 2 102 . 27 GLU H H 9.22 0.02 2 103 . 27 GLU HA H 2.84 0.02 2 104 . 27 GLU HB2 H 1.291 0.02 2 105 . 27 GLU HB3 H 1.912 0.02 2 106 . 27 GLU HG2 H 1.601 0.02 2 107 . 27 GLU HG3 H 2.232 0.02 2 108 . 28 GLY H H 7.76 0.02 2 109 . 28 GLY HA2 H 4.94 0.02 2 110 . 28 GLY HA3 H 3.81 0.02 2 111 . 29 GLU H H 9.15 0.02 2 112 . 29 GLU HA H 3.96 0.02 2 113 . 29 GLU HB2 H 2.04 0.02 2 114 . 29 GLU HG2 H 2.33 0.02 2 115 . 29 GLU HG3 H 2.26 0.02 2 116 . 30 ASP H H 8.89 0.02 2 117 . 30 ASP HA H 4.54 0.02 2 118 . 30 ASP HB2 H 2.86 0.02 2 119 . 30 ASP HB3 H 2.66 0.02 2 120 . 31 GLN H H 7.21 0.02 2 121 . 31 GLN HA H 4.53 0.02 2 122 . 31 GLN HB2 H 2.041 0.02 2 123 . 31 GLN HB3 H 1.652 0.02 2 124 . 31 GLN HG2 H 1.45 0.02 2 125 . 31 GLN HG3 H 0.55 0.02 2 126 . 31 GLN HE21 H 5.632 0.02 2 127 . 31 GLN HE22 H 7.201 0.02 2 128 . 32 TYR H H 7.70 0.02 2 129 . 32 TYR HA H 5.36 0.02 2 130 . 32 TYR HB2 H 2.651 0.02 2 131 . 32 TYR HB3 H 1.202 0.02 2 132 . 32 TYR HH H 6.44 0.02 2 133 . 33 TYR H H 8.98 0.02 2 134 . 33 TYR HA H 5.01 0.02 2 135 . 33 TYR HB2 H 2.291 0.02 2 136 . 33 TYR HB3 H 3.012 0.02 2 137 . 33 TYR HD1 H 6.18 0.02 2 138 . 33 TYR HE1 H 6.25 0.02 2 139 . 33 TYR HH H 5.52 0.02 2 140 . 34 ILE H H 9.09 0.02 2 141 . 34 ILE HA H 5.01 0.02 2 142 . 34 ILE HB H 2.40 0.02 2 143 . 34 ILE HG2 H 2.20 0.02 1 144 . 35 ASP H H 8.39 0.02 2 145 . 35 ASP HA H 4.23 0.02 2 146 . 35 ASP HB2 H 2.541 0.02 2 147 . 35 ASP HB3 H 1.032 0.02 2 148 . 36 PRO HA H 4.23 0.02 2 149 . 36 PRO HB2 H 2.081 0.02 2 150 . 36 PRO HB3 H 2.392 0.02 2 151 . 36 PRO HG2 H 1.961 0.02 2 152 . 36 PRO HG3 H 2.002 0.02 2 153 . 36 PRO HD2 H 4.18 0.02 2 154 . 36 PRO HD3 H 4.57 0.02 2 155 . 37 ASP H H 8.12 0.02 2 156 . 37 ASP HA H 4.70 0.02 2 157 . 37 ASP HB2 H 2.60 0.02 2 158 . 37 ASP HB3 H 2.74 0.02 2 159 . 38 VAL H H 6.95 0.02 2 160 . 38 VAL HA H 4.02 0.02 2 161 . 38 VAL HB H 1.51 0.02 2 162 . 38 VAL HG1 H 0.75 0.02 2 163 . 38 VAL HG2 H 0.90 0.02 2 164 . 39 CYS H H 7.41 0.02 2 165 . 39 CYS HB2 H 8.551 0.02 2 166 . 39 CYS HB3 H 10.77 0.02 2 167 . 40 ILE HA H 5.21 0.02 2 168 . 40 ILE HB H 2.72 0.02 2 169 . 40 ILE HG2 H 1.10 0.02 1 170 . 41 ASP HA H 5.24 0.02 2 171 . 41 ASP HB2 H 3.392 0.02 2 172 . 41 ASP HB3 H 3.061 0.02 2 173 . 42 CYS HA H 9.25 0.02 2 174 . 42 CYS HB2 H 9.401 0.02 2 175 . 42 CYS HB3 H 15.30 0.02 2 176 . 43 GLY H H 8.08 0.02 2 177 . 43 GLY HA2 H 4.36 0.02 2 178 . 43 GLY HA3 H 4.25 0.02 2 179 . 45 CYS HA H 6.85 0.02 2 180 . 45 CYS HB2 H 15.00 0.02 2 181 . 45 CYS HB3 H 4.922 0.02 2 182 . 46 GLU H H 8.42 0.02 2 183 . 46 GLU HA H 3.55 0.02 2 184 . 46 GLU HB2 H 2.08 0.02 2 185 . 46 GLU HB3 H 1.84 0.02 2 186 . 46 GLU HG2 H 2.25 0.02 2 187 . 47 ALA H H 6.89 0.02 2 188 . 47 ALA HA H 4.14 0.02 2 189 . 47 ALA HB H 1.35 0.02 1 190 . 48 VAL H H 6.68 0.02 2 191 . 48 VAL HA H 4.37 0.02 2 192 . 48 VAL HB H 2.12 0.02 2 193 . 48 VAL HG1 H 0.39 0.02 2 194 . 48 VAL HG2 H 0.68 0.02 2 195 . 49 CYS HA H 3.90 0.02 2 196 . 49 CYS HB2 H 9.001 0.02 2 197 . 49 CYS HB3 H 13.15 0.02 2 198 . 50 PRO HD2 H 3.35 0.02 2 199 . 51 VAL HA H 3.27 0.02 2 200 . 51 VAL HB H 1.20 0.02 2 201 . 51 VAL HG1 H 0.86 0.02 2 202 . 51 VAL HG2 H 0.94 0.02 2 203 . 52 SER H H 7.46 0.02 2 204 . 52 SER HA H 4.36 0.02 2 205 . 52 SER HB2 H 4.09 0.02 2 206 . 52 SER HB3 H 3.88 0.02 2 207 . 53 ALA H H 8.00 0.02 2 208 . 54 ILE HA H 4.99 0.02 2 209 . 54 ILE HB H 1.45 0.02 2 210 . 54 ILE HG2 H 0.94 0.02 1 211 . 55 TYR H H 8.36 0.02 2 212 . 55 TYR HA H 4.76 0.02 2 213 . 55 TYR HB2 H 3.072 0.02 2 214 . 55 TYR HB3 H 2.401 0.02 2 215 . 55 TYR HD1 H 7.1 0.02 2 216 . 55 TYR HE1 H 6.97 0.02 2 217 . 56 HIS H H 9.30 0.02 2 218 . 56 HIS HA H 3.27 0.02 2 219 . 56 HIS HB2 H 2.391 0.02 2 220 . 56 HIS HB3 H 2.732 0.02 2 221 . 56 HIS HD1 H 6.83 0.02 2 222 . 57 GLU H H 7.73 0.02 2 223 . 57 GLU HA H 3.84 0.02 2 224 . 57 GLU HB2 H 1.80 0.02 2 225 . 57 GLU HB3 H 1.69 0.02 2 226 . 57 GLU HG2 H 2.21 0.02 2 227 . 57 GLU HG3 H 2.02 0.02 2 228 . 58 ASP H H 9.97 0.02 2 229 . 58 ASP HA H 4.46 0.02 2 230 . 58 ASP HB2 H 2.31 0.02 2 231 . 58 ASP HB3 H 2.62 0.02 2 232 . 59 PHE H H 8.60 0.02 2 233 . 59 PHE HA H 4.66 0.02 2 234 . 59 PHE HB2 H 2.911 0.02 2 235 . 59 PHE HB3 H 3.752 0.02 2 236 . 59 PHE HD1 H 7.36 0.02 2 237 . 60 VAL H H 6.96 0.02 2 238 . 60 VAL HA H 3.41 0.02 2 239 . 60 VAL HB H 1.84 0.02 2 240 . 60 VAL HG1 H 1.02 0.02 2 241 . 61 PRO HA H 4.12 0.02 2 242 . 61 PRO HB2 H 1.121 0.02 2 243 . 61 PRO HB3 H 2.072 0.02 2 244 . 61 PRO HG2 H 1.71 0.02 2 245 . 61 PRO HG3 H 1.59 0.02 2 246 . 61 PRO HD2 H 2.841 0.02 2 247 . 61 PRO HD3 H 2.672 0.02 2 248 . 62 GLU H H 8.64 0.02 2 249 . 62 GLU HA H 3.83 0.02 2 250 . 62 GLU HB2 H 2.091 0.02 2 251 . 62 GLU HB3 H 1.922 0.02 2 252 . 62 GLU HG2 H 2.31 0.02 2 253 . 62 GLU HG3 H 2.27 0.02 2 254 . 63 GLU H H 9.62 0.02 2 255 . 63 GLU HA H 4.17 0.02 2 256 . 63 GLU HB2 H 1.721 0.02 2 257 . 63 GLU HB3 H 1.632 0.02 2 258 . 63 GLU HG2 H 1.45 0.02 2 259 . 64 TRP H H 8.24 0.02 2 260 . 64 TRP HA H 5.64 0.02 2 261 . 64 TRP HB2 H 2.921 0.02 2 262 . 64 TRP HB3 H 3.752 0.02 2 263 . 64 TRP HD1 H 7.34 0.02 2 264 . 64 TRP HE1 H 7.19 0.02 2 265 . 64 TRP HE3 H 9.98 0.02 2 266 . 64 TRP HZ2 H 7.46 0.02 2 267 . 64 TRP HZ3 H 7.50 0.02 2 268 . 64 TRP HH2 H 7.34 0.02 2 269 . 65 LYS H H 7.80 0.02 2 270 . 65 LYS HA H 4.01 0.02 2 271 . 65 LYS HB2 H 2.081 0.02 2 272 . 65 LYS HB3 H 2.032 0.02 2 273 . 65 LYS HG2 H 1.61 0.02 2 274 . 65 LYS HD2 H 1.69 0.02 2 275 . 65 LYS HE2 H 2.97 0.02 2 276 . 66 SER HA H 4.28 0.02 2 277 . 66 SER HB2 H 4.01 0.02 2 278 . 66 SER HB3 H 3.90 0.02 2 279 . 67 TYR H H 8.80 0.02 2 280 . 67 TYR HA H 4.17 0.02 2 281 . 67 TYR HB2 H 3.431 0.02 2 282 . 67 TYR HB3 H 3.012 0.02 2 283 . 67 TYR HD1 H 7.54 0.02 2 284 . 67 TYR HE1 H 7.09 0.02 2 285 . 68 ILE H H 8.33 0.02 2 286 . 68 ILE HA H 3.85 0.02 2 287 . 68 ILE HB H 2.12 0.02 2 288 . 68 ILE HG12 H 1.92 0.02 2 289 . 68 ILE HG13 H 1.24 0.02 2 290 . 68 ILE HG2 H 1.04 0.02 1 291 . 68 ILE HD1 H 1.11 0.02 1 292 . 69 GLN H H 8.06 0.02 2 293 . 69 GLN HA H 4.05 0.02 2 294 . 69 GLN HB2 H 2.261 0.02 2 295 . 69 GLN HB3 H 2.112 0.02 2 296 . 69 GLN HG2 H 2.52 0.02 2 297 . 69 GLN HG3 H 2.47 0.02 2 298 . 69 GLN HE21 H 8.16 0.02 2 299 . 69 GLN HE22 H 6.87 0.02 2 300 . 70 LYS H H 8.08 0.02 2 301 . 70 LYS HA H 4.07 0.02 2 302 . 70 LYS HB2 H 2.031 0.02 2 303 . 70 LYS HB3 H 1.802 0.02 2 304 . 70 LYS HG2 H 1.461 0.02 2 305 . 70 LYS HG3 H 1.552 0.02 2 306 . 70 LYS HD2 H 2.96 0.02 2 307 . 70 LYS HE2 H 3.62 0.02 2 308 . 71 ASN H H 8.22 0.02 2 309 . 71 ASN HA H 4.90 0.02 2 310 . 71 ASN HB2 H 3.721 0.02 2 311 . 71 ASN HB3 H 3.322 0.02 2 312 . 71 ASN HD21 H 8.74 0.02 2 313 . 72 ARG H H 7.32 0.02 2 314 . 72 ARG HA H 4.04 0.02 2 315 . 72 ARG HB2 H 2.042 0.02 2 316 . 72 ARG HB3 H 2.131 0.02 2 317 . 72 ARG HG2 H 1.62 0.02 2 318 . 72 ARG HG3 H 1.81 0.02 2 319 . 72 ARG HD2 H 3.45 0.02 2 320 . 72 ARG HD3 H 3.14 0.02 2 321 . 72 ARG HE H 7.61 0.02 2 322 . 73 ASP H H 9.29 0.02 2 323 . 73 ASP HA H 4.39 0.02 2 324 . 73 ASP HB2 H 2.711 0.02 2 325 . 73 ASP HB3 H 2.632 0.02 2 326 . 74 PHE H H 7.32 0.02 2 327 . 74 PHE HA H 3.75 0.02 2 328 . 74 PHE HB2 H 2.18 0.02 2 329 . 74 PHE HB3 H 2.13 0.02 2 330 . 74 PHE HD1 H 5.69 0.02 2 331 . 74 PHE HE1 H 6.93 0.02 2 332 . 74 PHE HZ H 7.09 0.02 2 333 . 75 PHE H H 7.02 0.02 2 334 . 75 PHE HA H 4.09 0.02 2 335 . 75 PHE HB2 H 2.731 0.02 2 336 . 75 PHE HB3 H 3.452 0.02 2 337 . 75 PHE HD1 H 7.61 0.02 2 338 . 75 PHE HE1 H 7.25 0.02 2 339 . 75 PHE HZ H 7.41 0.02 2 340 . 76 LYS H H 7.37 0.02 2 341 . 76 LYS HA H 4.30 0.02 2 342 . 76 LYS HB2 H 1.801 0.02 2 343 . 76 LYS HB3 H 1.882 0.02 2 344 . 76 LYS HG2 H 1.511 0.02 2 345 . 76 LYS HG3 H 1.452 0.02 2 346 . 76 LYS HD2 H 1.60 0.02 2 347 . 76 LYS HE2 H 2.97 0.02 2 348 . 77 LYS H H 7.84 0.02 2 349 . 77 LYS HA H 4.14 0.02 2 350 . 77 LYS HB2 H 1.65 0.02 2 351 . 77 LYS HB3 H 1.35 0.02 2 352 . 77 LYS HG2 H 1.60 0.02 2 353 . 77 LYS HD2 H 1.80 0.02 2 354 . 77 LYS HE2 H 2.92 0.02 2 stop_ save_ save_chemical_shift_assignment_two _Saveframe_category assigned_chemical_shifts _Details ; The assignments of this data set were derived from 1D-NOE difference experiments at 282 K in D2O solution. Hence, they refer only to protons in spatial proximity to the hyperfine-shifted betaCh2 protons of the cluster coordinating cysteines. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_2 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Fe8S8 Fd' _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 VAL H H 8.93 0.02 2 2 . 3 VAL HA H 4.09 0.02 2 3 . 3 VAL HB H 1.90 0.02 2 4 . 3 VAL HG1 H 0.86 0.02 2 5 . 5 THR H H 8.42 0.02 2 6 . 5 THR HA H 4.03 0.02 2 7 . 5 THR HB H 3.30 0.02 2 8 . 5 THR HG2 H 1.35 0.02 1 9 . 6 GLU HA H 3.30 0.02 2 10 . 6 GLU HB2 H 0.732 0.02 2 11 . 6 GLU HG2 H 2.181 0.02 2 12 . 6 GLU HG3 H 1.922 0.02 2 13 . 7 PRO HA H 4.28 0.02 2 14 . 7 PRO HB2 H 2.36 0.02 2 15 . 7 PRO HB3 H 1.28 0.02 2 16 . 7 PRO HG2 H 1.93 0.02 2 17 . 7 PRO HD2 H 2.18 0.02 2 18 . 7 PRO HD3 H 2.87 0.02 2 19 . 9 ILE H H 7.79 0.02 2 20 . 9 ILE HA H 4.33 0.02 2 21 . 9 ILE HB H 1.94 0.02 2 22 . 9 ILE HG12 H 1.54 0.02 2 23 . 9 ILE HD1 H 0.81 0.02 1 24 . 17 VAL HA H 4.85 0.02 2 25 . 17 VAL HB H 2.83 0.02 2 26 . 17 VAL HG1 H 0.98 0.02 2 27 . 17 VAL HG2 H 0.86 0.02 2 28 . 18 GLU H H 6.92 0.02 2 29 . 18 GLU HA H 4.09 0.02 2 30 . 18 GLU HB2 H 2.081 0.02 2 31 . 18 GLU HG2 H 2.33 0.02 2 32 . 18 GLU HG3 H 2.25 0.02 2 33 . 19 VAL H H 6.64 0.02 2 34 . 19 VAL HA H 4.48 0.02 2 35 . 19 VAL HB H 2.18 0.02 2 36 . 19 VAL HG1 H 0.74 0.02 2 37 . 19 VAL HG2 H 0.30 0.02 2 38 . 21 PRO HA H 5.14 0.02 2 39 . 21 PRO HB2 H 2.422 0.02 2 40 . 23 ASP H H 7.42 0.02 2 41 . 23 ASP HA H 4.32 0.02 2 42 . 23 ASP HB2 H 2.92 0.02 2 43 . 23 ASP HB3 H 2.52 0.02 2 44 . 25 ILE H H 7.97 0.02 2 45 . 25 ILE HA H 5.22 0.02 2 46 . 25 ILE HB H 1.79 0.02 2 47 . 25 ILE HG12 H 0.95 0.02 2 48 . 26 HIS H H 9.70 0.02 2 49 . 26 HIS HA H 5.01 0.02 2 50 . 26 HIS HB2 H 3.161 0.02 2 51 . 26 HIS HB3 H 3.632 0.02 2 52 . 26 HIS HD1 H 7.23 0.02 2 53 . 27 GLU H H 9.05 0.02 2 54 . 27 GLU HA H 2.66 0.02 2 55 . 27 GLU HB2 H 1.201 0.02 2 56 . 27 GLU HB3 H 1.772 0.02 2 57 . 27 GLU HG2 H 1.361 0.02 2 58 . 27 GLU HG3 H 2.202 0.02 2 59 . 28 GLY H H 7.70 0.02 2 60 . 28 GLY HA2 H 4.93 0.02 2 61 . 28 GLY HA3 H 3.81 0.02 2 62 . 30 ASP H H 8.87 0.02 2 63 . 30 ASP HA H 4.54 0.02 2 64 . 30 ASP HB2 H 2.87 0.02 2 65 . 30 ASP HB3 H 2.67 0.02 2 66 . 31 GLN H H 7.28 0.02 2 67 . 31 GLN HA H 4.56 0.02 2 68 . 31 GLN HB2 H 2.041 0.02 2 69 . 31 GLN HB3 H 1.752 0.02 2 70 . 31 GLN HG2 H 1.31 0.02 2 71 . 31 GLN HG3 H 0.52 0.02 2 72 . 31 GLN HE21 H 7.101 0.02 2 73 . 31 GLN HE22 H 5.522 0.02 2 74 . 33 TYR H H 8.86 0.02 2 75 . 33 TYR HA H 4.85 0.02 2 76 . 33 TYR HB2 H 2.241 0.02 2 77 . 33 TYR HB3 H 2.962 0.02 2 78 . 33 TYR HD1 H 6.12 0.02 2 79 . 33 TYR HE1 H 6.12 0.02 2 80 . 34 ILE H H 9.03 0.02 2 81 . 34 ILE HA H 5.01 0.02 2 82 . 34 ILE HB H 2.35 0.02 2 83 . 34 ILE HG12 H 2.20 0.02 2 84 . 35 ASP H H 8.37 0.02 2 85 . 35 ASP HA H 4.23 0.02 2 86 . 35 ASP HB2 H 2.521 0.02 2 87 . 35 ASP HB3 H 0.982 0.02 2 88 . 47 ALA H H 7.14 0.02 2 89 . 47 ALA HA H 4.21 0.02 2 90 . 47 ALA HB H 1.39 0.02 1 91 . 48 VAL H H 6.79 0.02 2 92 . 48 VAL HA H 4.42 0.02 2 93 . 48 VAL HB H 2.14 0.02 2 94 . 48 VAL HG1 H 0.76 0.02 2 95 . 48 VAL HG2 H 0.60 0.02 2 96 . 54 ILE H H 7.95 0.02 2 97 . 54 ILE HA H 5.04 0.02 2 98 . 55 TYR H H 8.44 0.02 2 99 . 55 TYR HA H 4.85 0.02 2 100 . 55 TYR HB2 H 3.102 0.02 2 101 . 55 TYR HB3 H 2.441 0.02 2 102 . 55 TYR HD1 H 7.16 0.02 2 103 . 55 TYR HE1 H 7.03 0.02 2 104 . 56 HIS H H 9.38 0.02 2 105 . 56 HIS HA H 3.26 0.02 2 106 . 56 HIS HB2 H 2.441 0.02 2 107 . 56 HIS HB3 H 2.762 0.02 2 108 . 56 HIS HD1 H 6.83 0.02 2 109 . 56 HIS HE1 H 7.71 0.02 2 110 . 57 GLU H H 7.71 0.02 2 111 . 57 GLU HA H 3.84 0.02 2 112 . 57 GLU HB2 H 1.80 0.02 2 113 . 57 GLU HB3 H 1.69 0.02 2 114 . 57 GLU HG2 H 2.02 0.02 2 115 . 57 GLU HG3 H 2.20 0.02 2 116 . 58 ASP H H 10.0 0.02 2 117 . 58 ASP HA H 4.46 0.02 2 118 . 58 ASP HB2 H 2.63 0.02 2 119 . 58 ASP HB3 H 2.31 0.02 2 120 . 59 PHE HA H 4.67 0.02 2 121 . 59 PHE HB2 H 2.931 0.02 2 122 . 59 PHE HB3 H 3.762 0.02 2 123 . 59 PHE HD1 H 7.37 0.02 2 124 . 63 GLU H H 9.65 0.02 2 125 . 63 GLU HA H 4.19 0.02 2 126 . 63 GLU HB2 H 1.761 0.02 2 127 . 63 GLU HB3 H 1.712 0.02 2 128 . 63 GLU HG2 H 1.50 0.02 2 129 . 64 TRP H H 8.30 0.02 2 130 . 64 TRP HA H 5.63 0.02 2 131 . 64 TRP HB2 H 2.931 0.02 2 132 . 64 TRP HB3 H 3.752 0.02 2 133 . 64 TRP HD1 H 7.34 0.02 2 134 . 64 TRP HE1 H 7.19 0.02 2 135 . 64 TRP HE3 H 9.94 0.02 2 136 . 64 TRP HZ2 H 7.46 0.02 2 137 . 64 TRP HZ3 H 7.50 0.02 2 138 . 64 TRP HH2 H 7.34 0.02 2 139 . 67 TYR H H 8.74 0.02 2 140 . 67 TYR HA H 4.14 0.02 2 141 . 67 TYR HB2 H 3.361 0.02 2 142 . 67 TYR HB3 H 2.982 0.02 2 143 . 67 TYR HD1 H 7.51 0.02 2 144 . 67 TYR HE1 H 7.02 0.02 2 145 . 71 ASN H H 8.19 0.02 2 146 . 71 ASN HA H 4.87 0.02 2 147 . 71 ASN HB2 H 3.701 0.02 2 148 . 71 ASN HB3 H 3.292 0.02 2 149 . 71 ASN HD21 H 8.64 0.02 2 150 . 72 ARG H H 7.29 0.02 2 151 . 72 ARG HA H 4.03 0.02 2 152 . 72 ARG HB2 H 2.032 0.02 2 153 . 72 ARG HB3 H 2.111 0.02 2 154 . 72 ARG HG2 H 1.79 0.02 2 155 . 72 ARG HG3 H 1.61 0.02 2 156 . 72 ARG HE H 7.54 0.02 2 157 . 73 ASP H H 9.27 0.02 2 158 . 73 ASP HA H 4.38 0.02 2 159 . 73 ASP HB2 H 2.701 0.02 2 160 . 73 ASP HB3 H 2.622 0.02 2 161 . 74 PHE H H 7.30 0.02 2 162 . 74 PHE HA H 3.73 0.02 1 stop_ save_