data_1551 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin ; _BMRB_accession_number 1551 _BMRB_flat_file_name bmr1551.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Pochapsky Thomas C. . 2 Ye Xiao Mei . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 174 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Pochapsky, Thomas C., Ye, Xiao Mei, "1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin," Biochemistry 30, 3850-3856 (1991). ; _Citation_title ; 1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin ; _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 Pochapsky Thomas C. . 2 Ye Xiao Mei . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3850 _Page_last 3856 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_P450_reductase _Saveframe_category molecular_system _Mol_system_name 'P450 reductase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'P450 reductase' $P450_reductase stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_P450_reductase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'P450 reductase' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; SKVVYVSHDGTRRQLDVADG VSLMQAAVSNGIYDIVGDCG GSASCATCHVYVNEAFTDKV PAANEREIGMLECVTAELKP NSRLCCQIIMTPELDGIVVD VPDRQW ; loop_ _Residue_seq_code _Residue_label 1 SER 2 LYS 3 VAL 4 VAL 5 TYR 6 VAL 7 SER 8 HIS 9 ASP 10 GLY 11 THR 12 ARG 13 ARG 14 GLN 15 LEU 16 ASP 17 VAL 18 ALA 19 ASP 20 GLY 21 VAL 22 SER 23 LEU 24 MET 25 GLN 26 ALA 27 ALA 28 VAL 29 SER 30 ASN 31 GLY 32 ILE 33 TYR 34 ASP 35 ILE 36 VAL 37 GLY 38 ASP 39 CYS 40 GLY 41 GLY 42 SER 43 ALA 44 SER 45 CYS 46 ALA 47 THR 48 CYS 49 HIS 50 VAL 51 TYR 52 VAL 53 ASN 54 GLU 55 ALA 56 PHE 57 THR 58 ASP 59 LYS 60 VAL 61 PRO 62 ALA 63 ALA 64 ASN 65 GLU 66 ARG 67 GLU 68 ILE 69 GLY 70 MET 71 LEU 72 GLU 73 CYS 74 VAL 75 THR 76 ALA 77 GLU 78 LEU 79 LYS 80 PRO 81 ASN 82 SER 83 ARG 84 LEU 85 CYS 86 CYS 87 GLN 88 ILE 89 ILE 90 MET 91 THR 92 PRO 93 GLU 94 LEU 95 ASP 96 GLY 97 ILE 98 VAL 99 VAL 100 ASP 101 VAL 102 PRO 103 ASP 104 ARG 105 GLN 106 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 BMRB 2278 putidaredoxin 100.00 106 100.00 100.00 6.14e-71 BMRB 4149 putidaredoxin 100.00 106 98.11 99.06 1.93e-69 BMRB 4154 putidaredoxin 100.00 106 99.06 100.00 2.13e-70 PDB 1GPX "C85s Gapdx, Nmr, 20 Structures" 100.00 106 98.11 99.06 1.93e-69 PDB 1OQQ "Crystal Structure Of C73sC85S MUTANT OF PUTIDAREDOXIN, A [2FE-2s] Ferredoxin From Pseudomonas Putida, At 1.47a Resolution" 100.00 106 97.17 98.11 1.81e-68 PDB 1OQR "Crystal Structure Of C73s Mutant Of Putidaredoxin, A [2fe- 2s] Ferredoxin From Pseudomonas Putida, At 1.65a Resolution" 100.00 106 98.11 99.06 1.93e-69 PDB 1PDX Putidaredoxin 100.00 106 99.06 100.00 2.13e-70 PDB 1PUT "An Nmr-Derived Model For The Solution Structure Of Oxidized Putidaredoxin, A 2fe, 2-S Ferredoxin From Pseudomonas" 100.00 106 100.00 100.00 6.14e-71 PDB 1R7S "Putidaredoxin (Fe2s2 Ferredoxin), C73g Mutant" 100.00 106 98.11 99.06 5.94e-69 PDB 1XLN "Crystal Structure Of Oxidized C73sC85S PUTIDAREDOXIN, A [2fe-2s] Ferredoxin From Pseudomonas Putida" 100.00 106 97.17 98.11 1.81e-68 PDB 1XLO "Structure Of Reduced C73s/c85s Putidaredoxin, A [2fe-2s] Ferredoxin From Pseudomonas Putida" 100.00 106 97.17 98.11 1.81e-68 PDB 1XLP "Structure Of Oxidized C73s Putidaredoxin From Pseudomonas Putida" 100.00 106 98.11 99.06 1.93e-69 PDB 1XLQ "Crystal Structure Of Reduced C73s Putidaredoxin From Pseudomonas Putida" 100.00 106 98.11 99.06 1.93e-69 PDB 1YJI "Rdc-Refined Solution Nmr Structure Of Reduced Putidaredoxin" 100.00 106 99.06 100.00 2.13e-70 PDB 1YJJ "Rdc-Refined Solution Nmr Structure Of Oxidized Putidaredoxin" 100.00 106 99.06 100.00 2.13e-70 PDB 2M56 "The Structure Of The Complex Of Cytochrome P450cam And Its Electron Donor Putidaredoxin Determined By Paramagnetic Nmr Spectros" 100.00 106 98.11 99.06 1.93e-69 PDB 3LB8 "Crystal Structure Of The Covalent Putidaredoxin Reductase- Putidaredoxin Complex" 100.00 106 97.17 98.11 1.81e-68 PDB 3W9C "Crystal Structure Of The Electron Transfer Complex Of Cytochrome P450cam With Putidaredoxin" 100.00 108 98.11 99.06 2.27e-69 PDB 4JWS "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 112 99.06 100.00 1.83e-70 PDB 4JWU "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 113 97.17 98.11 9.28e-68 PDB 4JX1 "Crystal Structure Of Reduced Cytochrome P450cam-putidaredoxin Complex Bound To Camphor And 5-exo-hydroxycamphor" 100.00 113 97.17 98.11 9.28e-68 DBJ BAA00414 "putidaredoxin [Pseudomonas putida]" 100.00 107 99.06 100.00 1.75e-70 DBJ BAN13288 "putidaredoxin [Pseudomonas putida]" 100.00 107 99.06 100.00 1.75e-70 GB AAA25759 "putidaredoxin [Pseudomonas putida]" 100.00 107 99.06 100.00 1.75e-70 REF WP_032492635 "putidaredoxin [Pseudomonas putida]" 100.00 107 99.06 100.00 1.75e-70 REF YP_009083114 "putidaredoxin [Pseudomonas putida]" 100.00 107 99.06 100.00 1.75e-70 SP P00259 "RecName: Full=Putidaredoxin; Short=PDX" 100.00 107 99.06 100.00 1.75e-70 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 $P450_reductase . 303 Bacteria . Pseudomonas putida generic 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 $P450_reductase 'not available' . . . . . 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 . _Model . _Field_strength . _Details . 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 7.4 . na temperature 290 . 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 DSS H . . ppm 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_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 'P450 reductase' _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 SER HA H 3.88 . 1 2 . 1 SER HB2 H 3.57 . 2 3 . 1 SER HB3 H 3.4 . 2 4 . 2 LYS H H 9.15 . 1 5 . 2 LYS HA H 4.58 . 1 6 . 2 LYS HB2 H 1.55 . 2 7 . 2 LYS HB3 H 1.29 . 2 8 . 2 LYS HG2 H 1.12 . 2 9 . 2 LYS HG3 H 1 . 2 10 . 2 LYS HD2 H 1.38 . 2 11 . 2 LYS HD3 H 1.25 . 2 12 . 2 LYS HE2 H 2.65 . 2 13 . 2 LYS HE3 H 2.82 . 2 14 . 3 VAL H H 8.48 . 1 15 . 3 VAL HA H 4.18 . 1 16 . 3 VAL HB H 1.38 . 1 17 . 3 VAL HG1 H .04 . 2 18 . 3 VAL HG2 H .45 . 2 19 . 4 VAL H H 8.5 . 1 20 . 4 VAL HA H 4.4 . 1 21 . 4 VAL HB H 1.78 . 1 22 . 4 VAL HG1 H .495 . 2 23 . 4 VAL HG2 H .53 . 2 24 . 5 TYR H H 8.84 . 1 25 . 5 TYR HA H 4.72 . 1 26 . 5 TYR HB2 H 2.72 . 2 27 . 5 TYR HB3 H 2.23 . 2 28 . 5 TYR HD1 H 6.48 . 1 29 . 5 TYR HD2 H 6.48 . 1 30 . 5 TYR HE1 H 6.05 . 1 31 . 5 TYR HE2 H 6.05 . 1 32 . 5 TYR HH H 8.02 . 1 33 . 6 VAL H H 9.5 . 1 34 . 6 VAL HA H 4.68 . 1 35 . 6 VAL HB H 2.18 . 1 36 . 6 VAL HG1 H .56 . 2 37 . 6 VAL HG2 H .715 . 2 38 . 14 GLN H H 8.55 . 1 39 . 14 GLN HA H 5.095 . 1 40 . 14 GLN HB2 H 1.68 . 1 41 . 14 GLN HB3 H 1.68 . 1 42 . 14 GLN HG2 H 1.82 . 2 43 . 14 GLN HG3 H 1.97 . 2 44 . 15 LEU H H 9.19 . 1 45 . 15 LEU HA H 4.54 . 1 46 . 15 LEU HB2 H 1.23 . 2 47 . 15 LEU HB3 H 1.31 . 2 48 . 15 LEU HG H 1.31 . 1 49 . 15 LEU HD1 H .52 . 2 50 . 15 LEU HD2 H .6 . 2 51 . 16 ASP H H 8.19 . 1 52 . 16 ASP HA H 4.71 . 1 53 . 16 ASP HB2 H 2.14 . 2 54 . 16 ASP HB3 H 2.42 . 2 55 . 17 VAL H H 9 . 1 56 . 17 VAL HA H 3.81 . 1 57 . 17 VAL HB H 1.58 . 1 58 . 17 VAL HG1 H .58 . 2 59 . 17 VAL HG2 H .66 . 2 60 . 18 ALA H H 8.4 . 1 61 . 18 ALA HA H 3.92 . 1 62 . 18 ALA HB H 1.1 . 1 63 . 50 VAL H H 8.19 . 1 64 . 50 VAL HA H 4.115 . 1 65 . 51 TYR H H 8.945 . 1 66 . 51 TYR HA H 4.96 . 1 67 . 51 TYR HB2 H 2.62 . 2 68 . 51 TYR HB3 H 2.69 . 2 69 . 51 TYR HD1 H 6.63 . 1 70 . 51 TYR HD2 H 6.63 . 1 71 . 51 TYR HE1 H 6.65 . 1 72 . 51 TYR HE2 H 6.65 . 1 73 . 52 VAL H H 8.615 . 1 74 . 52 VAL HA H 3.63 . 1 75 . 52 VAL HB H 1.89 . 1 76 . 52 VAL HG1 H .66 . 2 77 . 52 VAL HG2 H .81 . 2 78 . 53 ASN H H 8.26 . 1 79 . 53 ASN HA H 4.28 . 1 80 . 53 ASN HB2 H 2.57 . 2 81 . 53 ASN HB3 H 2.79 . 2 82 . 53 ASN HD21 H 8.04 . 1 83 . 53 ASN HD22 H 8.04 . 1 84 . 56 PHE H H 8.66 . 1 85 . 56 PHE HA H 4.26 . 1 86 . 56 PHE HB2 H 2.98 . 2 87 . 56 PHE HB3 H 2.57 . 2 88 . 56 PHE HD1 H 6.96 . 1 89 . 56 PHE HD2 H 6.96 . 1 90 . 56 PHE HE1 H 7.1 . 1 91 . 56 PHE HE2 H 7.1 . 1 92 . 56 PHE HZ H 7 . 1 93 . 76 ALA H H 7.62 . 1 94 . 76 ALA HA H 4.38 . 1 95 . 76 ALA HB H 1.41 . 1 96 . 77 GLU H H 7.91 . 1 97 . 77 GLU HA H 3.71 . 1 98 . 77 GLU HB2 H 1.58 . 2 99 . 77 GLU HB3 H 1.81 . 2 100 . 77 GLU HG2 H 2.09 . 2 101 . 77 GLU HG3 H 2.26 . 2 102 . 78 LEU H H 8.49 . 1 103 . 78 LEU HA H 4.41 . 1 104 . 78 LEU HB2 H 1.58 . 2 105 . 78 LEU HB3 H 1.59 . 2 106 . 78 LEU HG H 1.17 . 1 107 . 78 LEU HD1 H .67 . 2 108 . 78 LEU HD2 H .82 . 2 109 . 79 LYS H H 9.71 . 1 110 . 79 LYS HA H 4.8 . 1 111 . 79 LYS HB2 H 1.58 . 2 112 . 79 LYS HB3 H 1.73 . 2 113 . 79 LYS HG2 H .93 . 2 114 . 79 LYS HG3 H 1.07 . 2 115 . 79 LYS HD2 H 1.81 . 2 116 . 79 LYS HD3 H 1.95 . 2 117 . 79 LYS HE2 H 2.28 . 1 118 . 79 LYS HE3 H 2.28 . 1 119 . 80 PRO HA H 4.24 . 1 120 . 80 PRO HB2 H 1.76 . 2 121 . 80 PRO HB3 H 2.28 . 2 122 . 80 PRO HG2 H 1.83 . 2 123 . 80 PRO HG3 H 2.14 . 2 124 . 80 PRO HD2 H 3.7 . 2 125 . 80 PRO HD3 H 3.52 . 2 126 . 81 ASN H H 8.62 . 1 127 . 81 ASN HA H 4.68 . 1 128 . 81 ASN HB2 H 2.58 . 2 129 . 81 ASN HB3 H 2.71 . 2 130 . 81 ASN HD21 H 6.545 . 2 131 . 81 ASN HD22 H 7.45 . 2 132 . 82 SER H H 7.985 . 1 133 . 82 SER HA H 5.03 . 1 134 . 82 SER HB2 H 3.95 . 2 135 . 82 SER HB3 H 4 . 2 136 . 82 SER HG H 10.095 . 1 137 . 83 ARG H H 9.375 . 1 138 . 83 ARG HA H 4.65 . 1 139 . 83 ARG HB2 H 1.02 . 2 140 . 83 ARG HB3 H 1.05 . 2 141 . 83 ARG HG2 H 1.22 . 2 142 . 83 ARG HG3 H 1.56 . 2 143 . 83 ARG HD2 H 3.08 . 2 144 . 83 ARG HD3 H 3.39 . 2 145 . 83 ARG HE H 10.29 . 1 146 . 96 GLY H H 9.64 . 1 147 . 96 GLY HA2 H 2.82 . 2 148 . 96 GLY HA3 H 4.02 . 2 149 . 97 ILE H H 7.77 . 1 150 . 97 ILE HA H 1.03 . 1 151 . 97 ILE HB H .46 . 1 152 . 97 ILE HG12 H .64 . 2 153 . 97 ILE HG13 H 1.34 . 2 154 . 97 ILE HG2 H 1.1 . 1 155 . 97 ILE HD1 H .36 . 1 156 . 98 VAL H H 4.88 . 1 157 . 98 VAL HA H 4.48 . 1 158 . 98 VAL HB H 1.39 . 1 159 . 98 VAL HG1 H .61 . 2 160 . 98 VAL HG2 H .75 . 2 161 . 99 VAL H H 8.59 . 1 162 . 99 VAL HA H 4.75 . 1 163 . 99 VAL HB H 1.48 . 1 164 . 99 VAL HG1 H .3 . 2 165 . 99 VAL HG2 H .36 . 2 166 . 100 ASP H H 8.825 . 1 167 . 100 ASP HA H 5.28 . 1 168 . 100 ASP HB2 H 2.5 . 1 169 . 100 ASP HB3 H 2.5 . 1 170 . 101 VAL H H 8.96 . 1 171 . 101 VAL HA H 4.23 . 1 172 . 101 VAL HB H 1.88 . 1 173 . 101 VAL HG1 H .58 . 2 174 . 101 VAL HG2 H .72 . 2 stop_ save_