data_1324 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy ; _BMRB_accession_number 1324 _BMRB_flat_file_name bmr1324.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 Veitch Nigel C. . 2 Concar David W. . 3 Williams Robert J.P. . 4 Whitford David . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 58 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-14 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 ; Veitch, Nigel C., Concar, David W., Williams, Robert J. P., Whitford, David, "Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy," FEBS Lett. 238 (1), 49-55 (1988). ; _Citation_title ; Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Veitch Nigel C. . 2 Concar David W. . 3 Williams Robert J.P. . 4 Whitford David . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 238 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 49 _Page_last 55 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_cytochrome_b5 _Saveframe_category molecular_system _Mol_system_name 'cytochrome b5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome b5' $cytochrome_b5 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytochrome_b5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome b5' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; AVKYYTLEEIQKHNNSKSTW LILHYKVYDLTKFLEEHPGG EEVLREQAGGDATENFEDVG HSTDARELSKTFIIGELHPD DR ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 VAL 3 LYS 4 TYR 5 TYR 6 THR 7 LEU 8 GLU 9 GLU 10 ILE 11 GLN 12 LYS 13 HIS 14 ASN 15 ASN 16 SER 17 LYS 18 SER 19 THR 20 TRP 21 LEU 22 ILE 23 LEU 24 HIS 25 TYR 26 LYS 27 VAL 28 TYR 29 ASP 30 LEU 31 THR 32 LYS 33 PHE 34 LEU 35 GLU 36 GLU 37 HIS 38 PRO 39 GLY 40 GLY 41 GLU 42 GLU 43 VAL 44 LEU 45 ARG 46 GLU 47 GLN 48 ALA 49 GLY 50 GLY 51 ASP 52 ALA 53 THR 54 GLU 55 ASN 56 PHE 57 GLU 58 ASP 59 VAL 60 GLY 61 HIS 62 SER 63 THR 64 ASP 65 ALA 66 ARG 67 GLU 68 LEU 69 SER 70 LYS 71 THR 72 PHE 73 ILE 74 ILE 75 GLY 76 GLU 77 LEU 78 HIS 79 PRO 80 ASP 81 ASP 82 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-29 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 1323 "cytochrome b5" 100.00 82 100.00 100.00 3.44e-52 BMRB 17457 b5 100.00 104 100.00 100.00 8.84e-53 PDB 1CYO "Bovine Cytochrome B(5)" 100.00 93 100.00 100.00 1.32e-52 PDB 1EHB "Crystal Structure Of Recombinant Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 100.00 100.00 3.44e-52 PDB 1ES1 "Crystal Structure Of Val61his Mutant Of Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 98.78 98.78 6.66e-51 PDB 1HKO "Nmr Structure Of Bovine Cytochrome B5" 100.00 104 100.00 100.00 9.33e-53 PDB 1J0Q "Solution Structure Of Oxidized Bovine Microsomal Cytochrome B5 Mutant V61h" 98.78 82 98.77 98.77 4.29e-50 PDB 1LQX "Crystal Structure Of V45e Mutant Of Cytochrome B5" 100.00 82 98.78 98.78 4.36e-51 PDB 1LR6 "Crystal Structure Of V45y Mutant Of Cytochrome B5" 100.00 82 98.78 98.78 2.79e-51 PDB 1M20 "Crystal Structure Of F35y Mutant Of Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 98.78 100.00 1.14e-51 PDB 1M2I "Crystal Structure Of E44aE56A MUTANT OF CYTOCHROME B5" 100.00 82 97.56 97.56 7.27e-51 PDB 1M59 "Crystal Structure Of P40v Mutant Of Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 98.78 98.78 6.66e-51 PDB 1NX7 "Solution Structure Of Oxidized Bovine Microsomal Cytochrome B5" 100.00 82 100.00 100.00 3.44e-52 PDB 1SH4 "Solution Structure Of Oxidized Bovine Microsomal Cytochrome B5 Mutant V45h" 100.00 82 98.78 98.78 6.66e-51 PDB 1U9M "Crystal Structure Of F58w Mutant Of Cytochrome B5" 100.00 82 98.78 100.00 2.37e-51 PDB 1U9U "Crystal Structure Of F58y Mutant Of Cytochrome B5" 100.00 82 98.78 100.00 1.14e-51 PDB 3X32 "Crystal Structure Of The Oxidized Form Of The Solubilized Domain Of Porcine Cytochrome B5 In Form 1 Crystal" 100.00 94 98.78 100.00 6.54e-52 PDB 3X33 "Crystal Structure Of The Oxidized Form Of The Solubilized Domain Of Porcine Cytochrome B5 In Form 2 Crystal" 100.00 94 98.78 100.00 6.54e-52 PDB 3X34 "Crystal Structure Of The Reduced Form Of The Solubilized Domain Of Porcine Cytochrome B5 In Form 1 Crystal" 100.00 94 98.78 100.00 6.54e-52 PDB 3X35 "Crystal Structure Of The Reduced Form Of The Solubilized Domain Of Porcine Cytochrome B5 In Form 2 Crystal" 100.00 94 98.78 100.00 6.54e-52 PDB 4HIN "2.4a Resolution Structure Of Bovine Cytochrome B5 (s71l)" 100.00 82 98.78 98.78 3.74e-51 EMBL CAA31949 "unnamed protein product [Bos taurus]" 100.00 134 100.00 100.00 2.41e-52 GB AAA72186 "microsomal cytochrome b-5 [synthetic construct]" 100.00 94 97.56 98.78 4.45e-51 GB AAB32285 "peditoxin, pedin=cytochrome b-like heme protein [Toxopneustes pileolus=sea urchins, Lamarck, Peptide, 82 aa]" 100.00 82 97.56 100.00 1.88e-50 GB AAC14455 "cytochrome b-5 [Bos taurus]" 100.00 98 100.00 100.00 7.15e-53 GB AAC48779 "cytochrome b5 [Sus scrofa]" 100.00 134 98.78 100.00 1.12e-51 GB AAC48780 "cytochrome b5 [Sus scrofa]" 73.17 69 98.33 100.00 2.82e-34 PRF 1106188A "cytochrome b5" 100.00 97 100.00 100.00 1.07e-52 PRF 1106188C "cytochrome b5" 100.00 97 98.78 100.00 7.88e-52 PRF 1803548B "cytochrome b5" 100.00 134 100.00 100.00 2.41e-52 REF NP_001001770 "cytochrome b5 [Sus scrofa]" 100.00 134 98.78 100.00 1.12e-51 REF NP_001159663 "cytochrome b5 [Ovis aries]" 98.78 134 98.77 100.00 8.62e-51 REF NP_001180227 "cytochrome b5 [Canis lupus familiaris]" 98.78 134 97.53 100.00 7.67e-50 REF NP_001274163 "cytochrome b5 [Capra hircus]" 98.78 134 98.77 100.00 8.62e-51 REF NP_776458 "cytochrome b5 [Bos taurus]" 100.00 134 100.00 100.00 2.41e-52 SP P00171 "RecName: Full=Cytochrome b5" 100.00 134 100.00 100.00 2.41e-52 SP P00172 "RecName: Full=Cytochrome b5" 100.00 134 98.78 100.00 1.12e-51 TPG DAA15965 "TPA: cytochrome b5 [Bos taurus]" 100.00 134 100.00 100.00 2.41e-52 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue _Fraction $cytochrome_b5 cow 9913 Eukaryota Metazoa Bos taurus liver microsomes 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 $cytochrome_b5 '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 unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . na temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'cytochrome b5' _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 . 4 TYR H H 8.17 . 1 2 . 4 TYR HA H 5.71 . 1 3 . 5 TYR H H 8.75 . 1 4 . 5 TYR HA H 5.17 . 1 5 . 6 THR H H 9.23 . 1 6 . 6 THR HA H 4.64 . 1 7 . 20 TRP H H 8.95 . 1 8 . 20 TRP HA H 6.51 . 1 9 . 21 LEU H H 8.98 . 1 10 . 21 LEU HA H 5.03 . 1 11 . 22 ILE H H 8.65 . 1 12 . 22 ILE HA H 5.52 . 1 13 . 23 LEU H H 8.85 . 1 14 . 23 LEU HA H 4.91 . 1 15 . 24 HIS H H 9.47 . 1 16 . 24 HIS HA H 3.83 . 1 17 . 25 TYR H H 8.38 . 1 18 . 25 TYR HA H 3.87 . 1 19 . 26 LYS H H 8.46 . 1 20 . 26 LYS HA H 4.88 . 1 21 . 27 VAL H H 8.48 . 1 22 . 27 VAL HA H 4.45 . 1 23 . 28 TYR H H 9.34 . 1 24 . 28 TYR HA H 4.79 . 1 25 . 29 ASP H H 8.37 . 1 26 . 29 ASP HA H 5.24 . 1 27 . 30 LEU H H 8.53 . 1 28 . 30 LEU HA H 4.3 . 1 29 . 34 LEU H H 8.43 . 1 30 . 34 LEU HA H 2.93 . 1 31 . 44 LEU H H 5.94 . 1 32 . 44 LEU HA H 3.83 . 1 33 . 52 ALA H H 9.03 . 1 34 . 52 ALA HA H 5.2 . 1 35 . 53 THR H H 8.57 . 1 36 . 53 THR HA H 3.3 . 1 37 . 54 GLU H H 8.69 . 1 38 . 54 GLU HA H 3.82 . 1 39 . 58 ASP H H 8.08 . 1 40 . 58 ASP HA H 4.19 . 1 41 . 59 VAL H H 6.63 . 1 42 . 59 VAL HA H 3.18 . 1 43 . 61 HIS H H 6.2 . 1 44 . 61 HIS HA H 2.57 . 1 45 . 71 THR H H 7.87 . 1 46 . 71 THR HA H 4.01 . 1 47 . 72 PHE H H 7.6 . 1 48 . 72 PHE HA H 5 . 1 49 . 73 ILE H H 6.98 . 1 50 . 73 ILE HA H 3.7 . 1 51 . 74 ILE H H 8.85 . 1 52 . 74 ILE HA H 4.65 . 1 53 . 76 GLU H H 9.09 . 1 54 . 76 GLU HA H 5.32 . 1 55 . 80 ASP H H 11.12 . 1 56 . 80 ASP HA H 4.45 . 1 57 . 82 ARG H H 7.03 . 1 58 . 82 ARG HA H 4.08 . 1 stop_ save_