data_5091 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of A67V mutant of rat ferro cytochrome B5 ; _BMRB_accession_number 5091 _BMRB_flat_file_name bmr5091.str _Entry_type original _Submission_date 2001-07-19 _Accession_date 2001-07-24 _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 Shahzad N. . . 2 Dangi B. . . 3 Blankman J. I. . 4 Guiles R. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 418 "coupling constants" 66 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-02 original author . stop_ _Original_release_date 2003-06-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mutagenic modulation of the entropy change on oxidation of cytochrome B5: an analysis of the contribution of conformational entropy ; _Citation_status submitted _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 Shahzad N. . . 2 Dangi B. . . 3 Blankman J. I. . 4 Guiles R. D. . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'cytochrome B5' 'electron transport' 'solution structures' stop_ save_ ################################## # Molecular system description # ################################## save_system_CYTOCHROME_B5 _Saveframe_category molecular_system _Mol_system_name 'CYTOCHROME B5' _Abbreviation_common 'CYTOCHROME B5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CYTOCHROME B5' $CYTOCHROME_B5 HEM $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'not present' _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' _Abbreviation_common 'CYTOCHROME B5' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; DKDVKYYTLEEIQKHKDSKS TWVILHHKVYDLTKFLEEHP GGEEVLREQAGGDATENFED VGHSTDVRELSKTYIIGELH PDDRSKIAKPSETL ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 LYS 3 ASP 4 VAL 5 LYS 6 TYR 7 TYR 8 THR 9 LEU 10 GLU 11 GLU 12 ILE 13 GLN 14 LYS 15 HIS 16 LYS 17 ASP 18 SER 19 LYS 20 SER 21 THR 22 TRP 23 VAL 24 ILE 25 LEU 26 HIS 27 HIS 28 LYS 29 VAL 30 TYR 31 ASP 32 LEU 33 THR 34 LYS 35 PHE 36 LEU 37 GLU 38 GLU 39 HIS 40 PRO 41 GLY 42 GLY 43 GLU 44 GLU 45 VAL 46 LEU 47 ARG 48 GLU 49 GLN 50 ALA 51 GLY 52 GLY 53 ASP 54 ALA 55 THR 56 GLU 57 ASN 58 PHE 59 GLU 60 ASP 61 VAL 62 GLY 63 HIS 64 SER 65 THR 66 ASP 67 VAL 68 ARG 69 GLU 70 LEU 71 SER 72 LYS 73 THR 74 TYR 75 ILE 76 ILE 77 GLY 78 GLU 79 LEU 80 HIS 81 PRO 82 ASP 83 ASP 84 ARG 85 SER 86 LYS 87 ILE 88 ALA 89 LYS 90 PRO 91 SER 92 GLU 93 THR 94 LEU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 REF NP_071581 'cytochrome b-5 [Rattus norvegicus]' 100.00 134 98.94 98.94 1.47e-47 SWISS-PROT P00173 'Cytochrome b5' 100.00 134 98.94 98.94 1.47e-47 GenBank AAH86945 'Cytochrome b-5 [Rattus norvegicus]' 100.00 134 98.94 98.94 1.47e-47 GenBank EDL75180 'cytochrome b-5, isoform CRA_c [Rattus norvegicus]' 63.83 83 100.00 100.00 1.07e-27 GenBank AAA72557 'cytochrome b(5)' 100.00 99 98.94 98.94 4.42e-47 GenBank AAB67610 'cytochrome b5 [Rattus norvegicus]' 100.00 134 98.94 98.94 1.47e-47 DBJ BAA02492 'cytochrome b5 precursor [Rattus norvegicus]' 100.00 134 98.94 98.94 1.47e-47 GenBank AAA72420 'cytochrome b5' 92.55 92 98.85 98.85 5.22e-43 PDB 1MNY 'Dimethyl Propionate Ester Heme-Containing Cytochrome B5' 100.00 94 98.94 98.94 9.84e-47 PDB 2AXX 'The Solution Structure Of Oxidized Rat Microsomal Cytochrome B5, Nmr, 21 Structures' 100.00 94 98.94 98.94 9.84e-47 PDB 1IEU 'Apocytochrome B5, Ph 6.2, 298 K, Nmr, 10 Structures' 100.00 98 98.94 98.94 5.58e-47 PDB 1JEX 'Solution Structure Of A67v Mutant Of Rat Ferro Cytochrome B5' 100.00 94 100.00 100.00 3.77e-47 PDB 1I8C 'Solution Structure Of The Water-Soluble Fragment Of Rat Hepatic Apocytochrome B5' 100.00 98 98.94 98.94 5.58e-47 PDB 1IET 'Apocytochrome B5, Ph 6.2, 298 K, Nmr, Minimized Average Structure' 100.00 98 98.94 98.94 5.58e-47 PDB 1BLV 'Solution Structure Of Oxidized Rat Microsomal Cytochrome B5 In The Presence Of 2 M Guanidinium Chloride' 98.94 94 98.92 98.92 3.65e-46 PDB 1I87 'Solution Structure Of The Water-Soluble Fragment Of Rat Hepatic Apocytochrome B5' 100.00 98 98.94 98.94 5.58e-47 PDB 1B5B 'Rat Ferrocytochrome B5 B Conformation, Nmr, 1 Structure' 98.94 94 98.92 98.92 3.65e-46 PDB 1BFX 'The Solution Nmr Structure Of The B Form Of Oxidized Rat Microsomal Cytochrome B5, Minimized Average Structure' 100.00 99 98.94 98.94 4.42e-47 PDB 1AXX 'The Solution Structure Of Oxidized Rat Microsomal Cytochrome B5, Nmr, 19 Structures' 98.94 94 98.92 98.92 3.65e-46 PDB 1B5A 'Rat Ferrocytochrome B5 A Conformation, Nmr, 1 Structure' 98.94 94 98.92 98.92 3.65e-46 PDB 1AQA 'Solution Structure Of Reduced Microsomal Rat Cytochrome B5, Nmr, Minimized Average Structure' 100.00 94 98.94 98.94 9.84e-47 PDB 1AW3 'The Solution Nmr Structure Of Oxidized Rat Microsomal Cytochrome B5, Minimized Average Structure' 98.94 94 98.92 98.92 3.65e-46 BMRB 4130 'cytochrome b5' 100.00 94 98.94 98.94 9.84e-47 BMRB 4131 'cytochrome b5' 100.00 94 98.94 98.94 9.84e-47 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 9 15:44:13 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA H . 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 CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? 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 $CYTOCHROME_B5 'Norway rat' 10116 Eukaryota Metazoa Rattus norvegicus 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 '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 $CYTOCHROME_B5 2 mM . 'phosphate buffer' 1 mM . 'sodium dithionate' . mM . TSP 0.05 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task refinement stop_ _Details 'Guentert, P.' save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.1 loop_ _Task collection stop_ _Details Bruker save_ save_FELIX _Saveframe_category software _Name FELIX _Version 97 loop_ _Task 'data analysis' stop_ _Details MSI save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 313 . K 'ionic strength' 1 . mM 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methy protons' ppm . . . . . . 1.0 $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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _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 . 2 LYS H H 8.030 . 1 2 . 3 ASP H H 8.150 . 1 3 . 3 ASP HA H 4.500 . 1 4 . 3 ASP HB2 H 2.610 . 2 5 . 3 ASP HB3 H 2.490 . 2 6 . 4 VAL H H 7.590 . 1 7 . 4 VAL HA H 3.860 . 1 8 . 4 VAL HB H 1.660 . 1 9 . 4 VAL HG1 H 0.710 . 2 10 . 4 VAL HG2 H 0.410 . 2 11 . 5 LYS H H 8.080 . 1 12 . 5 LYS HA H 4.160 . 1 13 . 5 LYS HB2 H 1.680 . 2 14 . 5 LYS HG2 H 1.190 . 2 15 . 6 TYR H H 8.140 . 1 16 . 6 TYR HA H 5.750 . 1 17 . 6 TYR HB2 H 2.910 . 2 18 . 6 TYR HB3 H 2.700 . 2 19 . 6 TYR HD2 H 6.930 . 2 20 . 6 TYR HE1 H 6.660 . 1 21 . 7 TYR H H 8.740 . 1 22 . 7 TYR HA H 5.240 . 1 23 . 7 TYR HB2 H 3.240 . 2 24 . 7 TYR HB3 H 2.550 . 2 25 . 7 TYR HD2 H 6.990 . 2 26 . 7 TYR HE1 H 6.640 . 1 27 . 8 THR H H 9.200 . 1 28 . 8 THR HA H 4.510 . 1 29 . 8 THR HG2 H 1.260 . 1 30 . 9 LEU H H 9.760 . 1 31 . 9 LEU HA H 4.120 . 1 32 . 9 LEU HB2 H 1.620 . 2 33 . 9 LEU HB3 H 1.790 . 2 34 . 9 LEU HG H 1.240 . 1 35 . 9 LEU HD1 H 1.100 . 2 36 . 9 LEU HD2 H 1.050 . 2 37 . 10 GLU H H 8.470 . 1 38 . 10 GLU HA H 4.010 . 1 39 . 10 GLU HB2 H 2.320 . 2 40 . 10 GLU HB3 H 2.060 . 2 41 . 10 GLU HG2 H 2.700 . 2 42 . 10 GLU HG3 H 2.530 . 2 43 . 11 GLU H H 7.700 . 1 44 . 11 GLU HA H 4.140 . 1 45 . 11 GLU HB2 H 2.370 . 2 46 . 11 GLU HB3 H 2.220 . 2 47 . 11 GLU HG2 H 2.530 . 2 48 . 11 GLU HG3 H 2.770 . 2 49 . 12 ILE H H 8.530 . 1 50 . 12 ILE HA H 3.780 . 1 51 . 12 ILE HB H 2.030 . 1 52 . 12 ILE HG12 H 2.040 . 1 53 . 12 ILE HG13 H 1.710 . 2 54 . 12 ILE HG2 H 0.970 . 1 55 . 12 ILE HD1 H 0.690 . 1 56 . 13 GLN H H 8.220 . 1 57 . 13 GLN HA H 4.400 . 1 58 . 13 GLN HB2 H 2.270 . 2 59 . 13 GLN HB3 H 2.080 . 2 60 . 13 GLN HG2 H 2.680 . 2 61 . 13 GLN HG3 H 2.470 . 2 62 . 14 LYS H H 7.330 . 1 63 . 14 LYS HA H 4.120 . 1 64 . 14 LYS HB2 H 1.640 . 2 65 . 15 HIS H H 7.740 . 1 66 . 15 HIS HA H 4.150 . 1 67 . 15 HIS HB2 H 2.490 . 2 68 . 15 HIS HB3 H 2.170 . 2 69 . 15 HIS HD2 H 6.870 . 2 70 . 16 LYS H H 7.460 . 1 71 . 16 LYS HA H 4.880 . 1 72 . 16 LYS HB2 H 1.830 . 2 73 . 16 LYS HB3 H 1.400 . 2 74 . 16 LYS HD2 H 1.600 . 2 75 . 16 LYS HG2 H 1.340 . 2 76 . 16 LYS HE2 H 3.180 . 2 77 . 17 ASP H H 8.090 . 1 78 . 17 ASP HA H 4.930 . 1 79 . 17 ASP HB2 H 3.100 . 2 80 . 17 ASP HB3 H 2.640 . 2 81 . 18 SER H H 7.310 . 1 82 . 19 LYS H H 8.030 . 1 83 . 19 LYS HA H 4.220 . 1 84 . 19 LYS HB2 H 1.860 . 2 85 . 19 LYS HG2 H 1.410 . 2 86 . 20 SER H H 7.430 . 1 87 . 20 SER HA H 5.000 . 1 88 . 20 SER HB2 H 3.890 . 2 89 . 20 SER HB3 H 3.810 . 2 90 . 21 THR H H 8.790 . 1 91 . 21 THR HA H 4.510 . 1 92 . 21 THR HB H 3.650 . 1 93 . 21 THR HG2 H 0.980 . 1 94 . 22 TRP H H 8.790 . 1 95 . 22 TRP HA H 6.510 . 1 96 . 22 TRP HB2 H 3.240 . 2 97 . 22 TRP HB3 H 3.020 . 2 98 . 22 TRP HE3 H 6.800 . 1 99 . 22 TRP HZ3 H 5.940 . 1 100 . 22 TRP HH2 H 6.510 . 1 101 . 22 TRP HZ2 H 6.780 . 1 102 . 22 TRP HE1 H 8.930 . 1 103 . 23 VAL H H 9.030 . 1 104 . 23 VAL HA H 5.130 . 1 105 . 23 VAL HB H 2.300 . 1 106 . 23 VAL HG1 H 1.150 . 1 107 . 23 VAL HG2 H 1.060 . 1 108 . 24 ILE H H 8.510 . 1 109 . 24 ILE HA H 5.420 . 1 110 . 24 ILE HB H 1.830 . 1 111 . 24 ILE HG2 H 0.900 . 1 112 . 25 LEU H H 9.010 . 1 113 . 25 LEU HA H 4.940 . 1 114 . 25 LEU HB2 H 1.860 . 2 115 . 25 LEU HB3 H 1.250 . 2 116 . 25 LEU HG H 0.780 . 1 117 . 25 LEU HD1 H 0.610 . 2 118 . 25 LEU HD2 H -0.280 . 2 119 . 26 HIS H H 9.500 . 1 120 . 26 HIS HA H 4.100 . 1 121 . 26 HIS HB2 H 3.300 . 2 122 . 27 HIS H H 8.830 . 1 123 . 27 HIS HA H 4.030 . 1 124 . 27 HIS HB2 H 3.820 . 2 125 . 27 HIS HB3 H 3.400 . 2 126 . 27 HIS HD2 H 7.070 . 1 127 . 28 LYS H H 8.360 . 1 128 . 28 LYS HA H 4.970 . 1 129 . 28 LYS HB2 H 2.400 . 2 130 . 28 LYS HG2 H 1.600 . 2 131 . 28 LYS HD2 H 1.720 . 2 132 . 28 LYS HE2 H 3.160 . 2 133 . 29 VAL H H 8.570 . 1 134 . 29 VAL HA H 4.430 . 1 135 . 29 VAL HB H 1.300 . 1 136 . 29 VAL HG1 H 0.800 . 1 137 . 29 VAL HG2 H 0.290 . 1 138 . 30 TYR H H 9.350 . 1 139 . 30 TYR HA H 4.880 . 1 140 . 30 TYR HB2 H 3.010 . 2 141 . 30 TYR HB3 H 2.530 . 2 142 . 30 TYR HD1 H 7.220 . 1 143 . 30 TYR HE1 H 6.910 . 1 144 . 31 ASP H H 8.560 . 1 145 . 31 ASP HA H 5.230 . 1 146 . 31 ASP HB2 H 3.050 . 2 147 . 32 LEU H H 8.560 . 1 148 . 32 LEU HA H 4.370 . 1 149 . 32 LEU HB2 H 1.960 . 2 150 . 32 LEU HB3 H 1.710 . 2 151 . 32 LEU HG H 1.340 . 1 152 . 32 LEU HD1 H 0.840 . 2 153 . 32 LEU HD2 H 0.650 . 2 154 . 33 THR H H 8.700 . 1 155 . 33 THR HA H 3.590 . 1 156 . 33 THR HB H 4.290 . 1 157 . 33 THR HG2 H 1.300 . 1 158 . 34 LYS H H 9.070 . 1 159 . 34 LYS HA H 4.280 . 1 160 . 34 LYS HB2 H 2.100 . 2 161 . 34 LYS HB3 H 1.900 . 2 162 . 34 LYS HG2 H 1.610 . 2 163 . 34 LYS HD2 H 1.310 . 2 164 . 35 PHE H H 7.680 . 1 165 . 35 PHE HA H 4.390 . 1 166 . 35 PHE HB2 H 2.460 . 2 167 . 35 PHE HB3 H 2.090 . 2 168 . 35 PHE HD2 H 7.130 . 1 169 . 35 PHE HZ H 6.580 . 1 170 . 35 PHE HE2 H 6.290 . 1 171 . 36 LEU H H 7.110 . 1 172 . 36 LEU HA H 3.050 . 1 173 . 36 LEU HB2 H 1.880 . 2 174 . 36 LEU HB3 H 1.670 . 2 175 . 36 LEU HG H 1.180 . 1 176 . 36 LEU HD1 H 0.870 . 2 177 . 36 LEU HD2 H 0.600 . 2 178 . 37 GLU H H 7.620 . 1 179 . 37 GLU HA H 3.830 . 1 180 . 37 GLU HB2 H 1.920 . 2 181 . 37 GLU HB3 H 1.820 . 2 182 . 37 GLU HG2 H 2.110 . 2 183 . 38 GLU H H 7.030 . 1 184 . 38 GLU HA H 4.030 . 1 185 . 38 GLU HB2 H 1.830 . 2 186 . 38 GLU HB3 H 1.610 . 2 187 . 38 GLU HG2 H 2.110 . 2 188 . 38 GLU HG3 H 2.060 . 2 189 . 39 HIS H H 6.070 . 1 190 . 39 HIS HA H 2.480 . 1 191 . 39 HIS HB2 H 0.880 . 2 192 . 39 HIS HB3 H 0.460 . 2 193 . 39 HIS HD1 H 9.470 . 1 194 . 39 HIS HD2 H 1.470 . 1 195 . 39 HIS HE1 H 1.240 . 1 196 . 41 GLY H H 1.100 . 1 197 . 41 GLY HA2 H 3.960 . 2 198 . 41 GLY HA3 H 3.390 . 2 199 . 42 GLY H H 6.150 . 1 200 . 42 GLY HA2 H 4.000 . 2 201 . 42 GLY HA3 H 3.410 . 2 202 . 43 GLU H H 8.200 . 1 203 . 43 GLU HA H 3.580 . 1 204 . 43 GLU HB2 H 1.700 . 2 205 . 43 GLU HG2 H 1.930 . 2 206 . 44 GLU H H 8.390 . 1 207 . 44 GLU HA H 3.720 . 1 208 . 44 GLU HB2 H 2.040 . 2 209 . 44 GLU HG2 H 2.380 . 2 210 . 44 GLU HG3 H 2.320 . 2 211 . 45 VAL H H 8.260 . 1 212 . 45 VAL HA H 4.200 . 1 213 . 45 VAL HB H 2.620 . 1 214 . 45 VAL HG1 H 1.090 . 2 215 . 45 VAL HG2 H 1.010 . 2 216 . 46 LEU H H 6.010 . 1 217 . 46 LEU HA H 3.910 . 1 218 . 46 LEU HB2 H 1.480 . 2 219 . 46 LEU HB3 H 0.640 . 2 220 . 46 LEU HG H 0.250 . 1 221 . 46 LEU HD1 H -0.670 . 1 222 . 47 ARG H H 8.010 . 1 223 . 47 ARG HA H 3.790 . 1 224 . 47 ARG HB2 H 1.800 . 2 225 . 47 ARG HB3 H 1.470 . 2 226 . 47 ARG HD2 H 3.070 . 2 227 . 48 GLU H H 8.060 . 1 228 . 48 GLU HA H 4.120 . 1 229 . 48 GLU HB2 H 2.200 . 2 230 . 48 GLU HB3 H 1.770 . 2 231 . 48 GLU HG2 H 2.520 . 2 232 . 49 GLN H H 7.170 . 1 233 . 49 GLN HA H 4.620 . 1 234 . 49 GLN HB2 H 2.030 . 2 235 . 49 GLN HB3 H 1.710 . 2 236 . 49 GLN HG2 H 3.110 . 2 237 . 49 GLN HG3 H 2.760 . 2 238 . 50 ALA H H 7.240 . 1 239 . 50 ALA HA H 4.280 . 1 240 . 50 ALA HB H 1.700 . 1 241 . 51 GLY H H 9.660 . 1 242 . 51 GLY HA2 H 4.030 . 2 243 . 51 GLY HA3 H 3.820 . 2 244 . 52 GLY H H 7.730 . 1 245 . 52 GLY HA2 H 4.450 . 2 246 . 52 GLY HA3 H 3.950 . 2 247 . 53 ASP H H 8.590 . 1 248 . 53 ASP HA H 5.230 . 1 249 . 53 ASP HB2 H 3.030 . 2 250 . 53 ASP HB3 H 2.510 . 2 251 . 54 ALA H H 9.210 . 1 252 . 54 ALA HA H 5.240 . 1 253 . 54 ALA HB H 1.860 . 1 254 . 55 THR H H 8.340 . 1 255 . 55 THR HA H 3.390 . 1 256 . 55 THR HB H 4.110 . 1 257 . 55 THR HG2 H 0.570 . 1 258 . 56 GLU H H 8.800 . 1 259 . 56 GLU HA H 3.930 . 1 260 . 56 GLU HB3 H 2.020 . 2 261 . 56 GLU HB2 H 2.310 . 2 262 . 56 GLU HG2 H 3.040 . 2 263 . 56 GLU HG3 H 2.840 . 2 264 . 57 ASN H H 8.010 . 1 265 . 57 ASN HA H 4.530 . 1 266 . 58 PHE H H 8.830 . 1 267 . 58 PHE HA H 3.240 . 1 268 . 58 PHE HB3 H 2.930 . 2 269 . 58 PHE HB2 H 3.110 . 2 270 . 58 PHE HD1 H 6.150 . 1 271 . 58 PHE HE1 H 5.450 . 1 272 . 58 PHE HZ H 5.830 . 1 273 . 59 GLU H H 8.480 . 1 274 . 59 GLU HA H 3.710 . 1 275 . 59 GLU HB2 H 2.580 . 2 276 . 59 GLU HB3 H 1.980 . 2 277 . 60 ASP H H 7.810 . 1 278 . 60 ASP HA H 4.280 . 1 279 . 60 ASP HB2 H 2.790 . 2 280 . 60 ASP HB3 H 2.620 . 2 281 . 61 VAL H H 6.650 . 1 282 . 61 VAL HA H 3.240 . 1 283 . 61 VAL HB H 0.660 . 1 284 . 61 VAL HG1 H 0.280 . 1 285 . 61 VAL HG2 H -1.280 . 1 286 . 62 GLY H H 6.480 . 1 287 . 62 GLY HA2 H 3.720 . 2 288 . 62 GLY HA3 H 3.400 . 2 289 . 63 HIS H H 6.810 . 1 290 . 63 HIS HA H 2.810 . 1 291 . 63 HIS HB2 H 1.150 . 2 292 . 63 HIS HB3 H 0.720 . 2 293 . 63 HIS HD2 H 0.720 . 1 294 . 63 HIS HE1 H 1.000 . 1 295 . 64 SER H H 8.840 . 1 296 . 64 SER HA H 4.200 . 1 297 . 64 SER HB2 H 4.070 . 1 298 . 64 SER HB3 H 4.070 . 1 299 . 65 THR H H 8.330 . 1 300 . 66 ASP H H 8.350 . 1 301 . 66 ASP HA H 4.200 . 1 302 . 66 ASP HB2 H 2.770 . 1 303 . 67 VAL H H 7.620 . 1 304 . 67 VAL HA H 3.970 . 1 305 . 67 VAL HB H 1.860 . 1 306 . 67 VAL HG1 H 0.950 . 2 307 . 67 VAL HG2 H 0.280 . 2 308 . 68 ARG H H 7.790 . 1 309 . 68 ARG HA H 3.890 . 1 310 . 68 ARG HB2 H 1.920 . 1 311 . 68 ARG HB3 H 1.920 . 1 312 . 68 ARG HD2 H 1.560 . 2 313 . 69 GLU H H 7.720 . 1 314 . 69 GLU HA H 3.900 . 1 315 . 69 GLU HB2 H 1.910 . 2 316 . 69 GLU HG2 H 2.400 . 2 317 . 69 GLU HG3 H 2.200 . 2 318 . 70 LEU H H 8.030 . 1 319 . 70 LEU HA H 4.390 . 1 320 . 70 LEU HB2 H 1.870 . 2 321 . 70 LEU HB3 H 1.760 . 2 322 . 70 LEU HG H 1.440 . 1 323 . 71 SER H H 8.780 . 1 324 . 71 SER HA H 4.470 . 1 325 . 71 SER HB2 H 3.820 . 1 326 . 71 SER HB3 H 3.820 . 1 327 . 72 LYS H H 7.370 . 1 328 . 72 LYS HA H 4.190 . 1 329 . 72 LYS HB2 H 2.190 . 2 330 . 72 LYS HB3 H 2.020 . 2 331 . 72 LYS HG2 H 1.570 . 2 332 . 72 LYS HD2 H 1.810 . 2 333 . 73 THR H H 7.600 . 1 334 . 73 THR HA H 3.790 . 1 335 . 73 THR HB H 4.000 . 1 336 . 73 THR HG2 H 0.920 . 1 337 . 74 TYR H H 7.670 . 1 338 . 74 TYR HA H 4.160 . 1 339 . 74 TYR HB2 H 2.830 . 2 340 . 74 TYR HB3 H 2.420 . 2 341 . 74 TYR HD2 H 7.260 . 1 342 . 74 TYR HE1 H 6.550 . 1 343 . 75 ILE H H 7.090 . 1 344 . 75 ILE HA H 3.780 . 1 345 . 75 ILE HB H 1.660 . 1 346 . 75 ILE HD1 H 0.950 . 1 347 . 75 ILE HG2 H -0.030 . 1 348 . 76 ILE H H 8.960 . 1 349 . 76 ILE HA H 4.270 . 1 350 . 76 ILE HB H 1.920 . 1 351 . 76 ILE HG12 H 0.170 . 2 352 . 76 ILE HG13 H 0.400 . 2 353 . 76 ILE HG2 H 0.840 . 1 354 . 76 ILE HD1 H -0.950 . 1 355 . 77 GLY H H 7.450 . 1 356 . 77 GLY HA2 H 4.530 . 2 357 . 77 GLY HA3 H 4.210 . 2 358 . 78 GLU H H 9.060 . 1 359 . 78 GLU HA H 5.290 . 1 360 . 78 GLU HB2 H 1.860 . 2 361 . 78 GLU HG2 H 2.400 . 2 362 . 78 GLU HG3 H 2.310 . 2 363 . 79 LEU H H 8.790 . 1 364 . 79 LEU HA H 4.930 . 1 365 . 79 LEU HB2 H 1.900 . 2 366 . 79 LEU HG H 1.170 . 1 367 . 79 LEU HD1 H 1.020 . 2 368 . 79 LEU HD2 H 0.770 . 2 369 . 80 HIS H H 9.080 . 1 370 . 80 HIS HA H 3.870 . 1 371 . 80 HIS HB2 H 2.970 . 2 372 . 80 HIS HB3 H 2.680 . 2 373 . 80 HIS HD2 H 7.030 . 1 374 . 81 PRO HA H 3.830 . 1 375 . 81 PRO HB2 H 1.810 . 2 376 . 81 PRO HG2 H 1.610 . 2 377 . 81 PRO HD2 H 2.980 . 2 378 . 81 PRO HD3 H 2.230 . 2 379 . 82 ASP H H 11.010 . 1 380 . 82 ASP HA H 4.540 . 1 381 . 82 ASP HB2 H 1.810 . 2 382 . 82 ASP HB3 H 1.620 . 2 383 . 83 ASP H H 8.170 . 1 384 . 83 ASP HA H 4.990 . 1 385 . 83 ASP HB2 H 2.990 . 2 386 . 83 ASP HB3 H 2.730 . 2 387 . 84 ARG H H 7.370 . 1 388 . 84 ARG HA H 4.060 . 1 389 . 84 ARG HB2 H 1.860 . 2 390 . 84 ARG HG2 H 1.350 . 2 391 . 86 LYS H H 7.580 . 1 392 . 86 LYS HA H 4.230 . 1 393 . 86 LYS HB2 H 1.890 . 2 394 . 87 ILE H H 7.290 . 1 395 . 87 ILE HA H 4.280 . 1 396 . 87 ILE HB H 2.010 . 1 397 . 87 ILE HG12 H 0.880 . 1 398 . 87 ILE HG13 H 0.880 . 1 399 . 87 ILE HD1 H 0.860 . 1 400 . 88 ALA H H 7.780 . 1 401 . 88 ALA HA H 4.340 . 1 402 . 88 ALA HB H 1.360 . 1 403 . 89 LYS H H 8.220 . 1 404 . 89 LYS HA H 3.830 . 1 stop_ save_ save_chemical_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HEM _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 HEM HHA H 9.460 . 1 2 . 1 HEM HHB H 9.960 . 1 3 . 1 HEM HHC H 9.380 . 1 4 . 1 HEM HHD H 9.840 . 1 5 . 1 HEM HAB H 7.430 . 1 6 . 1 HEM HAC H 8.290 . 1 7 . 1 HEM HBB H 5.380 . 1 8 . 1 HEM HBBA H 5.080 . 1 9 . 1 HEM HBC H 6.030 . 1 10 . 1 HEM HBCA H 5.920 . 1 11 . 1 HEM HMA H 3.740 . 1 12 . 1 HEM HMB H 3.290 . 1 13 . 1 HEM HMC H 3.430 . 1 14 . 1 HEM HMD H 3.560 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_J-values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'CYTOCHROME B5' _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 4 VAL H 4 VAL HA 4.641162458 . . . 2 3JHNHA 5 LYS H 5 LYS HA 7.672058338 . . . 3 3JHNHA 6 TYR H 6 TYR HA 8.543777926 . . . 4 3JHNHA 7 TYR H 7 TYR HA 8.99807317 . . . 5 3JHNHA 8 THR H 8 THR HA 6.557057743 . . . 6 3JHNHA 9 LEU H 9 LEU HA 7.657888533 . . . 7 3JHNHA 10 GLU H 10 GLU HA 4.475954864 . . . 8 3JHNHA 11 GLU H 11 GLU HA 5.816874136 . . . 9 3JHNHA 13 GLN H 13 GLN HA 4.339509797 . . . 10 3JHNHA 15 HIS H 15 HIS HA 10.81564842 . . . 11 3JHNHA 16 LYS H 16 LYS HA 7.604317779 . . . 12 3JHNHA 17 ASP H 17 ASP HA 8.720089332 . . . 13 3JHNHA 19 LYS H 19 LYS HA 6.061375101 . . . 14 3JHNHA 20 SER H 20 SER HA 4.263617241 . . . 15 3JHNHA 21 THR H 21 THR HA 9.20907726 . . . 16 3JHNHA 22 TRP H 22 TRP HA 8.617551637 . . . 17 3JHNHA 23 VAL H 23 VAL HA 7.699456669 . . . 18 3JHNHA 24 ILE H 24 ILE HA 8.33140751 . . . 19 3JHNHA 25 LEU H 25 LEU HA 7.646741854 . . . 20 3JHNHA 27 HIS H 27 HIS HA 6.440563975 . . . 21 3JHNHA 28 LYS H 28 LYS HA 7.401927516 . . . 22 3JHNHA 29 VAL H 29 VAL HA 7.542333564 . . . 23 3JHNHA 30 TYR H 30 TYR HA 8.799279228 . . . 24 3JHNHA 31 ASP H 31 ASP HA 9.883303215 . . . 25 3JHNHA 32 LEU H 32 LEU HA 5.578614284 . . . 26 3JHNHA 35 PHE H 35 PHE HA 7.215802248 . . . 27 3JHNHA 37 GLU H 37 GLU HA 5.530046527 . . . 28 3JHNHA 38 GLU H 38 GLU HA 11.53929474 . . . 29 3JHNHA 42 GLY H 42 GLY HA 3.666247284 . . . 30 3JHNHA 43 GLU H 43 GLU HA 3.640730657 . . . 31 3JHNHA 44 GLU H 44 GLU HA 3.12002994 . . . 32 3JHNHA 45 VAL H 45 VAL HA 4.303926022 . . . 33 3JHNHA 46 LEU H 46 LEU HA 9.207297434 . . . 34 3JHNHA 47 ARG H 47 ARG HA 3.692492348 . . . 35 3JHNHA 48 GLU H 48 GLU HA 3.420957519 . . . 36 3JHNHA 49 GLN H 49 GLN HA 10.59884224 . . . 37 3JHNHA 50 ALA H 50 ALA HA 2.431869593 . . . 38 3JHNHA 51 GLY H 51 GLY HA 6.197573922 . . . 39 3JHNHA 52 GLY H 52 GLY HA 5.575487613 . . . 40 3JHNHA 53 ASP H 53 ASP HA 7.313492828 . . . 41 3JHNHA 54 ALA H 54 ALA HA 9.1516409 . . . 42 3JHNHA 57 ASN H 57 ASN HA 4.688339094 . . . 43 3JHNHA 58 PHE H 58 PHE HA 4.935960059 . . . 44 3JHNHA 59 GLU H 59 GLU HA 4.418695491 . . . 45 3JHNHA 60 ASP H 60 ASP HA 5.446915259 . . . 46 3JHNHA 61 VAL H 61 VAL HA 4.924107432 . . . 47 3JHNHA 62 GLY H 62 GLY HA 6.42276501 . . . 48 3JHNHA 63 HIS H 63 HIS HA 4.618437639 . . . 49 3JHNHA 64 SER H 64 SER HA 3.733765579 . . . 50 3JHNHA 66 ASP H 66 ASP HA 5.626838378 . . . 51 3JHNHA 67 VAL H 67 VAL HA 4.641162458 . . . 52 3JHNHA 68 ARG H 68 ARG HA 4.190359647 . . . 53 3JHNHA 70 LEU H 70 LEU HA 5.006721727 . . . 54 3JHNHA 71 SER H 71 SER HA 3.09618929 . . . 55 3JHNHA 72 LYS H 72 LYS HA 4.928574905 . . . 56 3JHNHA 73 THR H 73 THR HA 4.003079652 . . . 57 3JHNHA 74 TYR H 74 TYR HA 6.901804128 . . . 58 3JHNHA 75 ILE H 75 ILE HA 3.550772578 . . . 59 3JHNHA 77 GLY H 77 GLY HA 3.985897901 . . . 60 3JHNHA 78 GLU H 78 GLU HA 10.88974153 . . . 61 3JHNHA 79 LEU H 79 LEU HA 4.675362521 . . . 62 3JHNHA 82 ASP H 82 ASP HA 5.781285897 . . . 63 3JHNHA 83 ASP H 83 ASP HA 7.239402594 . . . 64 3JHNHA 84 ARG H 84 ARG HA 5.236904537 . . . 65 3JHNHA 86 LYS H 86 LYS HA 10.82036887 . . . 66 3JHNHA 88 ALA H 88 ALA HA 7.487396457 . . . stop_ save_