data_4806 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shifts of bovine ferric cytochrome b5 ; _BMRB_accession_number 4806 _BMRB_flat_file_name bmr4806.str _Entry_type original _Submission_date 2000-08-14 _Accession_date 2000-08-14 _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 Hom Kellie . . 2 Ma Qi-Feng . . 3 Wolfe Gary . . 4 Zhang Hong . . 5 Storch Elizabeth M . 6 Daggett Valerie . . 7 Basus Vladimir J . 8 Waskell Lucy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 116 "13C chemical shifts" 90 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-11-15 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4803 'cyt b5 red' 4804 'cyt b5 N17D red' 4805 'cyt b5 N17D oxid - cyt c oxid complex' 4807 'cyt b5 N17D oxid' 4808 'cyt b5 red - cyt c red complex' 4809 'cyt b5 N17D red - cyt c red complex' 4810 'cyt b5 oxid - cyt c oxid complex' stop_ _Original_release_date 2000-11-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Studies of the Association of Cytochrome b5 with Cytochrome c' _Citation_status 'in press' _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 Hom Kellie . . 2 Ma Qi-Feng . . 3 Wolfe Gary . . 4 Zhang Hong . . 5 Storch Elizabeth M . 6 Daggett Valerie . . 7 Basus Vladimir J . 8 Waskell Lucy . . stop_ _Journal_abbreviation Biochemistry _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 'bovine cytochrome b5' 'heteronuclear NMR' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293 ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_cytb5 _Saveframe_category molecular_system _Mol_system_name 'bovine ferric cytochrome b5' _Abbreviation_common 'oxidized cytb5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cytb5 $cytb5 heme $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_cytb5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ferric cytochrome b5' _Abbreviation_common cytb5 _Molecular_mass 9966 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; AVKYYTLEEIQKHNNSKSTW LILHYKVYDLTKFLEEHPGG EEVLREQAGGDATENFEDVG HSTDARELSKTFIIGELHPD DR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 3 ALA 2 4 VAL 3 5 LYS 4 6 TYR 5 7 TYR 6 8 THR 7 9 LEU 8 10 GLU 9 11 GLU 10 12 ILE 11 13 GLN 12 14 LYS 13 15 HIS 14 16 ASN 15 17 ASN 16 18 SER 17 19 LYS 18 20 SER 19 21 THR 20 22 TRP 21 23 LEU 22 24 ILE 23 25 LEU 24 26 HIS 25 27 TYR 26 28 LYS 27 29 VAL 28 30 TYR 29 31 ASP 30 32 LEU 31 33 THR 32 34 LYS 33 35 PHE 34 36 LEU 35 37 GLU 36 38 GLU 37 39 HIS 38 40 PRO 39 41 GLY 40 42 GLY 41 43 GLU 42 44 GLU 43 45 VAL 44 46 LEU 45 47 ARG 46 48 GLU 47 49 GLN 48 50 ALA 49 51 GLY 50 52 GLY 51 53 ASP 52 54 ALA 53 55 THR 54 56 GLU 55 57 ASN 56 58 PHE 57 59 GLU 58 60 ASP 59 61 VAL 60 62 GLY 61 63 HIS 62 64 SER 63 65 THR 64 66 ASP 65 67 ALA 66 68 ARG 67 69 GLU 68 70 LEU 69 71 SER 70 72 LYS 71 73 THR 72 74 PHE 73 75 ILE 74 76 ILE 75 77 GLY 76 78 GLU 77 79 LEU 78 80 HIS 79 81 PRO 80 82 ASP 81 83 ASP 82 84 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 2.65e-52 BMRB 1324 "cytochrome b5" 100.00 82 100.00 100.00 2.65e-52 BMRB 17457 b5 100.00 104 100.00 100.00 6.81e-53 BMRB 4803 cytb5 100.00 82 100.00 100.00 2.65e-52 BMRB 4804 cytb5-N17D 100.00 82 98.78 100.00 1.52e-51 BMRB 4807 cytb5-N17D 100.00 82 98.78 100.00 1.52e-51 BMRB 5745 Cyt-b5 100.00 104 100.00 100.00 6.81e-53 BMRB 6131 TB5 100.00 82 98.78 98.78 5.14e-51 PDB 1CYO "Bovine Cytochrome B(5)" 100.00 93 100.00 100.00 1.02e-52 PDB 1EHB "Crystal Structure Of Recombinant Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 100.00 100.00 2.65e-52 PDB 1ES1 "Crystal Structure Of Val61his Mutant Of Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 98.78 98.78 5.14e-51 PDB 1HKO "Nmr Structure Of Bovine Cytochrome B5" 100.00 104 100.00 100.00 7.19e-53 PDB 1J0Q "Solution Structure Of Oxidized Bovine Microsomal Cytochrome B5 Mutant V61h" 98.78 82 98.77 98.77 3.31e-50 PDB 1LQX "Crystal Structure Of V45e Mutant Of Cytochrome B5" 100.00 82 98.78 98.78 3.36e-51 PDB 1LR6 "Crystal Structure Of V45y Mutant Of Cytochrome B5" 100.00 82 98.78 98.78 2.15e-51 PDB 1M20 "Crystal Structure Of F35y Mutant Of Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 98.78 100.00 8.79e-52 PDB 1M2I "Crystal Structure Of E44aE56A MUTANT OF CYTOCHROME B5" 100.00 82 97.56 97.56 5.60e-51 PDB 1M59 "Crystal Structure Of P40v Mutant Of Trypsin-Solubilized Fragment Of Cytochrome B5" 100.00 82 98.78 98.78 5.14e-51 PDB 1NX7 "Solution Structure Of Oxidized Bovine Microsomal Cytochrome B5" 100.00 82 100.00 100.00 2.65e-52 PDB 1SH4 "Solution Structure Of Oxidized Bovine Microsomal Cytochrome B5 Mutant V45h" 100.00 82 98.78 98.78 5.14e-51 PDB 1U9M "Crystal Structure Of F58w Mutant Of Cytochrome B5" 100.00 82 98.78 100.00 1.82e-51 PDB 1U9U "Crystal Structure Of F58y Mutant Of Cytochrome B5" 100.00 82 98.78 100.00 8.79e-52 PDB 4HIN "2.4a Resolution Structure Of Bovine Cytochrome B5 (s71l)" 100.00 82 98.78 98.78 2.88e-51 EMBL CAA31949 "unnamed protein product [Bos taurus]" 100.00 134 100.00 100.00 1.86e-52 GB AAA72186 "microsomal cytochrome b-5 [synthetic construct]" 100.00 94 97.56 98.78 3.43e-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 1.45e-50 GB AAC14455 "cytochrome b-5 [Bos taurus]" 100.00 98 100.00 100.00 5.51e-53 GB AAC48779 "cytochrome b5 [Sus scrofa]" 100.00 134 98.78 100.00 8.61e-52 GB AAC48780 "cytochrome b5 [Sus scrofa]" 73.17 69 98.33 100.00 2.17e-34 PRF 1106188A "cytochrome b5" 100.00 97 100.00 100.00 8.27e-53 PRF 1106188C "cytochrome b5" 100.00 97 98.78 100.00 6.07e-52 PRF 1803548B "cytochrome b5" 100.00 134 100.00 100.00 1.86e-52 REF NP_001001770 "cytochrome b5 [Sus scrofa]" 100.00 134 98.78 100.00 8.61e-52 REF NP_001159663 "cytochrome b5 [Ovis aries]" 98.78 134 98.77 100.00 6.65e-51 REF NP_001180227 "cytochrome b5 [Canis lupus familiaris]" 98.78 134 97.53 100.00 5.91e-50 REF NP_001274163 "cytochrome b5 [Capra hircus]" 98.78 134 98.77 100.00 6.65e-51 REF NP_776458 "cytochrome b5 [Bos taurus]" 100.00 134 100.00 100.00 1.86e-52 SP P00171 "RecName: Full=Cytochrome b5 [Bos taurus]" 100.00 134 100.00 100.00 1.86e-52 SP P00172 "RecName: Full=Cytochrome b5 [Sus scrofa]" 100.00 134 98.78 100.00 8.61e-52 TPG DAA15965 "TPA: cytochrome b5 [Bos taurus]" 100.00 134 100.00 100.00 1.86e-52 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 Wed Jul 20 13:45:53 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 $cytb5 bovine 9913 Eukaryota Metazoa Bos taurus 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 _Vendor_name $cytb5 'recombinant technology' 'Escherichia coli' . . BL21(DE3) pUC19 Novagen $HEM vendor . . . . . Sigma 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 $cytb5 0.3 mM '[U-90% 13C; U-90% 15N]' $HEM 0.3 mM . stop_ save_ ############################ # Computer software used # ############################ save_Striker _Saveframe_category software _Name Striker _Version . loop_ _Task 'FID transformation' stop_ _Details 'In-house developed software for NMR data processing' _Citation_label $ref_1 save_ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task 'FID transformation' stop_ _Details . _Citation_label $ref_2 save_ save_Sparky _Saveframe_category software _Name Sparky _Version 3.3.2 loop_ _Task 'Spectral analysis' stop_ _Details 'In-house developed software for spectral analysis' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_13C-1H_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H HSQC' _Sample_label $sample_1 save_ save_(HB)CB(CGCD)HD_3 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCD)HD _Sample_label $sample_1 save_ save_(HB)CB(CGCDCE)HE_4 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCDCE)HE _Sample_label $sample_1 save_ save_1H-TOCSY-relayed_ct-[13C,_1H]-HMQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-TOCSY-relayed ct-[13C, 1H]-HMQC' _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NNH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _Sample_label $sample_1 save_ save_HBHA(CO)NNH_10 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NNH _Sample_label $sample_1 save_ save_HCCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_ct-HCACO_12 _Saveframe_category NMR_applied_experiment _Experiment_name ct-HCACO _Sample_label $sample_1 save_ save_13C-edited_NOESY-HMQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY-HMQC' _Sample_label $sample_1 save_ save_15N-edited_NOESY-HMQC_14 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HMQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.5 0.2 n/a temperature 298 1 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 . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name cytb5 _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 VAL H H 8.67 . 1 2 . 2 VAL HA H 3.82 . 1 3 . 2 VAL HB H 1.59 . 1 4 . 2 VAL HG1 H 0.66 . 2 5 . 2 VAL HG2 H 0.33 . 2 6 . 2 VAL CA C 61.8 . 1 7 . 2 VAL CB C 33.1 . 1 8 . 2 VAL N N 112.57 . 1 9 . 3 LYS H H 8.10 . 1 10 . 3 LYS HA H 4.08 . 1 11 . 3 LYS HB2 H 1.64 . 1 12 . 3 LYS HB3 H 1.64 . 1 13 . 3 LYS HG2 H 1.14 . 2 14 . 3 LYS HG3 H 0.97 . 2 15 . 3 LYS HD2 H 1.60 . 1 16 . 3 LYS HD3 H 1.60 . 1 17 . 3 LYS HE2 H 2.88 . 2 18 . 3 LYS HE3 H 2.75 . 2 19 . 3 LYS CA C 54.94 . 1 20 . 3 LYS CB C 33.1 . 1 21 . 3 LYS CG C 24.6 . 1 22 . 3 LYS CD C 28.7 . 1 23 . 3 LYS CE C 42.2 . 1 24 . 3 LYS N N 127.11 . 1 25 . 4 TYR H H 8.22 . 1 26 . 4 TYR HA H 5.70 . 1 27 . 4 TYR HB2 H 2.88 . 2 28 . 4 TYR HB3 H 2.70 . 2 29 . 4 TYR CA C 55.24 . 1 30 . 4 TYR N N 122.90 . 1 31 . 5 TYR H H 8.69 . 1 32 . 5 TYR HA H 5.23 . 1 33 . 5 TYR HB2 H 3.26 . 2 34 . 5 TYR HB3 H 2.56 . 2 35 . 5 TYR CA C 56.77 . 1 36 . 5 TYR CB C 42.7 . 1 37 . 5 TYR N N 118.39 . 1 38 . 6 THR H H 9.37 . 1 39 . 6 THR CA C 60.48 . 1 40 . 6 THR N N 115.72 . 1 41 . 7 LEU H H 9.50 . 1 42 . 7 LEU CA C 58.27 . 1 43 . 7 LEU N N 124.06 . 1 44 . 8 GLU H H 8.42 . 1 45 . 8 GLU CA C 59.25 . 1 46 . 8 GLU N N 116.93 . 1 47 . 9 GLU H H 7.62 . 1 48 . 9 GLU CA C 58.97 . 1 49 . 9 GLU N N 118.17 . 1 50 . 10 ILE H H 8.40 . 1 51 . 10 ILE CA C 65.50 . 1 52 . 10 ILE N N 121.54 . 1 53 . 11 GLN H H 8.21 . 1 54 . 11 GLN CA C 57.77 . 1 55 . 11 GLN N N 115.46 . 1 56 . 12 LYS H H 7.07 . 1 57 . 12 LYS CA C 56.65 . 1 58 . 12 LYS N N 114.35 . 1 59 . 13 HIS H H 7.69 . 1 60 . 13 HIS CA C 53.60 . 1 61 . 13 HIS CE1 C 134.56 . 1 62 . 13 HIS N N 121.50 . 1 63 . 14 ASN H H 7.31 . 1 64 . 14 ASN HB2 H 2.92 . 2 65 . 14 ASN HB3 H 2.19 . 2 66 . 14 ASN CA C 51.44 . 1 67 . 14 ASN N N 117.32 . 1 68 . 15 ASN H H 8.39 . 1 69 . 15 ASN HA H 4.55 . 1 70 . 15 ASN HB2 H 2.81 . 2 71 . 15 ASN HB3 H 2.67 . 2 72 . 15 ASN CA C 52.72 . 1 73 . 15 ASN CB C 40.8 . 1 74 . 15 ASN N N 126.50 . 1 75 . 16 SER H H 8.18 . 1 76 . 16 SER CA C 60.84 . 1 77 . 16 SER N N 113.13 . 1 78 . 17 LYS H H 7.94 . 1 79 . 17 LYS N N 119.85 . 1 80 . 18 SER CA C 57.83 . 1 81 . 19 THR H H 8.78 . 1 82 . 19 THR CA C 62.42 . 1 83 . 19 THR N N 123.30 . 1 84 . 20 TRP H H 8.71 . 1 85 . 20 TRP HA H 6.22 . 1 86 . 20 TRP HB2 H 3.01 . 2 87 . 20 TRP HB3 H 2.73 . 2 88 . 20 TRP CA C 52.20 . 1 89 . 20 TRP CB C 33.3 . 1 90 . 20 TRP N N 126.42 . 1 91 . 21 LEU H H 8.39 . 1 92 . 21 LEU CA C 54.35 . 1 93 . 21 LEU N N 115.58 . 1 94 . 22 ILE H H 7.98 . 1 95 . 22 ILE CA C 59.64 . 1 96 . 22 ILE N N 120.50 . 1 97 . 23 LEU H H 8.35 . 1 98 . 23 LEU HD1 H -0.82 . 2 99 . 23 LEU HD2 H -2.12 . 2 100 . 23 LEU CA C 53.10 . 1 101 . 23 LEU N N 122.38 . 1 102 . 24 HIS H H 9.21 . 1 103 . 24 HIS HE1 H 8.32 . 1 104 . 24 HIS CA C 56.78 . 1 105 . 24 HIS CE1 C 137.91 . 1 106 . 24 HIS N N 124.83 . 1 107 . 25 TYR H H 8.22 . 1 108 . 25 TYR CA C 60.45 . 1 109 . 25 TYR N N 106.95 . 1 110 . 26 LYS H H 8.24 . 1 111 . 26 LYS CA C 55.75 . 1 112 . 26 LYS N N 121.80 . 1 113 . 27 VAL H H 8.29 . 1 114 . 27 VAL HA H 4.07 . 1 115 . 27 VAL HG1 H 0.05 . 1 116 . 27 VAL HG2 H 0.05 . 1 117 . 27 VAL CA C 61.54 . 1 118 . 27 VAL N N 121.08 . 1 119 . 28 TYR H H 8.92 . 1 120 . 28 TYR CA C 55.90 . 1 121 . 28 TYR N N 126.47 . 1 122 . 29 ASP H H 8.06 . 1 123 . 29 ASP CA C 52.72 . 1 124 . 29 ASP N N 119.31 . 1 125 . 30 LEU H H 8.40 . 1 126 . 30 LEU HA H 4.31 . 1 127 . 30 LEU HB2 H 1.57 . 2 128 . 30 LEU HB3 H 1.28 . 2 129 . 30 LEU HG H 0.95 . 1 130 . 30 LEU HD1 H -0.07 . 2 131 . 30 LEU HD2 H -0.58 . 2 132 . 30 LEU CA C 52.69 . 1 133 . 30 LEU CB C 42.1 . 1 134 . 30 LEU CG C 26.3 . 1 135 . 30 LEU CD1 C 27.0 . 2 136 . 30 LEU CD2 C 24.0 . 2 137 . 30 LEU N N 122.44 . 1 138 . 31 THR H H 8.69 . 1 139 . 31 THR CA C 69.04 . 1 140 . 31 THR N N 119.22 . 1 141 . 32 LYS H H 9.03 . 1 142 . 32 LYS CA C 57.41 . 1 143 . 32 LYS N N 117.20 . 1 144 . 33 PHE H H 8.13 . 1 145 . 33 PHE CA C 57.33 . 1 146 . 33 PHE N N 120.05 . 1 147 . 34 LEU H H 7.43 . 1 148 . 34 LEU CA C 58.31 . 1 149 . 34 LEU N N 113.14 . 1 150 . 35 GLU H H 8.35 . 1 151 . 35 GLU CA C 57.28 . 1 152 . 35 GLU N N 117.96 . 1 153 . 36 GLU H H 7.85 . 1 154 . 36 GLU CA C 60.43 . 1 155 . 36 GLU N N 119.25 . 1 156 . 37 HIS H H 8.66 . 1 157 . 37 HIS N N 120.84 . 1 158 . 39 GLY CA C 46.59 . 1 159 . 40 GLY H H 10.85 . 1 160 . 40 GLY CA C 46.88 . 1 161 . 40 GLY N N 113.06 . 1 162 . 41 GLU H H 10.15 . 1 163 . 41 GLU CA C 59.42 . 1 164 . 41 GLU N N 121.36 . 1 165 . 42 GLU H H 9.65 . 1 166 . 42 GLU CA C 61.70 . 1 167 . 42 GLU N N 124.18 . 1 168 . 43 VAL H H 9.47 . 1 169 . 43 VAL CA C 64.21 . 1 170 . 43 VAL N N 113.18 . 1 171 . 44 LEU H H 7.35 . 1 172 . 44 LEU CA C 56.03 . 1 173 . 44 LEU N N 116.19 . 1 174 . 45 ARG H H 8.91 . 1 175 . 45 ARG CA C 59.52 . 1 176 . 45 ARG N N 119.89 . 1 177 . 46 GLU H H 8.19 . 1 178 . 46 GLU CA C 58.52 . 1 179 . 46 GLU N N 116.66 . 1 180 . 47 GLN H H 6.60 . 1 181 . 47 GLN CA C 53.11 . 1 182 . 47 GLN N N 112.94 . 1 183 . 48 ALA H H 6.82 . 1 184 . 48 ALA CA C 53.29 . 1 185 . 48 ALA N N 120.81 . 1 186 . 49 GLY H H 9.38 . 1 187 . 49 GLY CA C 45.27 . 1 188 . 49 GLY N N 110.04 . 1 189 . 50 GLY H H 7.38 . 1 190 . 50 GLY CA C 44.41 . 1 191 . 50 GLY N N 104.64 . 1 192 . 51 ASP H H 8.21 . 1 193 . 51 ASP CA C 53.54 . 1 194 . 51 ASP N N 117.59 . 1 195 . 52 ALA H H 8.33 . 1 196 . 52 ALA CA C 49.74 . 1 197 . 52 ALA N N 130.41 . 1 198 . 53 THR H H 8.03 . 1 199 . 53 THR CA C 69.14 . 1 200 . 53 THR N N 117.57 . 1 201 . 54 GLU H H 8.50 . 1 202 . 54 GLU CA C 59.66 . 1 203 . 54 GLU N N 119.20 . 1 204 . 55 ASN H H 7.45 . 1 205 . 55 ASN CA C 55.78 . 1 206 . 55 ASN N N 116.36 . 1 207 . 56 PHE H H 7.94 . 1 208 . 56 PHE CA C 62.12 . 1 209 . 56 PHE N N 117.93 . 1 210 . 57 GLU H H 8.81 . 1 211 . 57 GLU CA C 59.12 . 1 212 . 57 GLU N N 119.75 . 1 213 . 58 ASP H H 8.94 . 1 214 . 58 ASP CA C 57.44 . 1 215 . 58 ASP N N 121.72 . 1 216 . 59 VAL H H 8.17 . 1 217 . 59 VAL CA C 65.47 . 1 218 . 59 VAL N N 116.03 . 1 219 . 60 GLY H H 9.04 . 1 220 . 60 GLY CA C 47.98 . 1 221 . 60 GLY N N 109.21 . 1 222 . 61 HIS H H 11.28 . 1 223 . 61 HIS CA C 80.78 . 1 224 . 61 HIS N N 119.77 . 1 225 . 62 SER H H 11.62 . 1 226 . 62 SER CA C 59.26 . 1 227 . 62 SER N N 125.27 . 1 228 . 63 THR H H 9.37 . 1 229 . 63 THR CA C 67.10 . 1 230 . 63 THR N N 116.79 . 1 231 . 64 ASP H H 8.37 . 1 232 . 64 ASP CA C 57.73 . 1 233 . 64 ASP N N 121.75 . 1 234 . 65 ALA H H 8.82 . 1 235 . 65 ALA CA C 56.04 . 1 236 . 65 ALA N N 124.72 . 1 237 . 66 ARG H H 9.11 . 1 238 . 66 ARG CA C 60.68 . 1 239 . 66 ARG N N 118.80 . 1 240 . 67 GLU H H 9.13 . 1 241 . 67 GLU N N 123.13 . 1 242 . 68 LEU CA C 57.67 . 1 243 . 69 SER H H 8.48 . 1 244 . 69 SER CA C 62.12 . 1 245 . 69 SER N N 114.54 . 1 246 . 70 LYS H H 7.20 . 1 247 . 70 LYS CA C 58.79 . 1 248 . 70 LYS N N 120.21 . 1 249 . 71 THR H H 7.64 . 1 250 . 71 THR CA C 63.99 . 1 251 . 71 THR N N 109.93 . 1 252 . 72 PHE H H 7.28 . 1 253 . 72 PHE CA C 56.76 . 1 254 . 72 PHE N N 117.95 . 1 255 . 73 ILE H H 6.76 . 1 256 . 73 ILE CA C 62.83 . 1 257 . 73 ILE N N 120.24 . 1 258 . 74 ILE H H 8.62 . 1 259 . 74 ILE CA C 60.80 . 1 260 . 74 ILE N N 119.66 . 1 261 . 75 GLY H H 7.31 . 1 262 . 75 GLY CA C 45.69 . 1 263 . 75 GLY N N 110.77 . 1 264 . 76 GLU H H 8.99 . 1 265 . 76 GLU CA C 54.70 . 1 266 . 76 GLU N N 118.61 . 1 267 . 77 LEU H H 8.88 . 1 268 . 77 LEU CA C 54.61 . 1 269 . 77 LEU N N 122.95 . 1 270 . 78 HIS H H 9.05 . 1 271 . 78 HIS HE1 H 7.53 . 1 272 . 78 HIS CE1 C 139.12 . 1 273 . 78 HIS N N 131.26 . 1 274 . 79 PRO CA C 65.72 . 1 275 . 80 ASP H H 11.12 . 1 276 . 80 ASP CA C 56.44 . 1 277 . 80 ASP N N 121.07 . 1 278 . 81 ASP H H 8.21 . 1 279 . 81 ASP CA C 54.49 . 1 280 . 81 ASP N N 118.81 . 1 281 . 82 ARG H H 6.99 . 1 282 . 82 ARG N N 124.30 . 1 stop_ save_