data_4759 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N and 13Calpha assigned chemical shifts for reduced Escherichia coli cytochrome b562 ; _BMRB_accession_number 4759 _BMRB_flat_file_name bmr4759.str _Entry_type original _Submission_date 2000-06-12 _Accession_date 2000-06-12 _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 Assfalg Michael . . 2 Banci Lucia . . 3 Bertini Ivano . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 89 "13C chemical shifts" 92 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-07-21 original author . stop_ _Original_release_date 2000-07-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 15N and 13Calpha assigned chemical shifts for reduced Escherichia coli cytochrome b56 ; _Citation_status 'in preparation' _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Assfalg Michael . . 2 Banci Lucia . . 3 Bertini Ivano . . 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 2000 _Details . save_ ################################## # Molecular system description # ################################## save_sytem_cyt_b562 _Saveframe_category molecular_system _Mol_system_name 'cytochrome b562' _Abbreviation_common 'cyt b562' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome b562' $cyt_b562 Fe-heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'electron transfer protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_b562 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome b562' _Abbreviation_common 'cyt b562' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; ADLEDNMETLNDNLKVIEKA DNAAQVKDALTKMRAAALDA QKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLAN EGKVKEAQAAAEQLKTTRNA YHQKYR ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 LEU 4 GLU 5 ASP 6 ASN 7 MET 8 GLU 9 THR 10 LEU 11 ASN 12 ASP 13 ASN 14 LEU 15 LYS 16 VAL 17 ILE 18 GLU 19 LYS 20 ALA 21 ASP 22 ASN 23 ALA 24 ALA 25 GLN 26 VAL 27 LYS 28 ASP 29 ALA 30 LEU 31 THR 32 LYS 33 MET 34 ARG 35 ALA 36 ALA 37 ALA 38 LEU 39 ASP 40 ALA 41 GLN 42 LYS 43 ALA 44 THR 45 PRO 46 PRO 47 LYS 48 LEU 49 GLU 50 ASP 51 LYS 52 SER 53 PRO 54 ASP 55 SER 56 PRO 57 GLU 58 MET 59 LYS 60 ASP 61 PHE 62 ARG 63 HIS 64 GLY 65 PHE 66 ASP 67 ILE 68 LEU 69 VAL 70 GLY 71 GLN 72 ILE 73 ASP 74 ASP 75 ALA 76 LEU 77 LYS 78 LEU 79 ALA 80 ASN 81 GLU 82 GLY 83 LYS 84 VAL 85 LYS 86 GLU 87 ALA 88 GLN 89 ALA 90 ALA 91 ALA 92 GLU 93 GLN 94 LEU 95 LYS 96 THR 97 THR 98 ARG 99 ASN 100 ALA 101 TYR 102 HIS 103 GLN 104 LYS 105 TYR 106 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 1672 "cytochrome b562" 100.00 106 100.00 100.00 2.05e-68 BMRB 4767 apo_b562 100.00 106 100.00 100.00 2.05e-68 PDB 1APC "Solution Structure Of Apocytochrome B562" 100.00 106 100.00 100.00 2.05e-68 PDB 1LM3 "A Multi-Generation Analysis Of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed " 99.06 106 98.10 99.05 5.16e-66 PDB 1M6T "Crystal Structure Of B562ril, A Redesigned Four Helix Bundle" 99.06 106 98.10 98.10 5.32e-65 PDB 1QPU "Solution Structure Of Oxidized Escherichia Coli Cytochrome B562" 100.00 106 100.00 100.00 2.05e-68 PDB 1QQ3 "The Solution Structure Of The Heme Binding Variant Arg98cys Of Oxidized Escherichia Coli Cytochrome B562" 100.00 106 99.06 99.06 3.34e-67 PDB 256B "Improvement Of The 2.5 Angstroms Resolution Model Of Cytochrome B562 By Redetermining The Primary Structure And Using Molecular" 100.00 106 100.00 100.00 2.05e-68 PDB 2BC5 "Crystal Structure Of E. Coli Cytochrome B562 With Engineered C-Type Heme Linkages" 100.00 106 97.17 97.17 2.80e-65 PDB 3U8P "Cytochrome B562 Integral Fusion With Egfp" 100.00 347 100.00 100.00 1.68e-65 PDB 4EA3 "Structure Of The NOFQ OPIOID RECEPTOR IN COMPLEX WITH A PEPTIDE Mimetic" 99.06 434 98.10 98.10 2.03e-64 PDB 4EIY "Crystal Structure Of The Chimeric Protein Of A2aar-Bril In Complex With Zm241385 At 1.8a Resolution" 99.06 447 98.10 98.10 2.74e-64 PDB 4IAQ "Crystal Structure Of The Chimeric Protein Of 5-ht1b-bril In Complex With Dihydroergotamine (psi Community Target)" 99.06 403 98.10 98.10 9.65e-65 PDB 4IAR "Crystal Structure Of The Chimeric Protein Of 5-ht1b-bril In Complex With Ergotamine (psi Community Target)" 99.06 401 98.10 98.10 9.18e-65 PDB 4IB4 "Crystal Structure Of The Chimeric Protein Of 5-ht2b-bril In Complex With Ergotamine" 99.06 430 98.10 98.10 5.39e-63 PDB 4JKV "Structure Of The Human Smoothened 7tm Receptor In Complex With An Antitumor Agent" 99.06 475 98.10 98.10 5.10e-64 PDB 4L6R "Structure Of The Class B Human Glucagon G Protein Coupled Receptor" 99.06 425 98.10 98.10 2.31e-64 PDB 4N4W "Structure Of The Human Smoothened Receptor In Complex With Sant-1" 99.06 475 98.10 98.10 5.10e-64 PDB 4N6H "1.8 A Structure Of The Human Delta Opioid 7tm Receptor (psi Community Target)" 99.06 414 98.10 98.10 1.26e-64 PDB 4NC3 "Crystal Structure Of The 5-ht2b Receptor Solved Using Serial Femtosecond Crystallography In Lipidic Cubic Phase" 99.06 430 98.10 98.10 5.39e-63 PDB 4NTJ "Structure Of The Human P2y12 Receptor In Complex With An Antithrombotic Drug" 99.06 466 98.10 98.10 4.35e-63 PDB 4O9R "Human Smoothened Receptor Structure In Complex With Cyclopamine" 99.06 468 98.10 98.10 4.38e-64 PDB 4OR2 "Human Class C G Protein-coupled Metabotropic Glutamate Receptor 1 In Complex With A Negative Allosteric Modulator" 99.06 389 98.10 98.10 6.81e-65 PDB 4PXZ "Crystal Structure Of P2y12 Receptor In Complex With 2mesadp" 99.06 466 98.10 98.10 4.35e-63 PDB 4PY0 "Crystal Structure Of P2y12 Receptor In Complex With 2mesatp" 99.06 466 98.10 98.10 4.35e-63 PDB 4QIM "Structure Of The Human Smoothened Receptor In Complex With Anta Xv" 99.06 468 98.10 98.10 4.38e-64 PDB 4QIN "Structure Of The Human Smoothened Receptor In Complex With Sag1.5" 99.06 468 98.10 98.10 4.38e-64 PDB 4RWA "Synchrotron Structure Of The Human Delta Opioid Receptor In Complex With A Bifunctional Peptide (psi Community Target)" 99.06 411 98.10 98.10 1.17e-64 PDB 4RWD "Xfel Structure Of The Human Delta Opioid Receptor In Complex With A Bifunctional Peptide" 99.06 411 98.10 98.10 1.17e-64 DBJ BAB38636 "cytochrome b(562) [Escherichia coli O157:H7 str. Sakai]" 94.34 100 97.00 100.00 4.92e-63 DBJ BAG80065 "cytochrome b562 [Escherichia coli SE11]" 100.00 128 100.00 100.00 4.66e-69 DBJ BAI28542 "cytochrome b562 [Escherichia coli O26:H11 str. 11368]" 98.11 130 99.04 99.04 7.30e-66 DBJ BAI33713 "cytochrome b562 [Escherichia coli O103:H2 str. 12009]" 100.00 128 99.06 99.06 2.73e-68 DBJ BAI38842 "cytochrome b562 [Escherichia coli O111:H- str. 11128]" 100.00 128 100.00 100.00 4.66e-69 EMBL CAA47706 "cytochrome b562 [Escherichia coli]" 100.00 128 100.00 100.00 4.66e-69 EMBL CAP78754 "Soluble cytochrome b562 [Escherichia coli LF82]" 100.00 128 97.17 98.11 2.23e-67 EMBL CAQ34585 "cytochrome b562 (soluble) [Escherichia coli BL21(DE3)]" 94.34 100 100.00 100.00 2.95e-64 EMBL CAQ91733 "soluble cytochrome b562 [Escherichia fergusonii ATCC 35469]" 100.00 128 98.11 99.06 6.38e-68 EMBL CAR01210 "soluble cytochrome b562 [Escherichia coli IAI1]" 100.00 128 100.00 100.00 4.66e-69 GB AAA97133 "cytochrome b562 [Escherichia coli str. K-12 substr. MG1655]" 94.34 100 97.00 100.00 4.92e-63 GB AAB20782 "cytochrome b562 [Escherichia coli]" 100.00 128 100.00 100.00 4.66e-69 GB AAG59433 "cytochrome b (562) [Escherichia coli O157:H7 str. EDL933]" 94.34 100 97.00 100.00 4.92e-63 GB AAN45672 "Soluble cytochrome B562 precursor [Shigella flexneri 2a str. 301]" 80.19 114 98.82 98.82 4.11e-51 GB AAN83756 "Soluble cytochrome b562 precursor [Escherichia coli CFT073]" 100.00 128 97.17 98.11 2.23e-67 PIR E86121 "cytochrome b (562) [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 94.34 100 97.00 100.00 4.92e-63 PIR E91280 "cytochrome b(562) [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" 94.34 100 97.00 100.00 4.92e-63 REF NP_290867 "cytochrome b562 [Escherichia coli O157:H7 str. EDL933]" 94.34 100 97.00 100.00 4.92e-63 REF NP_313240 "cytochrome b(562) [Escherichia coli O157:H7 str. Sakai]" 100.00 128 97.17 100.00 8.94e-68 REF NP_709965 "soluble cytochrome B562 [Shigella flexneri 2a str. 301]" 80.19 114 98.82 98.82 4.11e-51 REF NP_757182 "soluble cytochrome b562 [Escherichia coli CFT073]" 100.00 128 97.17 98.11 2.23e-67 REF WP_000112424 "cytochrome b562, partial [Escherichia coli]" 96.23 102 100.00 100.00 9.58e-66 SP P0ABE7 "RecName: Full=Soluble cytochrome b562; Short=Cytochrome b-562; Flags: Precursor [Escherichia coli]" 100.00 128 100.00 100.00 4.66e-69 SP P0ABE8 "RecName: Full=Soluble cytochrome b562; Short=Cytochrome b-562; Flags: Precursor [Escherichia coli O157:H7]" 100.00 128 97.17 100.00 8.94e-68 SP Q8CVG7 "RecName: Full=Soluble cytochrome b562; Short=Cytochrome b-562; Flags: Precursor [Escherichia coli CFT073]" 100.00 128 97.17 98.11 2.23e-67 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 Mon Jun 13 15:18:35 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 $cyt_b562 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $cyt_b562 '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 $cyt_b562 2.0 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _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_1H-15N_HMQC-NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC-NOESY' _Sample_label $sample_1 save_ save_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.8 0.1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label NOESY '1H-15N HMQC-NOESY' HCCH-TOCSY HNCA HN(CO)CA HNHA stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cytochrome b562' _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 CA C 48.9 . 1 2 . 2 ASP N N 119.1 . 1 3 . 2 ASP H H 8.7 . 1 4 . 2 ASP CA C 50.3 . 1 5 . 3 LEU N N 121.7 . 1 6 . 3 LEU H H 8.5 . 1 7 . 3 LEU CA C 56.1 . 1 8 . 4 GLU N N 116.7 . 1 9 . 4 GLU H H 8.5 . 1 10 . 4 GLU CA C 57.4 . 1 11 . 12 ASP N N 117.7 . 1 12 . 12 ASP H H 9.3 . 1 13 . 12 ASP CA C 54.8 . 1 14 . 13 ASN N N 116.2 . 1 15 . 13 ASN H H 7.9 . 1 16 . 13 ASN CA C 55.3 . 1 17 . 14 LEU N N 123.8 . 1 18 . 14 LEU H H 8.3 . 1 19 . 14 LEU CA C 56.3 . 1 20 . 15 LYS N N 116.7 . 1 21 . 15 LYS H H 7.5 . 1 22 . 15 LYS CA C 57.1 . 1 23 . 16 VAL N N 118.5 . 1 24 . 16 VAL H H 7.5 . 1 25 . 16 VAL CA C 64.1 . 1 26 . 17 ILE N N 119.1 . 1 27 . 17 ILE H H 8.0 . 1 28 . 17 ILE CA C 64.1 . 1 29 . 18 GLU N N 116.4 . 1 30 . 18 GLU H H 7.9 . 1 31 . 18 GLU CA C 56.3 . 1 32 . 19 LYS N N 115.1 . 1 33 . 19 LYS H H 7.4 . 1 34 . 19 LYS CA C 52.9 . 1 35 . 20 ALA N N 123.0 . 1 36 . 20 ALA H H 7.3 . 1 37 . 20 ALA CA C 50.9 . 1 38 . 21 ASP N N 115.7 . 1 39 . 21 ASP H H 8.7 . 1 40 . 21 ASP CA C 50.8 . 1 41 . 22 ASN N N 113.0 . 1 42 . 22 ASN H H 7.6 . 1 43 . 22 ASN CA C 49.7 . 1 44 . 23 ALA N N 121.9 . 1 45 . 23 ALA H H 9.1 . 1 46 . 23 ALA CA C 53.0 . 1 47 . 24 ALA N N 121.7 . 1 48 . 24 ALA H H 8.4 . 1 49 . 24 ALA CA C 53.2 . 1 50 . 25 GLN N N 117.0 . 1 51 . 25 GLN H H 8.0 . 1 52 . 25 GLN CA C 56.0 . 1 53 . 26 VAL N N 117.5 . 1 54 . 26 VAL H H 7.1 . 1 55 . 26 VAL CA C 64.5 . 1 56 . 27 LYS N N 119.1 . 1 57 . 27 LYS H H 8.8 . 1 58 . 27 LYS CA C 57.9 . 1 59 . 28 ASP N N 120.1 . 1 60 . 28 ASP H H 8.2 . 1 61 . 28 ASP CA C 55.1 . 1 62 . 29 ALA N N 121.2 . 1 63 . 29 ALA H H 7.6 . 1 64 . 29 ALA CA C 52.6 . 1 65 . 30 LEU N N 117.7 . 1 66 . 30 LEU H H 8.6 . 1 67 . 30 LEU CA C 55.4 . 1 68 . 31 THR N N 115.9 . 1 69 . 31 THR H H 8.3 . 1 70 . 31 THR CA C 65.3 . 1 71 . 32 LYS N N 121.9 . 1 72 . 32 LYS H H 7.5 . 1 73 . 32 LYS CA C 57.2 . 1 74 . 33 MET N N 118.3 . 1 75 . 33 MET H H 8.3 . 1 76 . 33 MET CA C 57.3 . 1 77 . 34 ARG N N 120.4 . 1 78 . 34 ARG H H 8.5 . 1 79 . 34 ARG CA C 57.9 . 1 80 . 35 ALA N N 116.4 . 1 81 . 35 ALA H H 7.0 . 1 82 . 35 ALA CA C 52.2 . 1 83 . 36 ALA N N 120.1 . 1 84 . 36 ALA H H 7.4 . 1 85 . 36 ALA CA C 51.7 . 1 86 . 37 ALA N N 119.6 . 1 87 . 37 ALA H H 8.2 . 1 88 . 37 ALA CA C 52.0 . 1 89 . 38 LEU N N 114.6 . 1 90 . 38 LEU H H 7.4 . 1 91 . 38 LEU CA C 54.6 . 1 92 . 39 ASP N N 118.8 . 1 93 . 39 ASP H H 7.4 . 1 94 . 39 ASP CA C 54.5 . 1 95 . 40 ALA N N 123.5 . 1 96 . 40 ALA H H 7.8 . 1 97 . 40 ALA CA C 51.4 . 1 98 . 41 GLN N N 112.8 . 1 99 . 41 GLN H H 6.5 . 1 100 . 41 GLN CA C 54.9 . 1 101 . 42 LYS N N 113.6 . 1 102 . 42 LYS H H 6.8 . 1 103 . 42 LYS CA C 53.8 . 1 104 . 43 ALA N N 122.5 . 1 105 . 43 ALA H H 7.7 . 1 106 . 43 ALA CA C 49.3 . 1 107 . 44 THR N N 114.1 . 1 108 . 44 THR H H 8.2 . 1 109 . 44 THR CA C 56.9 . 1 110 . 46 PRO CA C 63.7 . 1 111 . 47 LYS N N 115.1 . 1 112 . 47 LYS H H 9.5 . 1 113 . 47 LYS CA C 56.7 . 1 114 . 48 LEU N N 114.3 . 1 115 . 48 LEU H H 7.9 . 1 116 . 48 LEU CA C 50.4 . 1 117 . 49 GLU N N 118.5 . 1 118 . 49 GLU H H 7.3 . 1 119 . 49 GLU CA C 56.5 . 1 120 . 50 ASP N N 114.9 . 1 121 . 50 ASP H H 8.5 . 1 122 . 50 ASP CA C 51.1 . 1 123 . 51 LYS N N 118.5 . 1 124 . 51 LYS H H 7.7 . 1 125 . 51 LYS CA C 51.2 . 1 126 . 52 SER N N 117.0 . 1 127 . 52 SER H H 8.9 . 1 128 . 52 SER CA C 54.4 . 1 129 . 53 PRO CA C 63.1 . 1 130 . 54 ASP N N 113.3 . 1 131 . 54 ASP H H 8.0 . 1 132 . 54 ASP CA C 50.3 . 1 133 . 55 SER N N 115.7 . 1 134 . 55 SER H H 7.8 . 1 135 . 55 SER CA C 54.8 . 1 136 . 56 PRO CA C 63.1 . 1 137 . 57 GLU N N 117.5 . 1 138 . 57 GLU H H 9.7 . 1 139 . 57 GLU CA C 58.8 . 1 140 . 58 MET N N 117.2 . 1 141 . 58 MET H H 7.6 . 1 142 . 58 MET CA C 53.7 . 1 143 . 59 LYS N N 118.5 . 1 144 . 59 LYS H H 8.5 . 1 145 . 59 LYS CA C 58.1 . 1 146 . 60 ASP N N 120.6 . 1 147 . 60 ASP H H 8.4 . 1 148 . 60 ASP CA C 55.5 . 1 149 . 61 PHE N N 121.2 . 1 150 . 61 PHE H H 8.9 . 1 151 . 61 PHE CA C 60.3 . 1 152 . 62 ARG N N 114.3 . 1 153 . 62 ARG H H 8.5 . 1 154 . 62 ARG CA C 59.2 . 1 155 . 63 HIS N N 119.8 . 1 156 . 63 HIS H H 8.6 . 1 157 . 63 HIS CA C 55.7 . 1 158 . 64 GLY N N 107.8 . 1 159 . 64 GLY H H 8.3 . 1 160 . 64 GLY CA C 68.7 . 1 161 . 65 PHE N N 114.9 . 1 162 . 65 PHE H H 7.0 . 1 163 . 65 PHE CA C 59.6 . 1 164 . 66 ASP N N 120.4 . 1 165 . 66 ASP H H 7.3 . 1 166 . 66 ASP CA C 55.6 . 1 167 . 67 ILE N N 120.6 . 1 168 . 67 ILE H H 7.8 . 1 169 . 67 ILE CA C 61.7 . 1 170 . 68 LEU N N 120.6 . 1 171 . 68 LEU H H 8.0 . 1 172 . 68 LEU CA C 55.7 . 1 173 . 69 VAL N N 117.5 . 1 174 . 69 VAL H H 9.0 . 1 175 . 69 VAL CA C 65.2 . 1 176 . 70 GLY N N 106.8 . 1 177 . 70 GLY H H 7.9 . 1 178 . 70 GLY CA C 45.1 . 1 179 . 71 GLN N N 120.4 . 1 180 . 71 GLN H H 8.1 . 1 181 . 71 GLN CA C 56.9 . 1 182 . 72 ILE N N 123.2 . 1 183 . 72 ILE H H 8.9 . 1 184 . 72 ILE CA C 63.8 . 1 185 . 73 ASP N N 121.4 . 1 186 . 73 ASP H H 9.2 . 1 187 . 73 ASP CA C 55.3 . 1 188 . 74 ASP N N 121.9 . 1 189 . 74 ASP H H 8.2 . 1 190 . 74 ASP CA C 54.9 . 1 191 . 75 ALA N N 122.5 . 1 192 . 75 ALA H H 7.8 . 1 193 . 75 ALA CA C 52.8 . 1 194 . 76 LEU N N 121.2 . 1 195 . 76 LEU H H 9.3 . 1 196 . 76 LEU CA C 55.5 . 1 197 . 77 LYS N N 119.6 . 1 198 . 77 LYS H H 7.8 . 1 199 . 77 LYS CA C 57.7 . 1 200 . 78 LEU N N 117.0 . 1 201 . 78 LEU H H 6.9 . 1 202 . 78 LEU CA C 55.2 . 1 203 . 79 ALA N N 122.2 . 1 204 . 79 ALA H H 8.6 . 1 205 . 79 ALA CA C 53.3 . 1 206 . 80 ASN N N 118.0 . 1 207 . 80 ASN H H 8.9 . 1 208 . 80 ASN CA C 59.3 . 1 209 . 81 GLU N N 116.4 . 1 210 . 81 GLU H H 7.4 . 1 211 . 81 GLU CA C 53.5 . 1 212 . 82 GLY N N 107.0 . 1 213 . 82 GLY H H 7.9 . 1 214 . 82 GLY CA C 67.8 . 1 215 . 83 LYS N N 122.7 . 1 216 . 83 LYS H H 7.8 . 1 217 . 83 LYS CA C 52.4 . 1 218 . 84 VAL N N 121.9 . 1 219 . 84 VAL H H 7.7 . 1 220 . 84 VAL CA C 65.4 . 1 221 . 85 LYS N N 119.6 . 1 222 . 85 LYS H H 8.6 . 1 223 . 85 LYS CA C 56.9 . 1 224 . 86 GLU N N 120.6 . 1 225 . 86 GLU H H 9.3 . 1 226 . 86 GLU CA C 57.9 . 1 227 . 87 ALA N N 124.0 . 1 228 . 87 ALA H H 8.6 . 1 229 . 87 ALA CA C 53.2 . 1 230 . 88 GLN N N 116.4 . 1 231 . 88 GLN H H 8.7 . 1 232 . 88 GLN CA C 57.4 . 1 233 . 89 ALA N N 122.2 . 1 234 . 89 ALA H H 8.2 . 1 235 . 89 ALA CA C 52.7 . 1 236 . 90 ALA N N 121.2 . 1 237 . 90 ALA H H 8.2 . 1 238 . 90 ALA CA C 52.3 . 1 239 . 91 ALA N N 121.2 . 1 240 . 91 ALA H H 8.5 . 1 241 . 91 ALA CA C 51.8 . 1 242 . 92 GLU N N 115.4 . 1 243 . 92 GLU H H 7.8 . 1 244 . 92 GLU CA C 56.2 . 1 245 . 93 GLN N N 116.4 . 1 246 . 93 GLN H H 7.6 . 1 247 . 93 GLN CA C 55.5 . 1 248 . 94 LEU N N 118.0 . 1 249 . 94 LEU H H 7.9 . 1 250 . 94 LEU CA C 55.3 . 1 251 . 95 LYS N N 114.1 . 1 252 . 95 LYS H H 7.6 . 1 253 . 95 LYS CA C 57.7 . 1 254 . 96 THR N N 114.9 . 1 255 . 96 THR H H 7.4 . 1 256 . 96 THR CA C 63.5 . 1 257 . 97 THR N N 120.9 . 1 258 . 97 THR H H 7.2 . 1 259 . 97 THR CA C 63.4 . 1 260 . 98 ARG N N 119.6 . 1 261 . 98 ARG H H 8.4 . 1 262 . 98 ARG CA C 56.1 . 1 263 . 99 ASN N N 114.9 . 1 264 . 99 ASN H H 8.0 . 1 265 . 99 ASN CA C 52.6 . 1 266 . 100 ALA N N 120.9 . 1 267 . 100 ALA H H 7.5 . 1 268 . 100 ALA CA C 52.3 . 1 269 . 102 HIS N N 117.0 . 1 270 . 102 HIS H H 6.8 . 1 stop_ save_