data_4189 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Reduced Horse Heart Cytochrome c ; _BMRB_accession_number 4189 _BMRB_flat_file_name bmr4189.str _Entry_type original _Submission_date 1998-08-20 _Accession_date 1998-10-14 _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 Banci L. . . 2 Bertini I. . . 3 Huber J. G. . 4 Spyroulias G. A. . 5 Turano P. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 617 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-08 original author . stop_ _Original_release_date 2000-03-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of Reduced Horse Heart Cytochrome C' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99428887 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Huber J. G. . 4 Spyroulias G. A. . 5 Turano P. . . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_volume 4 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 21 _Page_last 31 _Year 1999 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_hh_cytc _Saveframe_category molecular_system _Mol_system_name 'cytochrome c' _Abbreviation_common 'hh cytc' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hh cytc' $hh_cytc heme $HEC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hh_cytc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c' _Abbreviation_common cytc _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GDVEKGKKIFVQKCAQCHTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ASP 3 VAL 4 GLU 5 LYS 6 GLY 7 LYS 8 LYS 9 ILE 10 PHE 11 VAL 12 GLN 13 LYS 14 CYS 15 ALA 16 GLN 17 CYS 18 HIS 19 THR 20 VAL 21 GLU 22 LYS 23 GLY 24 GLY 25 LYS 26 HIS 27 LYS 28 THR 29 GLY 30 PRO 31 ASN 32 LEU 33 HIS 34 GLY 35 LEU 36 PHE 37 GLY 38 ARG 39 LYS 40 THR 41 GLY 42 GLN 43 ALA 44 PRO 45 GLY 46 PHE 47 THR 48 TYR 49 THR 50 ASP 51 ALA 52 ASN 53 LYS 54 ASN 55 LYS 56 GLY 57 ILE 58 THR 59 TRP 60 LYS 61 GLU 62 GLU 63 THR 64 LEU 65 MET 66 GLU 67 TYR 68 LEU 69 GLU 70 ASN 71 PRO 72 LYS 73 LYS 74 TYR 75 ILE 76 PRO 77 GLY 78 THR 79 LYS 80 MET 81 ILE 82 PHE 83 ALA 84 GLY 85 ILE 86 LYS 87 LYS 88 LYS 89 THR 90 GLU 91 ARG 92 GLU 93 ASP 94 LEU 95 ILE 96 ALA 97 TYR 98 LEU 99 LYS 100 LYS 101 ALA 102 THR 103 ASN 104 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 1058 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1107 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1108 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1109 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1110 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1111 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1112 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1113 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1114 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1116 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1170 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 1171 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1404 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 16759 cytochrome_c 100.00 104 100.00 100.00 4.20e-68 BMRB 17120 cytc 100.00 105 99.04 100.00 6.63e-68 BMRB 17340 cytc 100.00 104 100.00 100.00 4.20e-68 BMRB 1736 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1783 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 17847 hCc 100.00 104 100.00 100.00 4.20e-68 BMRB 17848 hCc 100.00 104 100.00 100.00 4.20e-68 BMRB 1785 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1787 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 1789 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 216 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 220 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 224 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 2366 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 2367 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 2368 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 243 "cytochrome c" 100.00 104 100.00 100.00 4.20e-68 BMRB 244 "cytochrome c" 100.00 104 100.00 100.00 4.20e-68 BMRB 25640 entity_1 100.00 105 99.04 99.04 8.42e-67 BMRB 274 "cytochrome c" 100.00 104 100.00 100.00 4.20e-68 BMRB 285 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 286 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 316 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 317 "cytochrome c" 99.04 104 100.00 100.00 2.11e-67 BMRB 336 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 436 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 437 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 438 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 BMRB 439 "cytochrome c" 99.04 104 98.06 98.06 9.18e-65 PDB 1AKK "Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure" 100.00 104 100.00 100.00 4.20e-68 PDB 1CRC "Cytochrome C At Low Ionic Strength" 100.00 105 100.00 100.00 4.33e-68 PDB 1FI7 "Solution Structure Of The Imidazole Complex Of Cytochrome C" 100.00 104 100.00 100.00 4.20e-68 PDB 1FI9 "Solution Structure Of The Imidazole Complex Of Cytochrome C" 100.00 104 100.00 100.00 4.20e-68 PDB 1GIW "Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure" 99.04 104 100.00 100.00 2.11e-67 PDB 1HRC "High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C" 100.00 105 100.00 100.00 4.33e-68 PDB 1I5T "Solution Structure Of Cyanoferricytochrome C" 100.00 104 100.00 100.00 4.20e-68 PDB 1LC1 "Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr Minimized Average Structure" 100.00 104 100.00 100.00 4.20e-68 PDB 1LC2 "Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr 30 Structures" 100.00 104 100.00 100.00 4.20e-68 PDB 1M60 "Solution Structure Of Zinc-Substituted Cytochrome C" 100.00 104 100.00 100.00 4.20e-68 PDB 1OCD "Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure" 100.00 104 100.00 100.00 4.20e-68 PDB 1U75 "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" 100.00 104 100.00 100.00 4.20e-68 PDB 1WEJ "Igg1 Fab Fragment (Of E8 Antibody) Complexed With Horse Cytochrome C At 1.8 A Resolution" 100.00 105 100.00 100.00 4.33e-68 PDB 2B4Z "Crystal Structure Of Cytochrome C From Bovine Heart At 1.5 A Resolution." 100.00 104 97.12 98.08 8.16e-66 PDB 2FRC "Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure" 100.00 104 100.00 100.00 4.20e-68 PDB 2GIW "Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures" 100.00 104 100.00 100.00 4.20e-68 PDB 2PCB "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 100.00 104 100.00 100.00 4.20e-68 PDB 2YBB "Fitted Model For Bovine Mitochondrial Supercomplex I1iii2iv1 By Single Particle Cryo-Em (Emd-1876)" 100.00 104 97.12 98.08 8.16e-66 PDB 3J2T "An Improved Model Of The Human Apoptosome" 100.00 104 97.12 98.08 8.16e-66 PDB 3NBS "Crystal Structure Of Dimeric Cytochrome C From Horse Heart" 100.00 104 100.00 100.00 4.20e-68 PDB 3NBT "Crystal Structure Of Trimeric Cytochrome C From Horse Heart" 100.00 104 100.00 100.00 4.20e-68 PDB 3O1Y "Electron Transfer Complexes: Experimental Mapping Of The Redox- Dependent Cytochrome C Electrostatic Surface" 100.00 105 100.00 100.00 4.33e-68 PDB 3O20 "Electron Transfer Complexes:experimental Mapping Of The Redox- Dependent Cytochrome C Electrostatic Surface" 100.00 105 100.00 100.00 4.33e-68 PDB 3WC8 "Dimeric Horse Cytochrome C Obtained By Refolding With Desalting Method" 100.00 104 100.00 100.00 4.20e-68 PDB 3WUI "Dimeric Horse Cytochrome C Formed By Refolding From Molten Globule State" 100.00 104 100.00 100.00 4.20e-68 PDB 4NFG "K13r Mutant Of Horse Cytochrome C And Yeast Cytochrome C Peroxidase Complex" 100.00 104 97.12 100.00 3.89e-66 PDB 4RSZ "The X-ray Structure Of The Primary Adduct Formed In The Reaction Between Cisplatin And Cytochrome C" 100.00 104 100.00 100.00 4.20e-68 GB AAB33495 "apocytochrome c [horses, heart, Peptide, 104 aa]" 100.00 104 98.08 98.08 4.38e-66 GB AAI05398 "Cytochrome c, somatic [Bos taurus]" 100.00 105 97.12 98.08 6.69e-66 GB AAX77008 "cytochrome c-like protein [Sus scrofa]" 100.00 105 97.12 98.08 6.69e-66 GB ABA06541 "mitochondrial cytochrome c [Bubalus bubalis]" 100.00 104 97.12 98.08 8.16e-66 GB AEB61027 "cytochrome c-like protein, partial [Equus caballus]" 100.00 127 100.00 100.00 1.24e-68 PRF 610169A "cytochrome c" 100.00 104 100.00 100.00 4.20e-68 PRF 711086A "cytochrome c" 100.00 104 97.12 100.00 2.38e-67 REF NP_001039526 "cytochrome c [Bos taurus]" 100.00 105 97.12 98.08 6.69e-66 REF NP_001123442 "cytochrome c [Sus scrofa]" 100.00 105 97.12 98.08 6.69e-66 REF NP_001157486 "cytochrome c [Equus caballus]" 100.00 105 99.04 100.00 6.63e-68 REF XP_004007999 "PREDICTED: cytochrome c [Ovis aries]" 100.00 105 97.12 98.08 6.69e-66 REF XP_004418964 "PREDICTED: cytochrome c-like [Ceratotherium simum simum]" 100.00 105 98.08 99.04 2.51e-67 SP P00004 "RecName: Full=Cytochrome c" 100.00 105 100.00 100.00 3.34e-68 SP P62894 "RecName: Full=Cytochrome c" 100.00 105 97.12 98.08 6.69e-66 SP P62895 "RecName: Full=Cytochrome c" 100.00 105 97.12 98.08 6.69e-66 SP P62896 "RecName: Full=Cytochrome c" 100.00 105 97.12 98.08 6.69e-66 SP P68096 "RecName: Full=Cytochrome c" 100.00 105 99.04 100.00 6.63e-68 TPG DAA30512 "TPA: cytochrome c [Bos taurus]" 100.00 105 97.12 98.08 6.69e-66 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEC (HEME C)" _BMRB_code . _PDB_code HEC _Molecular_mass 618.503 _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 16 11:03:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 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 . ? NB NB N . 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 . ? NC NC N . 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 . ? ND ND N . 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 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HBC3 HBC3 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D 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 FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? SING NB C4B ? ? DOUB C1B C2B ? ? SING C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? DOUB C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? DOUB C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? SING CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING CBC HBC3 ? ? SING ND C1D ? ? SING ND C4D ? ? DOUB C1D C2D ? ? SING C2D C3D ? ? SING C2D CMD ? ? DOUB C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? 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 _Tissue $hh_cytc horse 9796 Eukaryota Metazoa Equus caballus heart 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 $hh_cytc . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details ; The sample was lyophilized in a phosphate solution. Reduction of the protein was accomplished by addition of sodium dithionite. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $hh_cytc . mM 2.5 3.0 . phosphate 100 mM . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details 'The sample was lyophilized in a deuterated phosphate solution' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $hh_cytc . mM 2.5 3.0 . phosphate 100 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Task ; Multiplication of raw data by a pure cosine-squared function Fourier Transform Polynomial baseline correction ; stop_ _Details . save_ save_xeasy _Saveframe_category software _Name XEASY _Version . loop_ _Task 'Volume integration of cross-peaks on 2D spectra' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model AVANCE _Field_strength 800 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a pressure 1013 . mbar temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 _Indirect_shift_ratio_citation_label DSS H 1 'methyl protons' ppm 0.00 . direct . . . 1.0 $citation_one 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'hh cytc' _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 GLY H H 8.31 . 1 2 . 1 GLY HA2 H 3.74 . 1 3 . 1 GLY HA3 H 4.00 . 1 4 . 2 ASP H H 9.45 . 1 5 . 2 ASP HA H 4.78 . 1 6 . 2 ASP HB2 H 2.84 . 1 7 . 2 ASP HB3 H 2.50 . 1 8 . 3 VAL H H 8.60 . 1 9 . 3 VAL HA H 3.65 . 1 10 . 3 VAL HB H 2.19 . 1 11 . 3 VAL HG1 H 1.07 . 1 12 . 3 VAL HG2 H 1.07 . 1 13 . 4 GLU H H 8.16 . 1 14 . 4 GLU HA H 4.12 . 1 15 . 4 GLU HB2 H 2.17 . 1 16 . 4 GLU HB3 H 2.12 . 1 17 . 4 GLU HG2 H 2.29 . 1 18 . 4 GLU HG3 H 2.37 . 1 19 . 5 LYS H H 8.15 . 1 20 . 5 LYS HA H 4.01 . 1 21 . 5 LYS HB2 H 1.84 . 1 22 . 5 LYS HB3 H 1.84 . 1 23 . 5 LYS HG2 H 1.42 . 1 24 . 5 LYS HG3 H 1.58 . 1 25 . 5 LYS HD2 H 1.75 . 1 26 . 5 LYS HD3 H 1.75 . 1 27 . 5 LYS HE2 H 3.00 . 1 28 . 5 LYS HE3 H 3.00 . 1 29 . 6 GLY H H 8.89 . 1 30 . 6 GLY HA2 H 4.22 . 1 31 . 6 GLY HA3 H 3.58 . 1 32 . 7 LYS H H 8.10 . 1 33 . 7 LYS HA H 2.29 . 1 34 . 7 LYS HB2 H 1.76 . 1 35 . 7 LYS HB3 H 1.76 . 1 36 . 7 LYS HG2 H 1.45 . 1 37 . 7 LYS HG3 H 1.61 . 1 38 . 7 LYS HD2 H 0.83 . 1 39 . 7 LYS HD3 H 0.83 . 1 40 . 7 LYS HE2 H 2.88 . 1 41 . 7 LYS HE3 H 2.88 . 1 42 . 8 LYS H H 6.99 . 1 43 . 8 LYS HA H 3.95 . 1 44 . 8 LYS HB2 H 1.95 . 1 45 . 8 LYS HB3 H 1.95 . 1 46 . 8 LYS HG2 H 1.43 . 1 47 . 8 LYS HG3 H 1.43 . 1 48 . 8 LYS HD2 H 1.70 . 1 49 . 8 LYS HD3 H 1.70 . 1 50 . 8 LYS HE2 H 2.98 . 1 51 . 8 LYS HE3 H 2.98 . 1 52 . 9 ILE H H 7.73 . 1 53 . 9 ILE HA H 3.89 . 1 54 . 9 ILE HB H 2.13 . 1 55 . 9 ILE HG12 H 1.28 . 1 56 . 9 ILE HG13 H 1.28 . 1 57 . 9 ILE HG2 H 1.16 . 1 58 . 10 PHE H H 8.70 . 1 59 . 10 PHE HA H 4.03 . 1 60 . 10 PHE HB2 H 2.99 . 1 61 . 10 PHE HB3 H 3.13 . 1 62 . 10 PHE HD1 H 7.20 . 1 63 . 10 PHE HD2 H 7.13 . 1 64 . 10 PHE HE1 H 6.17 . 1 65 . 10 PHE HE2 H 7.01 . 1 66 . 10 PHE HZ H 6.25 . 1 67 . 11 VAL H H 8.81 . 1 68 . 11 VAL HA H 3.56 . 1 69 . 11 VAL HB H 2.17 . 1 70 . 11 VAL HG1 H 0.96 . 1 71 . 11 VAL HG2 H 1.14 . 1 72 . 12 GLN H H 7.99 . 1 73 . 12 GLN HA H 4.23 . 1 74 . 12 GLN HB2 H 2.27 . 1 75 . 12 GLN HB3 H 2.32 . 1 76 . 12 GLN HG2 H 2.68 . 1 77 . 12 GLN HG3 H 2.46 . 1 78 . 13 LYS H H 9.01 . 1 79 . 13 LYS HA H 5.05 . 1 80 . 13 LYS HB2 H 2.49 . 1 81 . 13 LYS HB3 H 2.49 . 1 82 . 13 LYS HG2 H 1.80 . 1 83 . 13 LYS HG3 H 1.80 . 1 84 . 13 LYS HD2 H 2.05 . 1 85 . 13 LYS HD3 H 2.33 . 1 86 . 13 LYS HE2 H 3.18 . 1 87 . 13 LYS HE3 H 3.18 . 1 88 . 14 CYS H H 8.39 . 1 89 . 14 CYS HA H 5.33 . 1 90 . 14 CYS HB2 H 1.10 . 1 91 . 14 CYS HB3 H 1.85 . 1 92 . 15 ALA H H 7.43 . 1 93 . 15 ALA HA H 3.95 . 1 94 . 15 ALA HB H 1.41 . 1 95 . 16 GLN H H 8.85 . 1 96 . 16 GLN HA H 4.00 . 1 97 . 16 GLN HB2 H 2.02 . 1 98 . 16 GLN HB3 H 2.31 . 1 99 . 16 GLN HG2 H 2.51 . 1 100 . 16 GLN HG3 H 2.77 . 1 101 . 16 GLN HE21 H 7.16 . 1 102 . 16 GLN HE22 H 7.73 . 1 103 . 17 CYS H H 7.03 . 1 104 . 17 CYS HA H 4.20 . 1 105 . 17 CYS HB2 H 0.57 . 1 106 . 17 CYS HB3 H 1.54 . 1 107 . 18 HIS H H 6.39 . 1 108 . 18 HIS HA H 3.69 . 1 109 . 18 HIS HB2 H 1.07 . 1 110 . 18 HIS HB3 H 0.78 . 1 111 . 18 HIS HD1 H 9.63 . 1 112 . 18 HIS HD2 H 0.12 . 1 113 . 18 HIS HE1 H 0.41 . 1 114 . 19 THR H H 7.87 . 1 115 . 19 THR HA H 4.54 . 1 116 . 19 THR HB H 4.48 . 1 117 . 19 THR HG2 H 1.09 . 1 118 . 20 VAL H H 7.78 . 1 119 . 20 VAL HA H 3.91 . 1 120 . 20 VAL HB H 1.56 . 1 121 . 20 VAL HG2 H 0.42 . 1 122 . 21 GLU H H 8.82 . 1 123 . 21 GLU HA H 4.23 . 1 124 . 22 LYS H H 8.72 . 1 125 . 22 LYS HA H 3.16 . 1 126 . 22 LYS HB2 H 0.58 . 2 127 . 22 LYS HB3 H 1.32 . 2 128 . 23 GLY H H 9.25 . 1 129 . 23 GLY HA2 H 3.54 . 1 130 . 23 GLY HA3 H 3.88 . 1 131 . 24 GLY H H 7.87 . 1 132 . 24 GLY HA2 H 3.14 . 1 133 . 24 GLY HA3 H 3.80 . 1 134 . 25 LYS H H 8.32 . 1 135 . 25 LYS HA H 3.92 . 1 136 . 25 LYS HB2 H 1.52 . 1 137 . 25 LYS HB3 H 1.72 . 1 138 . 25 LYS HG2 H 1.46 . 1 139 . 25 LYS HG3 H 1.46 . 1 140 . 25 LYS HD2 H 1.33 . 1 141 . 25 LYS HD3 H 1.33 . 1 142 . 25 LYS HE2 H 2.88 . 1 143 . 25 LYS HE3 H 2.88 . 1 144 . 26 HIS H H 8.54 . 1 145 . 26 HIS HA H 4.46 . 1 146 . 26 HIS HB2 H 3.09 . 1 147 . 26 HIS HB3 H 2.90 . 1 148 . 26 HIS HD1 H 7.03 . 1 149 . 26 HIS HD2 H 7.50 . 1 150 . 26 HIS HE1 H 7.00 . 1 151 . 27 LYS H H 7.77 . 1 152 . 27 LYS HA H 4.49 . 1 153 . 27 LYS HB2 H 1.12 . 1 154 . 27 LYS HB3 H 1.12 . 1 155 . 28 THR H H 7.92 . 1 156 . 28 THR HA H 4.13 . 1 157 . 28 THR HB H 4.34 . 1 158 . 28 THR HG2 H 2.09 . 1 159 . 29 GLY H H 7.44 . 1 160 . 29 GLY HA2 H -0.20 . 1 161 . 29 GLY HA3 H 3.69 . 1 162 . 30 PRO HA H 3.60 . 1 163 . 30 PRO HB2 H 1.29 . 1 164 . 30 PRO HB3 H 0.39 . 1 165 . 30 PRO HG2 H 0.55 . 1 166 . 30 PRO HG3 H 1.44 . 1 167 . 30 PRO HD2 H 1.08 . 1 168 . 30 PRO HD3 H 1.45 . 1 169 . 31 ASN H H 10.65 . 1 170 . 31 ASN HA H 4.09 . 1 171 . 31 ASN HB2 H 1.96 . 1 172 . 31 ASN HB3 H 2.11 . 1 173 . 32 LEU H H 7.88 . 1 174 . 32 LEU HA H 4.05 . 1 175 . 32 LEU HB2 H 1.10 . 1 176 . 32 LEU HB3 H 1.47 . 1 177 . 32 LEU HG H 0.55 . 1 178 . 32 LEU HD1 H -0.76 . 1 179 . 32 LEU HD2 H -0.60 . 1 180 . 33 HIS H H 7.45 . 1 181 . 33 HIS HA H 3.78 . 1 182 . 33 HIS HB2 H 2.98 . 1 183 . 33 HIS HB3 H 2.98 . 1 184 . 33 HIS HD1 H 6.97 . 1 185 . 33 HIS HD2 H 6.83 . 1 186 . 33 HIS HE1 H 7.57 . 1 187 . 34 GLY H H 8.88 . 1 188 . 34 GLY HA2 H 3.74 . 1 189 . 34 GLY HA3 H 3.93 . 1 190 . 35 LEU H H 7.08 . 1 191 . 35 LEU HA H 3.63 . 1 192 . 35 LEU HB2 H 1.56 . 1 193 . 35 LEU HB3 H 2.20 . 1 194 . 35 LEU HG H 1.29 . 1 195 . 35 LEU HD1 H 0.71 . 1 196 . 35 LEU HD2 H 0.71 . 1 197 . 36 PHE H H 8.68 . 1 198 . 36 PHE HA H 3.98 . 1 199 . 36 PHE HB2 H 3.27 . 1 200 . 36 PHE HB3 H 2.85 . 1 201 . 36 PHE HD1 H 7.37 . 1 202 . 36 PHE HD2 H 7.37 . 1 203 . 36 PHE HE1 H 6.87 . 1 204 . 36 PHE HE2 H 6.87 . 1 205 . 36 PHE HZ H 7.14 . 1 206 . 37 GLY H H 9.52 . 1 207 . 37 GLY HA2 H 3.51 . 1 208 . 37 GLY HA3 H 4.46 . 1 209 . 38 ARG H H 8.37 . 1 210 . 38 ARG HA H 4.72 . 1 211 . 38 ARG HB2 H 2.19 . 1 212 . 38 ARG HB3 H 2.03 . 1 213 . 38 ARG HG2 H 1.97 . 1 214 . 38 ARG HG3 H 2.33 . 1 215 . 38 ARG HD2 H 3.20 . 1 216 . 38 ARG HD3 H 3.20 . 1 217 . 38 ARG HH11 H 6.72 . 1 218 . 38 ARG HH12 H 6.72 . 1 219 . 39 LYS H H 8.16 . 1 220 . 39 LYS HB2 H 1.61 . 1 221 . 39 LYS HB3 H 1.78 . 1 222 . 39 LYS HG2 H 1.51 . 1 223 . 39 LYS HG3 H 1.56 . 1 224 . 39 LYS HD2 H 1.42 . 1 225 . 39 LYS HD3 H 1.47 . 1 226 . 39 LYS HE2 H 2.89 . 1 227 . 39 LYS HE3 H 2.89 . 1 228 . 40 THR H H 7.39 . 1 229 . 40 THR HA H 4.51 . 1 230 . 40 THR HB H 4.46 . 1 231 . 40 THR HG2 H 0.87 . 1 232 . 41 GLY H H 8.61 . 1 233 . 41 GLY HA2 H 3.28 . 1 234 . 41 GLY HA3 H 1.50 . 1 235 . 42 GLN H H 8.54 . 1 236 . 42 GLN HA H 4.51 . 1 237 . 42 GLN HB2 H 1.90 . 1 238 . 42 GLN HB3 H 1.90 . 1 239 . 43 ALA H H 8.64 . 1 240 . 43 ALA HA H 4.67 . 1 241 . 43 ALA HB H 1.59 . 1 242 . 44 PRO HA H 4.55 . 1 243 . 44 PRO HB2 H 2.04 . 1 244 . 44 PRO HB3 H 2.40 . 1 245 . 44 PRO HG3 H 2.26 . 2 246 . 44 PRO HD2 H 3.87 . 1 247 . 44 PRO HD3 H 4.17 . 1 248 . 45 GLY H H 9.19 . 1 249 . 45 GLY HA2 H 3.83 . 1 250 . 45 GLY HA3 H 4.41 . 1 251 . 46 PHE H H 7.18 . 1 252 . 46 PHE HA H 4.19 . 1 253 . 46 PHE HB2 H 1.12 . 1 254 . 46 PHE HB3 H 2.35 . 1 255 . 46 PHE HD1 H 5.01 . 1 256 . 46 PHE HD2 H 6.40 . 1 257 . 46 PHE HE1 H 7.48 . 1 258 . 46 PHE HE2 H 6.90 . 1 259 . 46 PHE HZ H 7.74 . 1 260 . 47 THR H H 7.33 . 1 261 . 47 THR HA H 4.28 . 1 262 . 47 THR HB H 3.75 . 1 263 . 47 THR HG1 H 9.49 . 1 264 . 47 THR HG2 H 1.12 . 1 265 . 48 TYR H H 8.53 . 1 266 . 48 TYR HA H 5.22 . 1 267 . 48 TYR HB2 H 2.83 . 1 268 . 48 TYR HB3 H 3.70 . 1 269 . 48 TYR HD1 H 7.49 . 1 270 . 48 TYR HD2 H 7.97 . 1 271 . 48 TYR HE1 H 7.29 . 1 272 . 48 TYR HE2 H 7.06 . 1 273 . 48 TYR HH H 8.63 . 1 274 . 49 THR H H 10.30 . 1 275 . 49 THR HA H 4.48 . 1 276 . 49 THR HB H 4.73 . 1 277 . 49 THR HG1 H 8.69 . 1 278 . 49 THR HG2 H 1.79 . 1 279 . 50 ASP H H 8.85 . 1 280 . 50 ASP HA H 4.40 . 1 281 . 50 ASP HB2 H 2.60 . 1 282 . 50 ASP HB3 H 2.60 . 1 283 . 51 ALA H H 7.87 . 1 284 . 51 ALA HA H 3.94 . 1 285 . 51 ALA HB H 1.33 . 1 286 . 52 ASN H H 8.46 . 1 287 . 52 ASN HA H 4.23 . 1 288 . 52 ASN HB2 H 2.96 . 1 289 . 52 ASN HB3 H 3.13 . 1 290 . 53 LYS H H 8.09 . 1 291 . 53 LYS HA H 3.57 . 1 292 . 53 LYS HB2 H 1.88 . 1 293 . 53 LYS HB3 H 1.88 . 1 294 . 53 LYS HG2 H 1.56 . 1 295 . 53 LYS HG3 H 1.56 . 1 296 . 54 ASN H H 8.75 . 1 297 . 54 ASN HA H 4.51 . 1 298 . 54 ASN HB2 H 2.77 . 1 299 . 54 ASN HB3 H 2.82 . 1 300 . 55 LYS H H 7.49 . 1 301 . 55 LYS HA H 4.06 . 1 302 . 55 LYS HB2 H 1.87 . 1 303 . 55 LYS HB3 H 2.08 . 1 304 . 56 GLY H H 7.13 . 1 305 . 56 GLY HA2 H 3.75 . 1 306 . 56 GLY HA3 H 3.85 . 1 307 . 57 ILE H H 6.39 . 1 308 . 57 ILE HA H 4.40 . 1 309 . 57 ILE HB H 1.88 . 1 310 . 57 ILE HG12 H 0.44 . 1 311 . 57 ILE HG13 H 0.94 . 1 312 . 57 ILE HG2 H 0.75 . 1 313 . 57 ILE HD1 H -0.68 . 1 314 . 58 THR H H 8.20 . 1 315 . 58 THR HA H 4.22 . 1 316 . 58 THR HB H 3.78 . 1 317 . 58 THR HG1 H 11.01 . 1 318 . 58 THR HG2 H 0.97 . 1 319 . 59 TRP H H 9.02 . 1 320 . 59 TRP HB2 H 2.48 . 1 321 . 59 TRP HB3 H 3.80 . 1 322 . 59 TRP HD1 H 7.00 . 1 323 . 59 TRP HE1 H 10.07 . 1 324 . 59 TRP HE3 H 7.60 . 1 325 . 59 TRP HZ2 H 7.03 . 1 326 . 59 TRP HZ3 H 6.69 . 1 327 . 59 TRP HH2 H 5.72 . 1 328 . 60 LYS H H 8.20 . 1 329 . 60 LYS HA H 4.39 . 1 330 . 60 LYS HB2 H 2.11 . 1 331 . 60 LYS HB3 H 2.47 . 1 332 . 60 LYS HG2 H 1.51 . 1 333 . 60 LYS HG3 H 1.68 . 1 334 . 60 LYS HD2 H 1.75 . 1 335 . 60 LYS HD3 H 1.86 . 1 336 . 60 LYS HE2 H 2.98 . 1 337 . 60 LYS HE3 H 3.07 . 1 338 . 61 GLU H H 10.85 . 1 339 . 61 GLU HA H 3.93 . 1 340 . 61 GLU HB2 H 2.68 . 1 341 . 61 GLU HB3 H 2.68 . 1 342 . 62 GLU H H 9.67 . 1 343 . 62 GLU HA H 4.09 . 1 344 . 62 GLU HB2 H 2.12 . 1 345 . 62 GLU HB3 H 2.12 . 1 346 . 62 GLU HG2 H 2.43 . 1 347 . 62 GLU HG3 H 2.43 . 1 348 . 63 THR H H 7.22 . 1 349 . 63 THR HA H 4.34 . 1 350 . 63 THR HB H 4.53 . 1 351 . 63 THR HG2 H 1.38 . 1 352 . 64 LEU H H 8.89 . 1 353 . 64 LEU HA H 4.34 . 1 354 . 64 LEU HB2 H 2.06 . 1 355 . 64 LEU HB3 H 2.06 . 1 356 . 64 LEU HG H 1.91 . 1 357 . 64 LEU HD1 H 0.44 . 1 358 . 64 LEU HD2 H 0.72 . 1 359 . 65 MET H H 8.56 . 1 360 . 65 MET HA H 3.99 . 1 361 . 65 MET HB2 H 2.07 . 1 362 . 65 MET HB3 H 2.37 . 1 363 . 65 MET HG2 H 2.63 . 1 364 . 65 MET HG3 H 2.81 . 1 365 . 65 MET HE H 2.12 . 1 366 . 66 GLU H H 6.73 . 1 367 . 66 GLU HA H 4.07 . 1 368 . 66 GLU HB2 H 1.55 . 1 369 . 66 GLU HB3 H 1.79 . 1 370 . 66 GLU HG2 H 1.92 . 1 371 . 66 GLU HG3 H 2.29 . 1 372 . 67 TYR H H 8.27 . 1 373 . 67 TYR HA H 3.64 . 1 374 . 67 TYR HB2 H 2.71 . 1 375 . 67 TYR HB3 H 3.36 . 1 376 . 67 TYR HD1 H 0.73 . 1 377 . 67 TYR HD2 H 0.94 . 1 378 . 67 TYR HE1 H 0.10 . 1 379 . 67 TYR HE2 H 0.43 . 1 380 . 67 TYR HH H 3.07 . 1 381 . 68 LEU H H 8.34 . 1 382 . 68 LEU HA H 3.11 . 1 383 . 68 LEU HB2 H 1.72 . 1 384 . 68 LEU HB3 H 1.72 . 1 385 . 68 LEU HG H 1.93 . 1 386 . 68 LEU HD1 H 0.34 . 1 387 . 68 LEU HD2 H 1.08 . 1 388 . 69 GLU H H 6.90 . 1 389 . 69 GLU HA H 3.98 . 1 390 . 69 GLU HB2 H 1.75 . 1 391 . 69 GLU HB3 H 2.02 . 1 392 . 69 GLU HG2 H 2.11 . 1 393 . 69 GLU HG3 H 2.21 . 1 394 . 70 ASN H H 6.22 . 1 395 . 70 ASN HA H 4.26 . 1 396 . 70 ASN HB2 H 2.77 . 1 397 . 70 ASN HB3 H 2.81 . 1 398 . 71 PRO HA H 3.93 . 1 399 . 71 PRO HB2 H 2.77 . 1 400 . 71 PRO HB3 H 2.81 . 1 401 . 72 LYS H H 7.75 . 1 402 . 72 LYS HA H 3.80 . 1 403 . 72 LYS HB2 H 1.52 . 1 404 . 72 LYS HB3 H 1.70 . 1 405 . 72 LYS HG2 H 1.29 . 1 406 . 72 LYS HG3 H 1.29 . 1 407 . 72 LYS HE2 H 2.84 . 1 408 . 72 LYS HE3 H 2.84 . 1 409 . 73 LYS H H 7.00 . 1 410 . 73 LYS HA H 3.94 . 1 411 . 73 LYS HB2 H 1.58 . 1 412 . 73 LYS HB3 H 1.62 . 1 413 . 74 TYR H H 7.31 . 1 414 . 74 TYR HA H 4.41 . 1 415 . 74 TYR HB2 H 3.13 . 1 416 . 74 TYR HB3 H 3.26 . 1 417 . 74 TYR HD1 H 7.24 . 1 418 . 74 TYR HD2 H 7.24 . 1 419 . 74 TYR HE1 H 6.58 . 1 420 . 74 TYR HE2 H 6.58 . 1 421 . 75 ILE H H 8.33 . 1 422 . 75 ILE HA H 4.10 . 1 423 . 75 ILE HB H 1.88 . 1 424 . 75 ILE HG12 H 1.50 . 1 425 . 75 ILE HG13 H 1.79 . 1 426 . 75 ILE HG2 H 0.61 . 1 427 . 75 ILE HD1 H 0.96 . 1 428 . 76 PRO HA H 4.51 . 1 429 . 76 PRO HB2 H 2.20 . 1 430 . 76 PRO HB3 H 1.73 . 1 431 . 76 PRO HG2 H 1.95 . 1 432 . 76 PRO HG3 H 1.95 . 1 433 . 76 PRO HD2 H 3.17 . 1 434 . 76 PRO HD3 H 3.36 . 1 435 . 77 GLY H H 8.75 . 1 436 . 77 GLY HA2 H 3.61 . 1 437 . 77 GLY HA3 H 4.21 . 1 438 . 78 THR H H 8.16 . 1 439 . 78 THR HA H 4.51 . 1 440 . 78 THR HB H 4.28 . 1 441 . 78 THR HG1 H 8.38 . 1 442 . 78 THR HG2 H 0.80 . 1 443 . 79 LYS H H 7.96 . 1 444 . 79 LYS HA H 4.63 . 1 445 . 79 LYS HB2 H 1.96 . 1 446 . 79 LYS HB3 H 2.31 . 1 447 . 79 LYS HG2 H 1.79 . 1 448 . 79 LYS HG3 H 2.08 . 1 449 . 79 LYS HD2 H 1.90 . 1 450 . 79 LYS HD3 H 1.70 . 1 451 . 79 LYS HE2 H 3.46 . 1 452 . 79 LYS HE3 H 3.46 . 1 453 . 80 MET H H 7.13 . 1 454 . 80 MET HA H 3.10 . 1 455 . 80 MET HB2 H -0.22 . 1 456 . 80 MET HB3 H -2.64 . 1 457 . 80 MET HG2 H -1.89 . 1 458 . 80 MET HG3 H -3.77 . 1 459 . 80 MET HE H -3.30 . 1 460 . 81 ILE H H 8.01 . 1 461 . 81 ILE HA H 3.59 . 1 462 . 81 ILE HB H 2.10 . 1 463 . 81 ILE HG12 H 1.30 . 1 464 . 81 ILE HG13 H 1.44 . 1 465 . 81 ILE HG2 H 0.78 . 1 466 . 81 ILE HD1 H 0.68 . 1 467 . 82 PHE H H 6.55 . 1 468 . 82 PHE HA H 4.28 . 1 469 . 82 PHE HB2 H 0.55 . 1 470 . 82 PHE HB3 H 2.17 . 1 471 . 82 PHE HD1 H 6.70 . 1 472 . 82 PHE HD2 H 6.70 . 1 473 . 82 PHE HE1 H 7.39 . 1 474 . 82 PHE HE2 H 7.39 . 1 475 . 82 PHE HZ H 7.23 . 1 476 . 83 ALA H H 8.28 . 1 477 . 83 ALA HA H 3.63 . 1 478 . 83 ALA HB H 1.09 . 1 479 . 84 GLY HA2 H 2.99 . 1 480 . 84 GLY HA3 H 4.27 . 1 481 . 85 ILE H H 8.47 . 1 482 . 85 ILE HA H 4.29 . 1 483 . 85 ILE HB H 1.48 . 1 484 . 85 ILE HG12 H 1.29 . 1 485 . 85 ILE HG13 H 1.73 . 1 486 . 85 ILE HG2 H 1.06 . 1 487 . 85 ILE HD1 H 1.01 . 1 488 . 86 LYS H H 8.72 . 1 489 . 86 LYS HA H 4.08 . 1 490 . 86 LYS HB2 H 1.84 . 1 491 . 86 LYS HB3 H 1.84 . 1 492 . 86 LYS HG2 H 1.48 . 1 493 . 86 LYS HG3 H 1.62 . 1 494 . 87 LYS H H 8.41 . 1 495 . 87 LYS HA H 4.30 . 1 496 . 87 LYS HB2 H 1.62 . 1 497 . 87 LYS HB3 H 1.73 . 1 498 . 87 LYS HG2 H 1.50 . 1 499 . 87 LYS HG3 H 1.87 . 1 500 . 87 LYS HE2 H 3.03 . 1 501 . 87 LYS HE3 H 3.03 . 1 502 . 88 LYS H H 9.13 . 1 503 . 88 LYS HA H 3.40 . 1 504 . 88 LYS HB2 H 1.90 . 1 505 . 88 LYS HB3 H 1.90 . 1 506 . 88 LYS HG2 H 1.34 . 1 507 . 88 LYS HG3 H 1.34 . 1 508 . 89 THR H H 8.37 . 1 509 . 89 THR HA H 4.12 . 1 510 . 89 THR HB H 4.20 . 1 511 . 89 THR HG2 H 1.34 . 1 512 . 90 GLU H H 6.34 . 1 513 . 90 GLU HA H 4.31 . 1 514 . 90 GLU HB2 H 2.01 . 1 515 . 90 GLU HB3 H 2.09 . 1 516 . 90 GLU HG2 H 2.32 . 1 517 . 90 GLU HG3 H 2.43 . 1 518 . 91 ARG H H 7.50 . 1 519 . 91 ARG HA H 3.89 . 1 520 . 91 ARG HB2 H 2.18 . 1 521 . 91 ARG HB3 H 2.18 . 1 522 . 91 ARG HD2 H 3.35 . 1 523 . 91 ARG HD3 H 3.35 . 1 524 . 92 GLU H H 8.61 . 1 525 . 92 GLU HA H 3.89 . 1 526 . 92 GLU HB2 H 2.48 . 1 527 . 92 GLU HB3 H 2.48 . 1 528 . 92 GLU HG2 H 2.20 . 1 529 . 92 GLU HG3 H 2.33 . 1 530 . 93 ASP H H 8.54 . 1 531 . 93 ASP HA H 4.28 . 1 532 . 93 ASP HB2 H 2.68 . 1 533 . 93 ASP HB3 H 2.75 . 1 534 . 94 LEU H H 8.41 . 1 535 . 94 LEU HA H 4.31 . 1 536 . 94 LEU HB2 H 2.32 . 1 537 . 94 LEU HB3 H 2.32 . 1 538 . 94 LEU HG H 1.86 . 1 539 . 94 LEU HD1 H 1.49 . 1 540 . 94 LEU HD2 H 1.56 . 1 541 . 95 ILE H H 9.02 . 1 542 . 95 ILE HA H 3.73 . 1 543 . 95 ILE HB H 2.09 . 1 544 . 95 ILE HG12 H 1.99 . 1 545 . 95 ILE HG13 H 1.99 . 1 546 . 95 ILE HG2 H 1.22 . 1 547 . 95 ILE HD1 H 0.97 . 1 548 . 96 ALA H H 8.15 . 1 549 . 96 ALA HA H 4.14 . 1 550 . 96 ALA HB H 1.42 . 1 551 . 97 TYR H H 8.20 . 1 552 . 97 TYR HA H 4.24 . 1 553 . 97 TYR HB2 H 3.68 . 1 554 . 97 TYR HB3 H 3.15 . 1 555 . 97 TYR HD1 H 7.14 . 1 556 . 97 TYR HD2 H 6.71 . 1 557 . 97 TYR HE1 H 5.52 . 1 558 . 97 TYR HE2 H 6.59 . 1 559 . 98 LEU H H 9.12 . 1 560 . 98 LEU HA H 3.43 . 1 561 . 98 LEU HB2 H 2.33 . 1 562 . 98 LEU HB3 H 2.32 . 1 563 . 98 LEU HG H 2.21 . 1 564 . 98 LEU HD1 H 1.12 . 1 565 . 98 LEU HD2 H 0.71 . 1 566 . 99 LYS H H 9.04 . 1 567 . 99 LYS HA H 2.61 . 1 568 . 99 LYS HB2 H 1.30 . 1 569 . 99 LYS HB3 H 1.60 . 1 570 . 99 LYS HG2 H 0.26 . 1 571 . 99 LYS HG3 H 0.80 . 1 572 . 100 LYS H H 6.87 . 1 573 . 100 LYS HA H 4.06 . 1 574 . 100 LYS HB2 H 1.75 . 1 575 . 100 LYS HB3 H 1.75 . 1 576 . 100 LYS HG2 H 1.22 . 1 577 . 100 LYS HG3 H 1.60 . 1 578 . 100 LYS HD2 H 1.41 . 1 579 . 100 LYS HD3 H 1.41 . 1 580 . 100 LYS HE2 H 2.99 . 1 581 . 100 LYS HE3 H 2.99 . 1 582 . 101 ALA H H 8.68 . 1 583 . 101 ALA HA H 3.89 . 1 584 . 101 ALA HB H 0.56 . 1 585 . 102 THR H H 7.99 . 1 586 . 102 THR HA H 4.22 . 1 587 . 102 THR HB H 4.64 . 1 588 . 102 THR HG2 H 0.95 . 1 589 . 103 ASN H H 7.08 . 1 590 . 103 ASN HA H 4.87 . 1 591 . 103 ASN HB2 H 2.54 . 1 592 . 103 ASN HB3 H 2.82 . 1 593 . 103 ASN HD21 H 6.53 . 1 594 . 103 ASN HD22 H 7.93 . 1 595 . 104 GLU H H 7.32 . 1 596 . 104 GLU HA H 4.22 . 1 597 . 104 GLU HB2 H 1.95 . 1 598 . 104 GLU HB3 H 1.95 . 1 599 . 104 GLU HG2 H 2.29 . 1 600 . 104 GLU HG3 H 2.29 . 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name heme _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 HEC QM1 H 3.50 . 1 2 . 1 HEC HT2A H 5.20 . 1 3 . 1 HEC QT2 H 1.44 . 1 4 . 1 HEC QM3 H 3.84 . 1 5 . 1 HEC HT4A H 6.36 . 1 6 . 1 HEC QT4 H 2.58 . 1 7 . 1 HEC QM5 H 3.59 . 1 8 . 1 HEC HP61 H 3.46 . 1 9 . 1 HEC HP62 H 4.17 . 1 10 . 1 HEC HP64 H 3.93 . 1 11 . 1 HEC HP72 H 3.63 . 1 12 . 1 HEC HP71 H 4.14 . 1 13 . 1 HEC QM8 H 2.16 . 1 14 . 1 HEC HAM H 9.29 . 1 15 . 1 HEC HBM H 9.62 . 1 16 . 1 HEC HGM H 9.59 . 1 17 . 1 HEC HDM H 9.02 . 1 stop_ save_