data_5079 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone dynamics of the functional domain of Paracoccus denitrificans Cytochrome c552 in the Reduced state ; _BMRB_accession_number 5079 _BMRB_flat_file_name bmr5079.str _Entry_type original _Submission_date 2001-07-14 _Accession_date 2001-07-16 _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 Reincke Britta . . 2 Perez Carlos . . 3 Pristovsek Primoz . . 4 Luecke Christian . . 5 Ludwig Christian . . 6 Loehr Frank . . 7 Rogov Vladimir V. . 8 Ludwig Bernd . . 9 Rueterjans Heinz . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count T1_relaxation 2 T2_relaxation 2 heteronucl_NOE 2 stop_ loop_ _Data_type _Data_type_count "T1 relaxation values" 178 "T2 relaxation values" 177 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-10-16 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4471 'chemical shift assignments of reduced cytochrome c552' 4777 'chemical shift assignments of oxidized cytochrome c552' 5080 'cytochrome c552 oxidized' stop_ _Original_release_date 2001-10-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and Dynamics of the Functional Domain of Paracoccus denitrificans Cytochrome c552 in both Redox States ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11591150 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Reincke Britta . . 2 Perez Carlos . . 3 Pristovsek Primoz . . 4 Luecke Christian . . 5 Ludwig Christian . . 6 Loehr Frank . . 7 Rogov Vladimir V. . 8 Ludwig Bernd . . 9 Rueterjans Heinz . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12312 _Page_last 12320 _Year 2001 _Details . loop_ _Keyword cytochromes 'electron-transfer pathways' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Pristovsek, P., Luecke, C., Reincke, B., Loehr, F., Ludwig, B. & Rueterjans, H. (2000). Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state. J. Biomol. NMR, 16, 353-354. ; _Citation_title 'Complete 1H, 15N and 13C assignment of the functional domain of paracoccus denitrificans cytochrome c552 in the reduced state.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10826890 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pristovsek P. . . 2 Luecke C. . . 3 Reincke B. . . 4 Lohr F. . . 5 Ludwig B. . . 6 Ruterjans H. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 16 _Journal_issue 4 _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 353 _Page_last 354 _Year 2000 _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; Pristovsek, P., Luecke, C., Reincke, B., Ludwig, B. & Rueterjans, H. (2000) Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state. Eur. J. Biochem. 267, 4205-4212. ; _Citation_title 'Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10866825 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pristovsek P. . . 2 Luecke C. . . 3 Reincke B. . . 4 Ludwig B. . . 5 Ruterjans H. . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European journal of biochemistry / FEBS' _Journal_volume 267 _Journal_issue 13 _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 4205 _Page_last 4212 _Year 2000 _Details ; In order to determine the solution structure of Paracoccus denitrificans cytochrome c552 by NMR, we cloned and isotopically labeled a 10.5-kDa soluble fragment (100 residues) containing the functional domain of the 18.2-kDa membrane-bound protein. Using uniformly 15N-enriched samples of cytochrome c552 in the reduced state, a variety of two-dimensional and three-dimensional heteronuclear double-resonance NMR experiments was employed to achieve complete 1H and 15N assignments. A total of 1893 distance restraints was derived from homonuclear 2D-NOESY and heteronuclear 3D-NOESY spectra; 1486 meaningful restraints were used in the structure calculations. After restrained energy minimization a family of 20 structures was obtained with rmsd values of 0.56 +/- 0. 10 A and 1.09 +/- 0.09 A for the backbone and heavy atoms, respectively. The overall topology is similar to that seen in previously reported models of this class of proteins. The global fold consists of two long helices at the N-terminus and C-terminus and three shorter helices surrounding the heme moiety; the helices are connected by well-defined loops. Comparison with the X-ray structure shows some minor differences in the positions of the Trp57 and Phe65 side-chain rings as well as the heme propionate groups. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Reincke, B., Thoeny-Meyer, L., Dannehl, C., Odenwald, A., Aidim, M., Witt, H., Rueterjans, H. & Ludwig, B. (1999) Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase. Biochim. Biophys. Acta, 1441, 114-120. ; _Citation_title 'Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10216157 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Reincke B. . . 2 Thony-Meyer L. . . 3 Dannehl C. . . 4 Odenwald A. . . 5 Aidim M. . . 6 Witt H. . . 7 Ruterjans H. . . 8 Ludwig B. . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_name_full 'Biochimica et biophysica acta' _Journal_volume 1411 _Journal_issue 1 _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 114 _Page_last 120 _Year 1999 _Details ; A membrane-bound c-type cytochrome, c552, acts as the electron mediator between the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a soluble cytochrome c interacts with both complexes, the bacterial c552, the product of the cycM gene, shows a tripartite structure, with an N-terminal membrane anchor separated from a typical class I cytochrome domain by a highly charged region. Two derivative fragments, lacking either only the membrane spanning region or both N-terminal domains, were constructed on the genetic level, and expressed in Escherichia coli cotransformed with the ccm gene cluster encoding host-specific cytochrome c maturation factors. High levels of cytochromes c were expressed and located in the periplasm as holo-proteins; both these purified c552 fragments are functional in electron transport to oxidase, as ascertained by kinetic measurements, and will prove useful for future structural studies of complex formation by NMR and X-ray diffraction. ; save_ save_ref_4 _Saveframe_category citation _Citation_full ; Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene. Eur. J. Biochem., 231, 259-265. ; _Citation_title 'Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7628479 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Turba A. . . 2 Jetzek M. . . 3 Ludwig B. . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European journal of biochemistry / FEBS' _Journal_volume 231 _Journal_issue 1 _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 259 _Page_last 265 _Year 1995 _Details ; Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes in different branches of their electron transport system. Among the many cytochromes c present in the soil bacterium Paracoccus denitrificans, a membrane-bound cytochrome (c552) has been suggested to mediate the electron transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry, E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have purified this cytochrome from cytoplasmic membranes, and cloned and sequenced its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is highly similar to type-I cytochromes c, its N-terminal part contains a hydrophobic segment providing membrane attachment. In addition, we present immunological evidence for its functional role in respiration. ; save_ ################################## # Molecular system description # ################################## save_cyt_c552_system _Saveframe_category molecular_system _Mol_system_name 'cytochrome c552' _Abbreviation_common 'cyt c552' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cyt c552' $cyt_c552 'heme c' $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'electron-transfer mediator in bacterial respiratory chain' stop_ _Database_query_date . _Details ; SWISS-PROT P54820 'CYTOCHROME C-552' This deposit represents the soluble fragment containing the functional domain which starts at position 78 and is preceded by an additional Met residue. ; save_ ######################## # Monomeric polymers # ######################## save_cyt_c552 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Paracoccus denitrificans cytochrome c552, soluble fragment' _Abbreviation_common 'cyt c552' _Molecular_mass 10528 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; MADPAAGEKVFGKCKACHKL DGNDGVGPHLNGVVGRTVAG VDGFNYSDPMKAHGGDWTPE ALQEFLTNPKAVVKGTKMAF AGLPKIEDRANLIAYLEGQQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 PRO 5 ALA 6 ALA 7 GLY 8 GLU 9 LYS 10 VAL 11 PHE 12 GLY 13 LYS 14 CYS 15 LYS 16 ALA 17 CYS 18 HIS 19 LYS 20 LEU 21 ASP 22 GLY 23 ASN 24 ASP 25 GLY 26 VAL 27 GLY 28 PRO 29 HIS 30 LEU 31 ASN 32 GLY 33 VAL 34 VAL 35 GLY 36 ARG 37 THR 38 VAL 39 ALA 40 GLY 41 VAL 42 ASP 43 GLY 44 PHE 45 ASN 46 TYR 47 SER 48 ASP 49 PRO 50 MET 51 LYS 52 ALA 53 HIS 54 GLY 55 GLY 56 ASP 57 TRP 58 THR 59 PRO 60 GLU 61 ALA 62 LEU 63 GLN 64 GLU 65 PHE 66 LEU 67 THR 68 ASN 69 PRO 70 LYS 71 ALA 72 VAL 73 VAL 74 LYS 75 GLY 76 THR 77 LYS 78 MET 79 ALA 80 PHE 81 ALA 82 GLY 83 LEU 84 PRO 85 LYS 86 ILE 87 GLU 88 ASP 89 ARG 90 ALA 91 ASN 92 LEU 93 ILE 94 ALA 95 TYR 96 LEU 97 GLU 98 GLY 99 GLN 100 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-09-14 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 4471 cyt_c552 100.00 100 100.00 100.00 2.08e-66 BMRB 4777 cyt_c552 100.00 100 100.00 100.00 2.08e-66 BMRB 5080 cyt_c552 100.00 100 100.00 100.00 2.08e-66 PDB 1C7M "Solution Structure Of The Functional Domain Of Paracoccus Denitrificans Cytochrome C552 In The Reduced State" 100.00 100 100.00 100.00 2.08e-66 PDB 1I6D "Solution Structure Of The Functional Domain Of Paracoccus Denitrificans Cytochrome C552 In The Reduced State" 100.00 100 100.00 100.00 2.08e-66 PDB 1I6E "Solution Structure Of The Functional Domain Of Paracoccus Denitrificans Cytochrome C552 In The Oxidized State" 100.00 100 100.00 100.00 2.08e-66 PDB 1QL3 "Structure Of The Soluble Domain Of Cytochrome C552 From Paracoccus Denitrificans In The Reduced State" 99.00 99 100.00 100.00 1.49e-65 PDB 1QL4 "Structure Of The Soluble Domain Of Cytochrome C552 From Paracoccus Denitrificans In The Oxidised State" 99.00 99 100.00 100.00 1.49e-65 PDB 3M97 "Structure Of The Soluble Domain Of Cytochrome C552 With Its Flexible Linker Segment From Paracoccus Denitrificans" 99.00 140 100.00 100.00 1.46e-65 EMBL CAA49830 "cytochrome C552 [Paracoccus denitrificans]" 99.00 176 100.00 100.00 1.08e-65 GB ABL69905 "cytochrome c, class I [Paracoccus denitrificans PD1222]" 99.00 176 100.00 100.00 9.68e-66 REF WP_011748102 "cytochrome C [Paracoccus denitrificans]" 99.00 176 100.00 100.00 9.68e-66 REF YP_915601 "cytochrome c, class I [Paracoccus denitrificans PD1222]" 99.00 176 100.00 100.00 9.68e-66 SP P54820 "RecName: Full=Cytochrome c-552; AltName: Full=Cytochrome c552 [Paracoccus denitrificans]" 99.00 176 100.00 100.00 1.08e-65 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 15:50:33 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 _ATCC_number $cyt_c552 . 266 Eubacteria . Paracoccus denitrificans 13543 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $cyt_c552 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET-22b(+) 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $cyt_c552 . mM 1.5 4 '[U-96% 15N]' 'potassium phosphate' 20 mM . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_XWIN-NMR _Saveframe_category software _Name XWIN-NMR _Version 1.3 loop_ _Task 'data collection and processing' stop_ _Details . save_ save_RMX _Saveframe_category software _Name RMX _Version 'rev. II/1997' loop_ _Task 'data analysis' stop_ _Details . save_ save_MODELFREE _Saveframe_category software _Name MODELFREE _Version 4.01 loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T1' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T2' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '{1H}-15N NOE' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details ; small excess sodium dithionite as reducing agent ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.2 n/a temperature 298 0.1 K stop_ save_ save_15N_T1_500 _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Spectrometer_frequency_1H 500 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name 'cyt c552' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 2 ALA N 0.802 0.031 2 3 ASP N 0.536 0.005 3 5 ALA N 0.488 0.005 4 6 ALA N 0.483 0.004 5 7 GLY N 0.463 0.005 6 8 GLU N 0.485 0.009 7 9 LYS N 0.465 0.004 8 10 VAL N 0.468 0.003 9 11 PHE N 0.474 0.008 10 12 GLY N 0.443 0.006 11 13 LYS N 0.482 0.014 12 14 CYS N 0.478 0.005 13 15 LYS N 0.474 0.005 14 16 ALA N 0.474 0.004 15 17 CYS N 0.480 0.010 16 18 HIS N 0.496 0.006 17 19 LYS N 0.508 0.007 18 20 LEU N 0.504 0.006 19 22 GLY N 0.467 0.005 20 23 ASN N 0.477 0.005 21 24 ASP N 0.535 0.006 22 25 GLY N 0.552 0.004 23 26 VAL N 0.523 0.008 24 27 GLY N 0.483 0.008 25 29 HIS N 0.469 0.009 26 30 LEU N 0.443 0.004 27 31 ASN N 0.449 0.004 28 32 GLY N 0.497 0.008 29 33 VAL N 0.447 0.007 30 34 VAL N 0.447 0.005 31 35 GLY N 0.464 0.002 32 36 ARG N 0.454 0.005 33 37 THR N 0.496 0.007 34 38 VAL N 0.513 0.005 35 39 ALA N 0.477 0.008 36 40 GLY N 0.502 0.009 37 41 VAL N 0.499 0.006 38 42 ASP N 0.438 0.005 39 43 GLY N 0.536 0.007 40 44 PHE N 0.498 0.004 41 45 ASN N 0.492 0.008 42 46 TYR N 0.520 0.005 43 47 SER N 0.509 0.008 44 48 ASP N 0.482 0.002 45 50 MET N 0.474 0.004 46 51 LYS N 0.464 0.004 47 54 GLY N 0.509 0.009 48 55 GLY N 0.526 0.006 49 56 ASP N 0.504 0.005 50 57 TRP N 0.494 0.003 51 58 THR N 0.470 0.005 52 60 GLU N 0.485 0.003 53 61 ALA N 0.447 0.005 54 62 LEU N 0.466 0.003 55 63 GLN N 0.465 0.005 56 65 PHE N 0.448 0.006 57 66 LEU N 0.455 0.003 58 67 THR N 0.466 0.005 59 68 ASN N 0.497 0.004 60 70 LYS N 0.500 0.005 61 71 ALA N 0.476 0.004 62 72 VAL N 0.503 0.004 63 73 VAL N 0.466 0.008 64 74 LYS N 0.510 0.004 65 75 GLY N 0.506 0.005 66 76 THR N 0.477 0.005 67 77 LYS N 0.472 0.007 68 78 MET N 0.461 0.005 69 79 ALA N 0.490 0.006 70 80 PHE N 0.669 0.010 71 81 ALA N 0.451 0.012 72 82 GLY N 0.496 0.024 73 83 LEU N 0.495 0.005 74 85 LYS N 0.448 0.010 75 86 ILE N 0.476 0.003 76 87 GLU N 0.463 0.003 77 88 ASP N 0.461 0.005 78 89 ARG N 0.473 0.004 79 90 ALA N 0.447 0.008 80 91 ASN N 0.461 0.002 81 92 LEU N 0.444 0.004 82 93 ILE N 0.459 0.006 83 94 ALA N 0.460 0.003 84 95 TYR N 0.476 0.005 85 96 LEU N 0.439 0.006 86 97 GLU N 0.481 0.006 87 98 GLY N 0.468 0.003 88 99 GLN N 0.475 0.006 89 100 GLN N 0.655 0.006 stop_ save_ save_15N_T1_600 _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name 'cyt c552' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 2 ALA N 0.804 0.023 2 3 ASP N 0.629 0.005 3 5 ALA N 0.583 0.003 4 6 ALA N 0.582 0.011 5 7 GLY N 0.565 0.006 6 8 GLU N 0.558 0.003 7 9 LYS N 0.570 0.012 8 10 VAL N 0.559 0.003 9 11 PHE N 0.565 0.003 10 12 GLY N 0.553 0.003 11 13 LYS N 0.553 0.001 12 14 CYS N 0.586 0.008 13 15 LYS N 0.587 0.011 14 16 ALA N 0.576 0.008 15 17 CYS N 0.623 0.008 16 18 HIS N 0.605 0.018 17 19 LYS N 0.630 0.004 18 20 LEU N 0.608 0.006 19 22 GLY N 0.565 0.009 20 23 ASN N 0.584 0.003 21 24 ASP N 0.630 0.003 22 25 GLY N 0.660 0.018 23 26 VAL N 0.602 0.003 24 27 GLY N 0.575 0.005 25 29 HIS N 0.577 0.009 26 30 LEU N 0.560 0.006 27 31 ASN N 0.523 0.004 28 32 GLY N 0.609 0.010 29 33 VAL N 0.549 0.003 30 34 VAL N 0.530 0.003 31 35 GLY N 0.554 0.003 32 36 ARG N 0.531 0.008 33 37 THR N 0.568 0.004 34 38 VAL N 0.622 0.004 35 39 ALA N 0.580 0.006 36 40 GLY N 0.617 0.004 37 41 VAL N 0.583 0.004 38 42 ASP N 0.528 0.004 39 43 GLY N 0.644 0.005 40 44 PHE N 0.586 0.006 41 45 ASN N 0.587 0.030 42 46 TYR N 0.640 0.007 43 47 SER N 0.600 0.006 44 48 ASP N 0.563 0.002 45 50 MET N 0.557 0.004 46 51 LYS N 0.555 0.003 47 54 GLY N 0.589 0.003 48 55 GLY N 0.632 0.074 49 56 ASP N 0.592 0.003 50 57 TRP N 0.589 0.007 51 58 THR N 0.596 0.011 52 60 GLU N 0.556 0.025 53 61 ALA N 0.543 0.012 54 62 LEU N 0.547 0.004 55 63 GLN N 0.547 0.002 56 65 PHE N 0.545 0.003 57 66 LEU N 0.539 0.005 58 67 THR N 0.551 0.005 59 68 ASN N 0.590 0.006 60 70 LYS N 0.575 0.015 61 71 ALA N 0.577 0.003 62 72 VAL N 0.594 0.047 63 73 VAL N 0.582 0.003 64 74 LYS N 0.604 0.008 65 75 GLY N 0.607 0.015 66 76 THR N 0.545 0.011 67 77 LYS N 0.549 0.005 68 78 MET N 0.542 0.055 69 79 ALA N 0.586 0.007 70 80 PHE N 0.847 0.005 71 81 ALA N 0.570 0.024 72 82 GLY N 0.610 0.010 73 83 LEU N 0.561 0.020 74 85 LYS N 0.570 0.002 75 86 ILE N 0.564 0.003 76 87 GLU N 0.542 0.004 77 88 ASP N 0.565 0.004 78 89 ARG N 0.560 0.004 79 90 ALA N 0.552 0.002 80 91 ASN N 0.556 0.007 81 92 LEU N 0.515 0.018 82 93 ILE N 0.547 0.031 83 94 ALA N 0.541 0.007 84 95 TYR N 0.553 0.003 85 96 LEU N 0.541 0.003 86 97 GLU N 0.551 0.002 87 98 GLY N 0.556 0.008 88 99 GLN N 0.569 0.006 89 100 GLN N 0.772 0.006 stop_ save_ save_15N_T2_500 _Saveframe_category T2_relaxation _Details . loop_ _Experiment_label $_1 stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Spectrometer_frequency_1H 500 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name 'cyt c552' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 2 ALA N 0.266 0.005 . . 2 3 ASP N 0.134 0.001 . . 3 5 ALA N 0.125 0.001 . . 4 6 ALA N 0.126 0.001 . . 5 7 GLY N 0.124 0.001 . . 6 9 LYS N 0.115 0.001 . . 7 10 VAL N 0.118 0.001 . . 8 11 PHE N 0.113 0.001 . . 9 12 GLY N 0.114 0.001 . . 10 13 LYS N 0.111 0.002 . . 11 14 CYS N 0.117 0.001 . . 12 15 LYS N 0.112 0.001 . . 13 16 ALA N 0.118 0.000 . . 14 17 CYS N 0.110 0.005 . . 15 18 HIS N 0.118 0.001 . . 16 19 LYS N 0.121 0.001 . . 17 20 LEU N 0.128 0.001 . . 18 22 GLY N 0.117 0.002 . . 19 23 ASN N 0.113 0.001 . . 20 24 ASP N 0.128 0.001 . . 21 25 GLY N 0.151 0.001 . . 22 26 VAL N 0.133 0.003 . . 23 27 GLY N 0.122 0.001 . . 24 29 HIS N 0.113 0.001 . . 25 30 LEU N 0.120 0.001 . . 26 31 ASN N 0.109 0.001 . . 27 32 GLY N 0.117 0.001 . . 28 33 VAL N 0.116 0.001 . . 29 34 VAL N 0.115 0.000 . . 30 35 GLY N 0.118 0.001 . . 31 36 ARG N 0.114 0.001 . . 32 37 THR N 0.113 0.001 . . 33 38 VAL N 0.130 0.003 . . 34 39 ALA N 0.117 0.001 . . 35 40 GLY N 0.129 0.002 . . 36 41 VAL N 0.123 0.002 . . 37 42 ASP N 0.124 0.004 . . 38 43 GLY N 0.142 0.001 . . 39 44 PHE N 0.129 0.001 . . 40 45 ASN N 0.132 0.001 . . 41 46 TYR N 0.134 0.001 . . 42 47 SER N 0.115 0.001 . . 43 48 ASP N 0.122 0.000 . . 44 50 MET N 0.119 0.001 . . 45 51 LYS N 0.117 0.001 . . 46 54 GLY N 0.133 0.001 . . 47 55 GLY N 0.131 0.001 . . 48 56 ASP N 0.125 0.001 . . 49 57 TRP N 0.126 0.001 . . 50 58 THR N 0.120 0.001 . . 51 60 GLU N 0.123 0.001 . . 52 61 ALA N 0.115 0.001 . . 53 62 LEU N 0.114 0.001 . . 54 63 GLN N 0.116 0.000 . . 55 65 PHE N 0.118 0.001 . . 56 66 LEU N 0.118 0.001 . . 57 67 THR N 0.116 0.001 . . 58 68 ASN N 0.126 0.002 . . 59 70 LYS N 0.121 0.001 . . 60 71 ALA N 0.114 0.000 . . 61 72 VAL N 0.129 0.001 . . 62 73 VAL N 0.119 0.001 . . 63 74 LYS N 0.138 0.001 . . 64 75 GLY N 0.124 0.001 . . 65 76 THR N 0.114 0.001 . . 66 77 LYS N 0.117 0.001 . . 67 78 MET N 0.120 0.001 . . 68 79 ALA N 0.132 0.001 . . 69 80 PHE N 0.181 0.001 . . 70 81 ALA N 0.125 0.001 . . 71 82 GLY N 0.130 0.003 . . 72 83 LEU N 0.125 0.001 . . 73 85 LYS N 0.124 0.001 . . 74 86 ILE N 0.126 0.001 . . 75 87 GLU N 0.118 0.001 . . 76 88 ASP N 0.114 0.001 . . 77 89 ARG N 0.114 0.001 . . 78 90 ALA N 0.114 0.001 . . 79 91 ASN N 0.114 0.001 . . 80 92 LEU N 0.114 0.001 . . 81 93 ILE N 0.113 0.001 . . 82 94 ALA N 0.111 0.000 . . 83 95 TYR N 0.117 0.001 . . 84 96 LEU N 0.112 0.001 . . 85 97 GLU N 0.113 0.001 . . 86 98 GLY N 0.124 0.002 . . 87 99 GLN N 0.125 0.001 . . 88 100 GLN N 0.204 0.002 . . stop_ save_ save_15N_T2_600 _Saveframe_category T2_relaxation _Details . loop_ _Experiment_label $_1 stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Spectrometer_frequency_1H 600 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name 'cyt c552' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 2 ALA N 0.270 0.005 . . 2 3 ASP N 0.140 0.001 . . 3 5 ALA N 0.123 0.001 . . 4 6 ALA N 0.129 0.001 . . 5 7 GLY N 0.127 0.004 . . 6 8 GLU N 0.115 0.001 . . 7 9 LYS N 0.114 0.001 . . 8 10 VAL N 0.118 0.001 . . 9 11 PHE N 0.109 0.001 . . 10 12 GLY N 0.106 0.003 . . 11 13 LYS N 0.110 0.002 . . 12 14 CYS N 0.107 0.001 . . 13 15 LYS N 0.105 0.002 . . 14 16 ALA N 0.113 0.001 . . 15 17 CYS N 0.105 0.018 . . 16 18 HIS N 0.102 0.001 . . 17 19 LYS N 0.101 0.002 . . 18 20 LEU N 0.121 0.002 . . 19 22 GLY N 0.116 0.001 . . 20 23 ASN N 0.109 0.001 . . 21 24 ASP N 0.130 0.001 . . 22 25 GLY N 0.155 0.002 . . 23 26 VAL N 0.125 0.001 . . 24 27 GLY N 0.118 0.001 . . 25 29 HIS N 0.105 0.004 . . 26 30 LEU N 0.111 0.002 . . 27 31 ASN N 0.104 0.001 . . 28 32 GLY N 0.115 0.001 . . 29 33 VAL N 0.110 0.001 . . 30 34 VAL N 0.111 0.001 . . 31 35 GLY N 0.113 0.001 . . 32 36 ARG N 0.114 0.001 . . 33 37 THR N 0.120 0.002 . . 34 38 VAL N 0.127 0.001 . . 35 39 ALA N 0.113 0.003 . . 36 40 GLY N 0.119 0.003 . . 37 41 VAL N 0.122 0.001 . . 38 42 ASP N 0.118 0.001 . . 39 43 GLY N 0.143 0.001 . . 40 44 PHE N 0.124 0.001 . . 41 45 ASN N 0.132 0.001 . . 42 46 TYR N 0.141 0.002 . . 43 47 SER N 0.111 0.001 . . 44 48 ASP N 0.122 0.001 . . 45 50 MET N 0.114 0.001 . . 46 51 LYS N 0.115 0.001 . . 47 54 GLY N 0.128 0.001 . . 48 55 GLY N 0.127 0.001 . . 49 56 ASP N 0.122 0.001 . . 50 57 TRP N 0.127 0.001 . . 51 58 THR N 0.118 0.000 . . 52 60 GLU N 0.121 0.000 . . 53 61 ALA N 0.121 0.001 . . 54 62 LEU N 0.115 0.001 . . 55 63 GLN N 0.118 0.001 . . 56 65 PHE N 0.113 0.001 . . 57 66 LEU N 0.120 0.001 . . 58 67 THR N 0.116 0.001 . . 59 68 ASN N 0.130 0.002 . . 60 70 LYS N 0.120 0.001 . . 61 71 ALA N 0.111 0.001 . . 62 72 VAL N 0.127 0.001 . . 63 73 VAL N 0.121 0.002 . . 64 74 LYS N 0.140 0.003 . . 65 75 GLY N 0.124 0.001 . . 66 76 THR N 0.115 0.001 . . 67 77 LYS N 0.123 0.001 . . 68 78 MET N 0.113 0.000 . . 69 79 ALA N 0.116 0.002 . . 70 80 PHE N 0.159 0.001 . . 71 81 ALA N 0.122 0.001 . . 72 82 GLY N 0.132 0.003 . . 73 83 LEU N 0.119 0.001 . . 74 85 LYS N 0.122 0.001 . . 75 86 ILE N 0.124 0.001 . . 76 87 GLU N 0.113 0.001 . . 77 88 ASP N 0.116 0.001 . . 78 89 ARG N 0.114 0.001 . . 79 90 ALA N 0.113 0.001 . . 80 91 ASN N 0.113 0.001 . . 81 92 LEU N 0.112 0.001 . . 82 93 ILE N 0.111 0.001 . . 83 94 ALA N 0.112 0.001 . . 84 95 TYR N 0.116 0.001 . . 85 96 LEU N 0.110 0.002 . . 86 97 GLU N 0.114 0.001 . . 87 98 GLY N 0.123 0.001 . . 88 99 GLN N 0.127 0.000 . . 89 100 GLN N 0.205 0.004 . . stop_ save_ save_heteronuclear_NOE_500 _Saveframe_category heteronuclear_NOE _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name ? _Atom_one_atom_name . _Atom_two_atom_name . _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value . _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 2 ALA -0.037 0.030 3 ASP 0.694 0.030 5 ALA 0.753 0.030 6 ALA 0.743 0.030 7 GLY 0.754 0.030 8 GLU 0.778 0.030 9 LYS 0.758 0.030 10 VAL 0.752 0.030 11 PHE 0.781 0.030 12 GLY 0.759 0.030 13 LYS 0.769 0.030 14 CYS 0.763 0.030 15 LYS 0.787 0.030 16 ALA 0.764 0.030 17 CYS 0.787 0.030 18 HIS 0.781 0.030 19 LYS 0.759 0.030 20 LEU 0.761 0.030 22 GLY 0.768 0.030 23 ASN 0.789 0.030 24 ASP 0.766 0.030 25 GLY 0.672 0.030 26 VAL 0.718 0.030 27 GLY 0.773 0.030 29 HIS 0.791 0.030 30 LEU 0.751 0.030 31 ASN 0.784 0.030 32 GLY 0.745 0.030 33 VAL 0.787 0.030 34 VAL 0.791 0.030 35 GLY 0.762 0.030 36 ARG 0.788 0.030 37 THR 0.806 0.030 38 VAL 0.766 0.030 39 ALA 0.773 0.030 40 GLY 0.787 0.030 41 VAL 0.752 0.030 42 ASP 0.760 0.030 43 GLY 0.746 0.030 44 PHE 0.767 0.030 45 ASN 0.764 0.030 46 TYR 0.749 0.030 47 SER 0.773 0.030 48 ASP 0.768 0.030 50 MET 0.746 0.030 51 LYS 0.754 0.030 54 GLY 0.728 0.030 55 GLY 0.753 0.030 56 ASP 0.736 0.030 57 TRP 0.772 0.030 58 THR 0.758 0.030 60 GLU 0.766 0.030 61 ALA 0.778 0.030 62 LEU 0.751 0.030 63 GLN 0.750 0.030 65 PHE 0.767 0.030 66 LEU 0.761 0.030 67 THR 0.780 0.030 68 ASN 0.807 0.030 70 LYS 0.733 0.030 71 ALA 0.752 0.030 72 VAL 0.738 0.030 73 VAL 0.763 0.030 74 LYS 0.714 0.030 75 GLY 0.744 0.030 76 THR 0.786 0.030 77 LYS 0.780 0.030 78 MET 0.728 0.030 79 ALA 0.742 0.030 80 PHE 0.590 0.030 81 ALA 0.799 0.030 83 LEU 0.748 0.030 85 LYS 0.767 0.030 86 ILE 0.722 0.030 87 GLU 0.764 0.030 88 ASP 0.752 0.030 89 ARG 0.769 0.030 90 ALA 0.768 0.030 91 ASN 0.758 0.030 92 LEU 0.757 0.030 93 ILE 0.769 0.030 94 ALA 0.767 0.030 95 TYR 0.725 0.030 96 LEU 0.780 0.030 97 GLU 0.759 0.030 98 GLY 0.736 0.030 99 GLN 0.724 0.030 100 GLN 0.363 0.030 stop_ save_ save_heteronuclear_NOE_600 _Saveframe_category heteronuclear_NOE _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name ? _Atom_one_atom_name . _Atom_two_atom_name . _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value . _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 2 ALA 0.016 0.030 3 ASP 0.722 0.030 5 ALA 0.808 0.030 6 ALA 0.795 0.030 7 GLY 0.790 0.030 8 GLU 0.811 0.030 9 LYS 0.808 0.030 10 VAL 0.800 0.030 11 PHE 0.803 0.030 12 GLY 0.789 0.030 13 LYS 0.795 0.030 14 CYS 0.807 0.030 15 LYS 0.806 0.030 16 ALA 0.803 0.030 17 CYS 0.826 0.030 18 HIS 0.808 0.030 19 LYS 0.776 0.030 20 LEU 0.795 0.030 22 GLY 0.835 0.030 23 ASN 0.820 0.030 24 ASP 0.796 0.030 25 GLY 0.717 0.030 26 VAL 0.770 0.030 27 GLY 0.796 0.030 29 HIS 0.832 0.030 30 LEU 0.778 0.030 31 ASN 0.826 0.030 32 GLY 0.792 0.030 33 VAL 0.816 0.030 34 VAL 0.818 0.030 35 GLY 0.801 0.030 36 ARG 0.820 0.030 37 THR 0.838 0.030 38 VAL 0.797 0.030 39 ALA 0.811 0.030 40 GLY 0.832 0.030 41 VAL 0.799 0.030 42 ASP 0.835 0.030 43 GLY 0.767 0.030 44 PHE 0.817 0.030 45 ASN 0.793 0.030 46 TYR 0.787 0.030 47 SER 0.807 0.030 48 ASP 0.807 0.030 50 MET 0.770 0.030 51 LYS 0.793 0.030 54 GLY 0.766 0.030 55 GLY 0.797 0.030 56 ASP 0.797 0.030 57 TRP 0.804 0.030 58 THR 0.806 0.030 60 GLU 0.807 0.030 61 ALA 0.796 0.030 62 LEU 0.779 0.030 63 GLN 0.794 0.030 65 PHE 0.794 0.030 66 LEU 0.818 0.030 67 THR 0.814 0.030 68 ASN 0.781 0.030 70 LYS 0.754 0.030 71 ALA 0.794 0.030 72 VAL 0.766 0.030 73 VAL 0.794 0.030 74 LYS 0.748 0.030 75 GLY 0.774 0.030 76 THR 0.814 0.030 77 LYS 0.785 0.030 78 MET 0.796 0.030 79 ALA 0.797 0.030 80 PHE 0.590 0.030 81 ALA 0.779 0.030 82 GLY 0.803 0.030 83 LEU 0.792 0.030 85 LYS 0.794 0.030 86 ILE 0.793 0.030 87 GLU 0.802 0.030 88 ASP 0.809 0.030 89 ARG 0.800 0.030 90 ALA 0.814 0.030 91 ASN 0.799 0.030 92 LEU 0.824 0.030 93 ILE 0.799 0.030 94 ALA 0.797 0.030 95 TYR 0.803 0.030 96 LEU 0.806 0.030 97 GLU 0.803 0.030 98 GLY 0.790 0.030 99 GLN 0.763 0.030 100 GLN 0.410 0.030 stop_ save_