data_4073 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4073 _Entry.Title ; Backbone 1H, 13C and 15N Chemical Shift Assignments for Oxidized Human Ferredoxin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1997-11-20 _Entry.Accession_date 1997-11-20 _Entry.Last_release_date 2016-09-15 _Entry.Original_release_date 2016-09-15 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Bin Xia . . . . 4073 2 Brian Volkman . F. . . 4073 3 John Markley . L. . . 4073 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4073 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 264 4073 '15N chemical shifts' 89 4073 '1H chemical shifts' 185 4073 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 1997-11-20 . original author 'original release' 4073 1 . . 2002-04-08 . update BMRB 'update of relationships' 4073 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4073 'Chemical Shift of Oxidized Human Ferredoxin' 4073 BMRB 5337 'Complete assignments of 1H, 13C and 15N Chemical Shifts for Oxidized Human Adrenodoxin (4-114)' 4073 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4073 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98191359 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Xia, B., Volkman, B. F. , and Markley, J. L., "Evidence for Oxidation-State-Dependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy," Biochemistry 37, 3965-3973 (1998). ; _Citation.Title ; Evidence for Oxidation-State-Dependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 37 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 3965 _Citation.Page_last 3973 _Citation.Year 1998 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Bin Xia . . . . 4073 1 2 Brian Volkman . F. . . 4073 1 3 John Markley . L. . . 4073 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'F2S2 cluster' 4073 1 'HuFd reduced' 4073 1 NMR 4073 1 adrenodoxin 4073 1 'human ferrodoxin (HuFd)' 4073 1 stop_ save_ save_citation_one _Citation.Sf_category citations _Citation.Sf_framecode citation_one _Citation.Entry_ID 4073 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7819194 _Citation.Full_citation ; Xia, B., Cheng, H., Skjeldal, L., Coghlan, V. M., Vickery, L. E., and Markley, J. L., Biochemistry 34, 180-187, (1995). ; _Citation.Title ; Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 34 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 180 _Citation.Page_last 187 _Citation.Year 1995 _Citation.Details ; Human mitochondrial ferredoxin is a [2Fe-2S] protein that functions to transfer electrons from NADPH-dependent ferredoxin reductase to cytochrome P450 enzymes. Two of the three histidines of human ferredoxin are strictly conserved in the sequences of all known vertebrate ferredoxins, and one of these (His56) is adjacent to Cys55, which serves as one of the ligands to the iron-sulfur cluster. All but 16 of its residues show sequence identity with those of bovine ferredoxin. It has been proposed for bovine ferredoxin that His56 hydrogen bonds with a labile sulfur and that the reduction of the iron-sulfur center is accompanied by the uptake of a proton by this histidine [Lambeth, J. D., Seybert, D. W., Lancaster, J. R., Jr., Salerno, J. C., & Kamin, H. (1982) Mol. Cell. Biochem. 45, 13-31]. In this paper, we report procedures for labeling human ferredoxin uniformly with 15N using 15NH4Cl and selectively with 13C by the incorporation of [U-13C]histidine. Most of the imidazole 1H, 13C, and 15N resonances of the three histidines have been assigned by heteronuclear two-dimensional single- and multiple-bond correlation spectroscopy. Site-directed mutagenesis was used in assigning the NMR signals from His56. The pKa values of His10 (6.5) and His62 (5.8) in oxidized human ferredoxin were found to be similar to those reported previously for the corresponding residues of bovine ferredoxin [Greenfield, N. J., Wu, X., & Jordan, F. (1989) Biochim. Biophys. Acta 995, 246-254; Miura, S., Tamita, S., & Ichikawa, Y. (1991) J. Biol. Chem. 266, 19212-19216].(ABSTRACT TRUNCATED AT 250 WORDS) ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 B Xia B. . . . 4073 2 2 H Cheng H. . . . 4073 2 3 L Skjeldal L. . . . 4073 2 4 'V M' Coghlan V. M. . . 4073 2 5 'L E' Vickery L. E. . . 4073 2 6 'J L' Markley J. L. . . 4073 2 stop_ save_ save_citation_two _Citation.Sf_category citations _Citation.Sf_framecode citation_two _Citation.Entry_ID 4073 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8755728 _Citation.Full_citation ; Xia B., Cheng H., Bandarian V., Reed G. H., & Markley J. L., Biochemistry 35, 9488-9495,(1996). ; _Citation.Title ; Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 35 _Citation.Journal_issue 29 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 9488 _Citation.Page_last 9495 _Citation.Year 1996 _Citation.Details ; Human ferredoxin, the human equivalent of bovine adrenodoxin, is a small iron-sulfur protein with one [2Fe-2S] cluster. It functions, as do other vertebrate ferredoxins, to transfer electrons during the processes of steroid hormone synthesis. A DNA fragment encoding the mature form of human ferredoxin was cloned into an expression vector under control of the T7 RNA polymerase/promoter system. The protein was overproduced in Escherichia coli, and the [2Fe-2S] cluster was incorporated into the protein by in vitro reconstitution. The overall yield was approximately 30 mg of purified, reconstituted ferredoxin per liter of culture. Four of the five cysteines in human ferredoxin are coordinated to the iron-sulfur cluster. First, the non-ligand cysteine (cysteine-95) was mutated to alanine, and then double mutants were created in which each of the other four cysteines (at positions 46, 52, 55, and 92) were mutated individually to serine. The wild-type ferredoxin and each of the five mutant proteins were studied by UV-visible spectroscopy and electron paramagnetic resonance spectroscopy. The EPR gav values of all five mutants were very similar to that of wild-type human ferredoxin. In the reduced state, three of the cysteine-to-serine mutants exhibited axial EPR spectra similar to that of wild-type, but one of the double mutants (C52S/C95A) exhibited a rhombic EPR spectrum. The UV-visible spectroscopic properties of the wild-type and the C95A mutant ferredoxins were identical, but those of the other cysteine-to-serine mutant proteins of human ferredoxin were quite different from those of the wild-type protein and each other. These results, along with those from cysteine-to-serine mutations in other ferredoxins, provide the basis for a more comprehensive theoretical and practical understanding of the features important to the ligation of [2Fe-2S] clusters, although they do not yet permit determination of which two cysteines ligate Fe(II) and which ligate Fe(III) in the reduced protein. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 B. Xia B. . . . 4073 3 2 H. Cheng H. . . . 4073 3 3 V. Bandarian V. . . . 4073 3 4 G.H. Reed G. H. . . 4073 3 5 J.L. Markley J. L. . . 4073 3 stop_ save_ save_citation_three _Citation.Sf_category citations _Citation.Sf_framecode citation_three _Citation.Entry_ID 4073 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation 'Chylla, R. A. & Markley, J. L. J. Magn. Reson. (Series B) 102, 148-154, (1993)' _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 R. Chylla A. . . . 4073 4 2 J.L. Markley J. L. . . 4073 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HuFd-ox _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HuFd-ox _Assembly.Entry_ID 4073 _Assembly.ID 1 _Assembly.Name 'oxidized human ferredoxin' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic yes _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'oxidized form of the protein' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4073 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 HuFd-ox 1 $HuFd-ox . . . native . . . . . 4073 1 2 2Fe2S 2 $FE . . . native . . . . . 4073 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 coordinate single . 1 . 1 CYS 46 46 SG . 2 . 2 FE 1 1 FE . . . . . . . . . . 4073 1 2 coordinate single . 1 . 1 CYS 52 52 SG . 2 . 2 FE 1 1 FE . . . . . . . . . . 4073 1 3 coordinate single . 1 . 1 CYS 92 92 SG . 2 . 2 FE 1 1 FE . . . . . . . . . . 4073 1 4 coordinate single . 1 . 1 CYS 95 95 SG . 2 . 2 FE 1 1 FE . . . . . . . . . . 4073 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1AYF . . . . . . 4073 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID HuFd-ox abbreviation 4073 1 'oxidized human ferredoxin' system 4073 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'cholesterol biosynthesis' 4073 1 'electron transfer' 4073 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HuFd-ox _Entity.Sf_category entity _Entity.Sf_framecode HuFd-ox _Entity.Entry_ID 4073 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'human ferredoxin' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; SSSEDKITVHFINRDGETLT TKGKVGDSLLDVVVENNLDI DGFGACEGTLACSTCHLIFE DHIYEKLDAITDEENDMLDL AYGLTDRSRLGCQICLTKSM DNMTVRVPETVADARQSIDV GKTS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 124 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 13800 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID HuFd abbreviation 4073 1 HuFd-ox variant 4073 1 'human ferredoxin' common 4073 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . SER . 4073 1 2 . SER . 4073 1 3 . SER . 4073 1 4 . GLU . 4073 1 5 . ASP . 4073 1 6 . LYS . 4073 1 7 . ILE . 4073 1 8 . THR . 4073 1 9 . VAL . 4073 1 10 . HIS . 4073 1 11 . PHE . 4073 1 12 . ILE . 4073 1 13 . ASN . 4073 1 14 . ARG . 4073 1 15 . ASP . 4073 1 16 . GLY . 4073 1 17 . GLU . 4073 1 18 . THR . 4073 1 19 . LEU . 4073 1 20 . THR . 4073 1 21 . THR . 4073 1 22 . LYS . 4073 1 23 . GLY . 4073 1 24 . LYS . 4073 1 25 . VAL . 4073 1 26 . GLY . 4073 1 27 . ASP . 4073 1 28 . SER . 4073 1 29 . LEU . 4073 1 30 . LEU . 4073 1 31 . ASP . 4073 1 32 . VAL . 4073 1 33 . VAL . 4073 1 34 . VAL . 4073 1 35 . GLU . 4073 1 36 . ASN . 4073 1 37 . ASN . 4073 1 38 . LEU . 4073 1 39 . ASP . 4073 1 40 . ILE . 4073 1 41 . ASP . 4073 1 42 . GLY . 4073 1 43 . PHE . 4073 1 44 . GLY . 4073 1 45 . ALA . 4073 1 46 . CYS . 4073 1 47 . GLU . 4073 1 48 . GLY . 4073 1 49 . THR . 4073 1 50 . LEU . 4073 1 51 . ALA . 4073 1 52 . CYS . 4073 1 53 . SER . 4073 1 54 . THR . 4073 1 55 . CYS . 4073 1 56 . HIS . 4073 1 57 . LEU . 4073 1 58 . ILE . 4073 1 59 . PHE . 4073 1 60 . GLU . 4073 1 61 . ASP . 4073 1 62 . HIS . 4073 1 63 . ILE . 4073 1 64 . TYR . 4073 1 65 . GLU . 4073 1 66 . LYS . 4073 1 67 . LEU . 4073 1 68 . ASP . 4073 1 69 . ALA . 4073 1 70 . ILE . 4073 1 71 . THR . 4073 1 72 . ASP . 4073 1 73 . GLU . 4073 1 74 . GLU . 4073 1 75 . ASN . 4073 1 76 . ASP . 4073 1 77 . MET . 4073 1 78 . LEU . 4073 1 79 . ASP . 4073 1 80 . LEU . 4073 1 81 . ALA . 4073 1 82 . TYR . 4073 1 83 . GLY . 4073 1 84 . LEU . 4073 1 85 . THR . 4073 1 86 . ASP . 4073 1 87 . ARG . 4073 1 88 . SER . 4073 1 89 . ARG . 4073 1 90 . LEU . 4073 1 91 . GLY . 4073 1 92 . CYS . 4073 1 93 . GLN . 4073 1 94 . ILE . 4073 1 95 . CYS . 4073 1 96 . LEU . 4073 1 97 . THR . 4073 1 98 . LYS . 4073 1 99 . SER . 4073 1 100 . MET . 4073 1 101 . ASP . 4073 1 102 . ASN . 4073 1 103 . MET . 4073 1 104 . THR . 4073 1 105 . VAL . 4073 1 106 . ARG . 4073 1 107 . VAL . 4073 1 108 . PRO . 4073 1 109 . GLU . 4073 1 110 . THR . 4073 1 111 . VAL . 4073 1 112 . ALA . 4073 1 113 . ASP . 4073 1 114 . ALA . 4073 1 115 . ARG . 4073 1 116 . GLN . 4073 1 117 . SER . 4073 1 118 . ILE . 4073 1 119 . ASP . 4073 1 120 . VAL . 4073 1 121 . GLY . 4073 1 122 . LYS . 4073 1 123 . THR . 4073 1 124 . SER . 4073 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . SER 1 1 4073 1 . SER 2 2 4073 1 . SER 3 3 4073 1 . GLU 4 4 4073 1 . ASP 5 5 4073 1 . LYS 6 6 4073 1 . ILE 7 7 4073 1 . THR 8 8 4073 1 . VAL 9 9 4073 1 . HIS 10 10 4073 1 . PHE 11 11 4073 1 . ILE 12 12 4073 1 . ASN 13 13 4073 1 . ARG 14 14 4073 1 . ASP 15 15 4073 1 . GLY 16 16 4073 1 . GLU 17 17 4073 1 . THR 18 18 4073 1 . LEU 19 19 4073 1 . THR 20 20 4073 1 . THR 21 21 4073 1 . LYS 22 22 4073 1 . GLY 23 23 4073 1 . LYS 24 24 4073 1 . VAL 25 25 4073 1 . GLY 26 26 4073 1 . ASP 27 27 4073 1 . SER 28 28 4073 1 . LEU 29 29 4073 1 . LEU 30 30 4073 1 . ASP 31 31 4073 1 . VAL 32 32 4073 1 . VAL 33 33 4073 1 . VAL 34 34 4073 1 . GLU 35 35 4073 1 . ASN 36 36 4073 1 . ASN 37 37 4073 1 . LEU 38 38 4073 1 . ASP 39 39 4073 1 . ILE 40 40 4073 1 . ASP 41 41 4073 1 . GLY 42 42 4073 1 . PHE 43 43 4073 1 . GLY 44 44 4073 1 . ALA 45 45 4073 1 . CYS 46 46 4073 1 . GLU 47 47 4073 1 . GLY 48 48 4073 1 . THR 49 49 4073 1 . LEU 50 50 4073 1 . ALA 51 51 4073 1 . CYS 52 52 4073 1 . SER 53 53 4073 1 . THR 54 54 4073 1 . CYS 55 55 4073 1 . HIS 56 56 4073 1 . LEU 57 57 4073 1 . ILE 58 58 4073 1 . PHE 59 59 4073 1 . GLU 60 60 4073 1 . ASP 61 61 4073 1 . HIS 62 62 4073 1 . ILE 63 63 4073 1 . TYR 64 64 4073 1 . GLU 65 65 4073 1 . LYS 66 66 4073 1 . LEU 67 67 4073 1 . ASP 68 68 4073 1 . ALA 69 69 4073 1 . ILE 70 70 4073 1 . THR 71 71 4073 1 . ASP 72 72 4073 1 . GLU 73 73 4073 1 . GLU 74 74 4073 1 . ASN 75 75 4073 1 . ASP 76 76 4073 1 . MET 77 77 4073 1 . LEU 78 78 4073 1 . ASP 79 79 4073 1 . LEU 80 80 4073 1 . ALA 81 81 4073 1 . TYR 82 82 4073 1 . GLY 83 83 4073 1 . LEU 84 84 4073 1 . THR 85 85 4073 1 . ASP 86 86 4073 1 . ARG 87 87 4073 1 . SER 88 88 4073 1 . ARG 89 89 4073 1 . LEU 90 90 4073 1 . GLY 91 91 4073 1 . CYS 92 92 4073 1 . GLN 93 93 4073 1 . ILE 94 94 4073 1 . CYS 95 95 4073 1 . LEU 96 96 4073 1 . THR 97 97 4073 1 . LYS 98 98 4073 1 . SER 99 99 4073 1 . MET 100 100 4073 1 . ASP 101 101 4073 1 . ASN 102 102 4073 1 . MET 103 103 4073 1 . THR 104 104 4073 1 . VAL 105 105 4073 1 . ARG 106 106 4073 1 . VAL 107 107 4073 1 . PRO 108 108 4073 1 . GLU 109 109 4073 1 . THR 110 110 4073 1 . VAL 111 111 4073 1 . ALA 112 112 4073 1 . ASP 113 113 4073 1 . ALA 114 114 4073 1 . ARG 115 115 4073 1 . GLN 116 116 4073 1 . SER 117 117 4073 1 . ILE 118 118 4073 1 . ASP 119 119 4073 1 . VAL 120 120 4073 1 . GLY 121 121 4073 1 . LYS 122 122 4073 1 . THR 123 123 4073 1 . SER 124 124 4073 1 stop_ save_ save_FE _Entity.Sf_category entity _Entity.Sf_framecode FE _Entity.Entry_ID 4073 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name FE _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID FE _Entity.Nonpolymer_comp_label $chem_comp_FE _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . FE . 4073 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4073 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $HuFd-ox . 9609 organism . 'Homo sapiens' Human . . . . Homo sapiens . . . . . . . . . . . . . 4073 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4073 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $HuFd-ox . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 (DE3)pLysS . plasmid . . HuFd/pET9a . . . 4073 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_FE _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_FE _Chem_comp.Entry_ID 4073 _Chem_comp.ID FE _Chem_comp.Provenance PDB _Chem_comp.Name 'FE (III) ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code FE _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code FE _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 3 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Fe _Chem_comp.Formula_weight 55.845 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 11 10:30:25 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/Fe/q+3 InChI InChI 1.03 4073 FE VTLYFUHAOXGGBS-UHFFFAOYSA-N InChIKey InChI 1.03 4073 FE [Fe+3] SMILES ACDLabs 10.04 4073 FE [Fe+3] SMILES CACTVS 3.341 4073 FE [Fe+3] SMILES 'OpenEye OEToolkits' 1.5.0 4073 FE [Fe+3] SMILES_CANONICAL CACTVS 3.341 4073 FE [Fe+3] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4073 FE stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID 'iron(+3) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4073 FE iron(3+) 'SYSTEMATIC NAME' ACDLabs 10.04 4073 FE stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID FE . FE . . FE . . N 3 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 4073 FE stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4073 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'human ferredoxin' '[U-99.8% 15N]' . . 1 $HuFd-ox . . . 1 2 mM . . . . 4073 1 2 Tris-HCl . . . . . . . 50 . . mM . . . . 4073 1 stop_ save_ save_sample_two _Sample.Sf_category sample _Sample.Sf_framecode sample_two _Sample.Entry_ID 4073 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'human ferredoxin' '[U-99% 13C; U-99.8% 15N]' . . 1 $HuFd-ox . . . 1 2 mM . . . . 4073 2 2 Tris-HCl . . . . . . . 50 . . mM . . . . 4073 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_HuFd-ox _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_HuFd-ox _Sample_condition_list.Entry_ID 4073 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.4 0.1 pH 4073 1 temperature 295 1 K 4073 1 stop_ save_ ############################ # Computer software used # ############################ save_software_Felix _Software.Sf_category software _Software.Sf_framecode software_Felix _Software.Entry_ID 4073 _Software.ID 1 _Software.Name FELIX _Software.Version '2.30 & 95.0' _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Molecular Simulations, San Diego, CA' . . 4073 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'used for all FT of data' 4073 1 stop_ save_ save_software_Peakpick _Software.Sf_category software _Software.Sf_framecode software_Peakpick _Software.Entry_ID 4073 _Software.ID 2 _Software.Name Peakpick _Software.Version 1.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Molecular Simulations, San Diego, CA' . . 4073 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'used for peakpicking all data' 4073 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $citation_three 4073 2 stop_ save_ save_software_PPFLX _Software.Sf_category software _Software.Sf_framecode software_PPFLX _Software.Entry_ID 4073 _Software.ID 3 _Software.Name PPFLX _Software.Version 1.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Molecular Simulations, San Diego, CA' . . 4073 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'used for peakpicking all data' 4073 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_one _NMR_spectrometer.Entry_ID 4073 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX500 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_two _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_two _NMR_spectrometer.Entry_ID 4073 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX600 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_three _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_three _NMR_spectrometer.Entry_ID 4073 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX750 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4073 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_one Bruker DMX500 . 500 . . . 4073 1 2 spectrometer_two Bruker DMX600 . 600 . . . 4073 1 3 spectrometer_three Bruker DMX750 . 750 . . . 4073 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4073 _Experiment_list.ID 1 _Experiment_list.Details ; SUMMARY TABLE: Spectral Parameters for the NMR Data Sets Collected on Human Ferredoxin d1 (1H)b d2 d3 Matrix Size Experiment SF(/MHz) SW (/Hz) Nucleus SW (/Hz) N2c Nucleus SW(/Hz) N3c (d1 x d2 x d3) 2D 1H-15N HSQC 500.13 6009.615 15N 1666.67 256 512 x 25 3D HNCO 500.13 6009.615 13C' 2000.00 64 15N 1666.67 36 512 x 256 x 128 3D HNCA 500.13 6009.615 13Ca 4545.45 60 15N 1666.67 32 512 x 256 x 128 3D HN(CO)CA 500.13 6009.615 13Ca 4545.45 64 15N 1666.67 28 512 x 256 x 128 3D HNCACB 500.13 6009.615 13Ca/b 7352.94 64 15N 1666.67 32 512 x 256 x 128 3D CBCA(CO)NH 500.13 6009.615 13Ca/b 7352.94 42 15N 1666.67 32 512 x 256 x 128 3D HCACO 500.13 6009.615 13C' 2000.00 64 13Ca 4545.45 32 512 x 256 x 128 3D 15N-TOCSYd 750.13 8992.806 1H 8992.806 128 15N 2500 32 512 x 512 x 128 3D 15N-NOESYd 750.13 8992.806 1H 8992.806 128 15N 2500 32 512 x 512 x 128 3D 15N-TOCSYe 600.13 6944.444 1H 6944.444 150 15N 1818.18 40 512 x 512 x 128 3D 15N-NOESY 600.13 6944.444 1H 6944.444 150 15N 1818.18 40 512 x 512 x 128 *Summary Table was provided by the author. a-The parameters listed here apply to NMR data sets for both oxidized and reduced human ferredoxin, except that 3D 15N-TOCSY and 3D 15N-NOESY. b-A total of 1024 complex points were collected in the 1H dimension (d1) of all experiments. In all experiments except HCACO, the right half of the spectrum (upfield of H2O) in d1 dimension contained no signals and was discarded. c-N2 and N3 are the numbers of complex points collected for d2 and d3 dimensions, respectively. d-NMR experimental data collected for oxidized HuFd. e-NMR experimental data collected for reduced HuFd. ; loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 2D_1H-15N_HSQC . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 2 3D_HNCO . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 3 3D_HNCA . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 4 3D_HN(CO)CA . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 5 3D_HNCACB . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 6 3D_CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 7 3D_HCACO . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 8 3D_15N-TOCSYd . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 9 3D_15N-NOESYd . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 10 3D_15N-TOCSYe . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 11 3D_15N-NOESY . . . . . . . . . . . . . . . . 1 $sample_conditions_HuFd-ox . . . . . . . . . . . . . . . . . . . . . 4073 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference _Chem_shift_reference.Entry_ID 4073 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 external indirect . . . . . . 4073 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct . . . . . . 4073 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 external indirect . . . . . . 4073 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignment _Assigned_chem_shift_list.Entry_ID 4073 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_HuFd-ox _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 2D_1H-15N_HSQC 1 $sample_one . 4073 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 SER CA C 13 58.51 . . 1 . . . . . . . . 4073 1 2 . 1 1 2 2 SER CB C 13 64.15 . . 1 . . . . . . . . 4073 1 3 . 1 1 3 3 SER H H 1 8.63 . . 1 . . . . . . . . 4073 1 4 . 1 1 3 3 SER HA H 1 4.44 . . 1 . . . . . . . . 4073 1 5 . 1 1 3 3 SER C C 13 174.84 . . 1 . . . . . . . . 4073 1 6 . 1 1 3 3 SER CA C 13 59.01 . . 1 . . . . . . . . 4073 1 7 . 1 1 3 3 SER CB C 13 63.74 . . 1 . . . . . . . . 4073 1 8 . 1 1 3 3 SER N N 15 118.62 . . 1 . . . . . . . . 4073 1 9 . 1 1 4 4 GLU H H 1 8.44 . . 1 . . . . . . . . 4073 1 10 . 1 1 4 4 GLU HA H 1 4.31 . . 1 . . . . . . . . 4073 1 11 . 1 1 4 4 GLU C C 13 176.15 . . 1 . . . . . . . . 4073 1 12 . 1 1 4 4 GLU CA C 13 56.71 . . 1 . . . . . . . . 4073 1 13 . 1 1 4 4 GLU CB C 13 30.33 . . 1 . . . . . . . . 4073 1 14 . 1 1 4 4 GLU N N 15 122.58 . . 1 . . . . . . . . 4073 1 15 . 1 1 5 5 ASP H H 1 8.32 . . 1 . . . . . . . . 4073 1 16 . 1 1 5 5 ASP HA H 1 4.61 . . 1 . . . . . . . . 4073 1 17 . 1 1 5 5 ASP C C 13 175.68 . . 1 . . . . . . . . 4073 1 18 . 1 1 5 5 ASP CA C 13 54.59 . . 1 . . . . . . . . 4073 1 19 . 1 1 5 5 ASP CB C 13 41.13 . . 1 . . . . . . . . 4073 1 20 . 1 1 5 5 ASP N N 15 121.84 . . 1 . . . . . . . . 4073 1 21 . 1 1 6 6 LYS H H 1 8.11 . . 1 . . . . . . . . 4073 1 22 . 1 1 6 6 LYS HA H 1 4.88 . . 1 . . . . . . . . 4073 1 23 . 1 1 6 6 LYS C C 13 176.27 . . 1 . . . . . . . . 4073 1 24 . 1 1 6 6 LYS CA C 13 55.49 . . 1 . . . . . . . . 4073 1 25 . 1 1 6 6 LYS CB C 13 35.55 . . 1 . . . . . . . . 4073 1 26 . 1 1 6 6 LYS N N 15 120.62 . . 1 . . . . . . . . 4073 1 27 . 1 1 7 7 ILE H H 1 9.03 . . 1 . . . . . . . . 4073 1 28 . 1 1 7 7 ILE HA H 1 4.47 . . 1 . . . . . . . . 4073 1 29 . 1 1 7 7 ILE C C 13 175.02 . . 1 . . . . . . . . 4073 1 30 . 1 1 7 7 ILE CA C 13 59.02 . . 1 . . . . . . . . 4073 1 31 . 1 1 7 7 ILE CB C 13 40.92 . . 1 . . . . . . . . 4073 1 32 . 1 1 7 7 ILE N N 15 119.32 . . 1 . . . . . . . . 4073 1 33 . 1 1 8 8 THR H H 1 8.90 . . 1 . . . . . . . . 4073 1 34 . 1 1 8 8 THR HA H 1 4.73 . . 1 . . . . . . . . 4073 1 35 . 1 1 8 8 THR C C 13 174.18 . . 1 . . . . . . . . 4073 1 36 . 1 1 8 8 THR CA C 13 63.49 . . 1 . . . . . . . . 4073 1 37 . 1 1 8 8 THR CB C 13 69.17 . . 1 . . . . . . . . 4073 1 38 . 1 1 8 8 THR N N 15 122.61 . . 1 . . . . . . . . 4073 1 39 . 1 1 9 9 VAL H H 1 8.56 . . 1 . . . . . . . . 4073 1 40 . 1 1 9 9 VAL HA H 1 4.21 . . 1 . . . . . . . . 4073 1 41 . 1 1 9 9 VAL C C 13 173.52 . . 1 . . . . . . . . 4073 1 42 . 1 1 9 9 VAL CA C 13 61.15 . . 1 . . . . . . . . 4073 1 43 . 1 1 9 9 VAL CB C 13 35.72 . . 1 . . . . . . . . 4073 1 44 . 1 1 9 9 VAL N N 15 125.50 . . 1 . . . . . . . . 4073 1 45 . 1 1 10 10 HIS H H 1 8.65 . . 1 . . . . . . . . 4073 1 46 . 1 1 10 10 HIS HA H 1 5.41 . . 1 . . . . . . . . 4073 1 47 . 1 1 10 10 HIS C C 13 174.61 . . 1 . . . . . . . . 4073 1 48 . 1 1 10 10 HIS CA C 13 54.22 . . 1 . . . . . . . . 4073 1 49 . 1 1 10 10 HIS CB C 13 31.18 . . 1 . . . . . . . . 4073 1 50 . 1 1 10 10 HIS N N 15 126.08 . . 1 . . . . . . . . 4073 1 51 . 1 1 11 11 PHE H H 1 9.65 . . 1 . . . . . . . . 4073 1 52 . 1 1 11 11 PHE HA H 1 5.18 . . 1 . . . . . . . . 4073 1 53 . 1 1 11 11 PHE C C 13 175.63 . . 1 . . . . . . . . 4073 1 54 . 1 1 11 11 PHE CA C 13 55.68 . . 1 . . . . . . . . 4073 1 55 . 1 1 11 11 PHE CB C 13 41.89 . . 1 . . . . . . . . 4073 1 56 . 1 1 11 11 PHE N N 15 123.24 . . 1 . . . . . . . . 4073 1 57 . 1 1 12 12 ILE H H 1 9.11 . . 1 . . . . . . . . 4073 1 58 . 1 1 12 12 ILE HA H 1 4.72 . . 1 . . . . . . . . 4073 1 59 . 1 1 12 12 ILE C C 13 176.24 . . 1 . . . . . . . . 4073 1 60 . 1 1 12 12 ILE CA C 13 60.47 . . 1 . . . . . . . . 4073 1 61 . 1 1 12 12 ILE CB C 13 37.14 . . 1 . . . . . . . . 4073 1 62 . 1 1 12 12 ILE N N 15 123.60 . . 1 . . . . . . . . 4073 1 63 . 1 1 13 13 ASN H H 1 8.98 . . 1 . . . . . . . . 4073 1 64 . 1 1 13 13 ASN HA H 1 4.68 . . 1 . . . . . . . . 4073 1 65 . 1 1 13 13 ASN C C 13 177.29 . . 1 . . . . . . . . 4073 1 66 . 1 1 13 13 ASN CA C 13 51.27 . . 1 . . . . . . . . 4073 1 67 . 1 1 13 13 ASN CB C 13 38.93 . . 1 . . . . . . . . 4073 1 68 . 1 1 13 13 ASN N N 15 125.92 . . 1 . . . . . . . . 4073 1 69 . 1 1 14 14 ARG H H 1 8.67 . . 1 . . . . . . . . 4073 1 70 . 1 1 14 14 ARG HA H 1 4.05 . . 1 . . . . . . . . 4073 1 71 . 1 1 14 14 ARG C C 13 176.30 . . 1 . . . . . . . . 4073 1 72 . 1 1 14 14 ARG CA C 13 59.33 . . 1 . . . . . . . . 4073 1 73 . 1 1 14 14 ARG CB C 13 29.56 . . 1 . . . . . . . . 4073 1 74 . 1 1 14 14 ARG N N 15 119.96 . . 1 . . . . . . . . 4073 1 75 . 1 1 15 15 ASP H H 1 7.72 . . 1 . . . . . . . . 4073 1 76 . 1 1 15 15 ASP HA H 1 4.61 . . 1 . . . . . . . . 4073 1 77 . 1 1 15 15 ASP C C 13 177.02 . . 1 . . . . . . . . 4073 1 78 . 1 1 15 15 ASP CA C 13 53.57 . . 1 . . . . . . . . 4073 1 79 . 1 1 15 15 ASP CB C 13 40.70 . . 1 . . . . . . . . 4073 1 80 . 1 1 15 15 ASP N N 15 116.90 . . 1 . . . . . . . . 4073 1 81 . 1 1 16 16 GLY H H 1 8.22 . . 1 . . . . . . . . 4073 1 82 . 1 1 16 16 GLY HA2 H 1 4.24 . . 2 . . . . . . . . 4073 1 83 . 1 1 16 16 GLY HA3 H 1 3.52 . . 2 . . . . . . . . 4073 1 84 . 1 1 16 16 GLY C C 13 174.39 . . 1 . . . . . . . . 4073 1 85 . 1 1 16 16 GLY CA C 13 45.30 . . 1 . . . . . . . . 4073 1 86 . 1 1 16 16 GLY N N 15 109.11 . . 1 . . . . . . . . 4073 1 87 . 1 1 17 17 GLU H H 1 8.02 . . 1 . . . . . . . . 4073 1 88 . 1 1 17 17 GLU HA H 1 4.29 . . 1 . . . . . . . . 4073 1 89 . 1 1 17 17 GLU C C 13 175.62 . . 1 . . . . . . . . 4073 1 90 . 1 1 17 17 GLU CA C 13 56.03 . . 1 . . . . . . . . 4073 1 91 . 1 1 17 17 GLU CB C 13 30.41 . . 1 . . . . . . . . 4073 1 92 . 1 1 17 17 GLU N N 15 123.16 . . 1 . . . . . . . . 4073 1 93 . 1 1 18 18 THR H H 1 8.80 . . 1 . . . . . . . . 4073 1 94 . 1 1 18 18 THR HA H 1 4.90 . . 1 . . . . . . . . 4073 1 95 . 1 1 18 18 THR C C 13 177.02 . . 1 . . . . . . . . 4073 1 96 . 1 1 18 18 THR CA C 13 63.17 . . 1 . . . . . . . . 4073 1 97 . 1 1 18 18 THR CB C 13 69.27 . . 1 . . . . . . . . 4073 1 98 . 1 1 18 18 THR N N 15 120.01 . . 1 . . . . . . . . 4073 1 99 . 1 1 19 19 LEU H H 1 10.12 . . 1 . . . . . . . . 4073 1 100 . 1 1 19 19 LEU HA H 1 4.81 . . 1 . . . . . . . . 4073 1 101 . 1 1 19 19 LEU C C 13 175.69 . . 1 . . . . . . . . 4073 1 102 . 1 1 19 19 LEU CA C 13 53.40 . . 1 . . . . . . . . 4073 1 103 . 1 1 19 19 LEU CB C 13 42.79 . . 1 . . . . . . . . 4073 1 104 . 1 1 19 19 LEU N N 15 132.44 . . 1 . . . . . . . . 4073 1 105 . 1 1 20 20 THR H H 1 8.96 . . 1 . . . . . . . . 4073 1 106 . 1 1 20 20 THR HA H 1 4.97 . . 1 . . . . . . . . 4073 1 107 . 1 1 20 20 THR C C 13 174.23 . . 1 . . . . . . . . 4073 1 108 . 1 1 20 20 THR CA C 13 63.97 . . 1 . . . . . . . . 4073 1 109 . 1 1 20 20 THR CB C 13 70.16 . . 1 . . . . . . . . 4073 1 110 . 1 1 20 20 THR N N 15 123.88 . . 1 . . . . . . . . 4073 1 111 . 1 1 21 21 THR H H 1 8.87 . . 1 . . . . . . . . 4073 1 112 . 1 1 21 21 THR HA H 1 4.71 . . 1 . . . . . . . . 4073 1 113 . 1 1 21 21 THR C C 13 171.96 . . 1 . . . . . . . . 4073 1 114 . 1 1 21 21 THR CA C 13 60.27 . . 1 . . . . . . . . 4073 1 115 . 1 1 21 21 THR CB C 13 70.50 . . 1 . . . . . . . . 4073 1 116 . 1 1 21 21 THR N N 15 123.66 . . 1 . . . . . . . . 4073 1 117 . 1 1 22 22 LYS H H 1 8.05 . . 1 . . . . . . . . 4073 1 118 . 1 1 22 22 LYS HA H 1 5.62 . . 1 . . . . . . . . 4073 1 119 . 1 1 22 22 LYS C C 13 176.57 . . 1 . . . . . . . . 4073 1 120 . 1 1 22 22 LYS CA C 13 53.95 . . 1 . . . . . . . . 4073 1 121 . 1 1 22 22 LYS CB C 13 36.10 . . 1 . . . . . . . . 4073 1 122 . 1 1 22 22 LYS N N 15 118.92 . . 1 . . . . . . . . 4073 1 123 . 1 1 23 23 GLY H H 1 8.93 . . 1 . . . . . . . . 4073 1 124 . 1 1 23 23 GLY HA2 H 1 4.73 . . 2 . . . . . . . . 4073 1 125 . 1 1 23 23 GLY HA3 H 1 3.32 . . 2 . . . . . . . . 4073 1 126 . 1 1 23 23 GLY C C 13 171.11 . . 1 . . . . . . . . 4073 1 127 . 1 1 23 23 GLY CA C 13 43.99 . . 1 . . . . . . . . 4073 1 128 . 1 1 23 23 GLY N N 15 108.10 . . 1 . . . . . . . . 4073 1 129 . 1 1 24 24 LYS H H 1 8.85 . . 1 . . . . . . . . 4073 1 130 . 1 1 24 24 LYS HA H 1 4.71 . . 1 . . . . . . . . 4073 1 131 . 1 1 24 24 LYS C C 13 176.48 . . 1 . . . . . . . . 4073 1 132 . 1 1 24 24 LYS CA C 13 55.08 . . 1 . . . . . . . . 4073 1 133 . 1 1 24 24 LYS CB C 13 33.47 . . 1 . . . . . . . . 4073 1 134 . 1 1 24 24 LYS N N 15 122.11 . . 1 . . . . . . . . 4073 1 135 . 1 1 25 25 VAL H H 1 8.50 . . 1 . . . . . . . . 4073 1 136 . 1 1 25 25 VAL HA H 1 3.22 . . 1 . . . . . . . . 4073 1 137 . 1 1 25 25 VAL C C 13 177.60 . . 1 . . . . . . . . 4073 1 138 . 1 1 25 25 VAL CA C 13 65.81 . . 1 . . . . . . . . 4073 1 139 . 1 1 25 25 VAL CB C 13 31.67 . . 1 . . . . . . . . 4073 1 140 . 1 1 25 25 VAL N N 15 123.28 . . 1 . . . . . . . . 4073 1 141 . 1 1 26 26 GLY H H 1 8.91 . . 1 . . . . . . . . 4073 1 142 . 1 1 26 26 GLY HA2 H 1 4.56 . . 2 . . . . . . . . 4073 1 143 . 1 1 26 26 GLY HA3 H 1 3.58 . . 2 . . . . . . . . 4073 1 144 . 1 1 26 26 GLY C C 13 174.54 . . 1 . . . . . . . . 4073 1 145 . 1 1 26 26 GLY CA C 13 45.26 . . 1 . . . . . . . . 4073 1 146 . 1 1 26 26 GLY N N 15 117.60 . . 1 . . . . . . . . 4073 1 147 . 1 1 27 27 ASP H H 1 8.24 . . 1 . . . . . . . . 4073 1 148 . 1 1 27 27 ASP HA H 1 4.74 . . 1 . . . . . . . . 4073 1 149 . 1 1 27 27 ASP C C 13 176.56 . . 1 . . . . . . . . 4073 1 150 . 1 1 27 27 ASP CA C 13 54.77 . . 1 . . . . . . . . 4073 1 151 . 1 1 27 27 ASP CB C 13 41.48 . . 1 . . . . . . . . 4073 1 152 . 1 1 27 27 ASP N N 15 123.94 . . 1 . . . . . . . . 4073 1 153 . 1 1 28 28 SER H H 1 9.80 . . 1 . . . . . . . . 4073 1 154 . 1 1 28 28 SER HA H 1 4.36 . . 1 . . . . . . . . 4073 1 155 . 1 1 28 28 SER CA C 13 57.18 . . 1 . . . . . . . . 4073 1 156 . 1 1 28 28 SER CB C 13 66.03 . . 1 . . . . . . . . 4073 1 157 . 1 1 28 28 SER N N 15 119.15 . . 1 . . . . . . . . 4073 1 158 . 1 1 29 29 LEU H H 1 8.31 . . 1 . . . . . . . . 4073 1 159 . 1 1 29 29 LEU HA H 1 4.58 . . 1 . . . . . . . . 4073 1 160 . 1 1 29 29 LEU CA C 13 58.04 . . 1 . . . . . . . . 4073 1 161 . 1 1 29 29 LEU CB C 13 41.04 . . 1 . . . . . . . . 4073 1 162 . 1 1 29 29 LEU N N 15 119.60 . . 1 . . . . . . . . 4073 1 163 . 1 1 30 30 LEU C C 13 175.32 . . 1 . . . . . . . . 4073 1 164 . 1 1 30 30 LEU CA C 13 55.71 . . 1 . . . . . . . . 4073 1 165 . 1 1 31 31 ASP H H 1 7.74 . . 1 . . . . . . . . 4073 1 166 . 1 1 31 31 ASP HA H 1 4.38 . . 1 . . . . . . . . 4073 1 167 . 1 1 31 31 ASP C C 13 177.78 . . 1 . . . . . . . . 4073 1 168 . 1 1 31 31 ASP CA C 13 58.05 . . 1 . . . . . . . . 4073 1 169 . 1 1 31 31 ASP N N 15 121.84 . . 1 . . . . . . . . 4073 1 170 . 1 1 32 32 VAL H H 1 7.82 . . 1 . . . . . . . . 4073 1 171 . 1 1 32 32 VAL HA H 1 3.85 . . 1 . . . . . . . . 4073 1 172 . 1 1 32 32 VAL C C 13 178.88 . . 1 . . . . . . . . 4073 1 173 . 1 1 32 32 VAL CA C 13 66.27 . . 1 . . . . . . . . 4073 1 174 . 1 1 32 32 VAL CB C 13 32.19 . . 1 . . . . . . . . 4073 1 175 . 1 1 32 32 VAL N N 15 117.97 . . 1 . . . . . . . . 4073 1 176 . 1 1 33 33 VAL H H 1 7.52 . . 1 . . . . . . . . 4073 1 177 . 1 1 33 33 VAL HA H 1 3.06 . . 1 . . . . . . . . 4073 1 178 . 1 1 33 33 VAL C C 13 178.01 . . 1 . . . . . . . . 4073 1 179 . 1 1 33 33 VAL CA C 13 67.33 . . 1 . . . . . . . . 4073 1 180 . 1 1 33 33 VAL CB C 13 32.31 . . 1 . . . . . . . . 4073 1 181 . 1 1 33 33 VAL N N 15 122.43 . . 1 . . . . . . . . 4073 1 182 . 1 1 34 34 VAL H H 1 8.48 . . 1 . . . . . . . . 4073 1 183 . 1 1 34 34 VAL HA H 1 3.76 . . 1 . . . . . . . . 4073 1 184 . 1 1 34 34 VAL C C 13 181.07 . . 1 . . . . . . . . 4073 1 185 . 1 1 34 34 VAL CA C 13 66.36 . . 1 . . . . . . . . 4073 1 186 . 1 1 34 34 VAL CB C 13 32.57 . . 1 . . . . . . . . 4073 1 187 . 1 1 34 34 VAL N N 15 119.47 . . 1 . . . . . . . . 4073 1 188 . 1 1 35 35 GLU H H 1 9.22 . . 1 . . . . . . . . 4073 1 189 . 1 1 35 35 GLU HA H 1 4.03 . . 1 . . . . . . . . 4073 1 190 . 1 1 35 35 GLU C C 13 177.91 . . 1 . . . . . . . . 4073 1 191 . 1 1 35 35 GLU CA C 13 59.35 . . 1 . . . . . . . . 4073 1 192 . 1 1 35 35 GLU CB C 13 29.41 . . 1 . . . . . . . . 4073 1 193 . 1 1 35 35 GLU N N 15 121.19 . . 1 . . . . . . . . 4073 1 194 . 1 1 36 36 ASN H H 1 7.21 . . 1 . . . . . . . . 4073 1 195 . 1 1 36 36 ASN HA H 1 4.73 . . 1 . . . . . . . . 4073 1 196 . 1 1 36 36 ASN C C 13 173.10 . . 1 . . . . . . . . 4073 1 197 . 1 1 36 36 ASN CA C 13 53.51 . . 1 . . . . . . . . 4073 1 198 . 1 1 36 36 ASN CB C 13 39.68 . . 1 . . . . . . . . 4073 1 199 . 1 1 36 36 ASN N N 15 112.04 . . 1 . . . . . . . . 4073 1 200 . 1 1 37 37 ASN H H 1 7.90 . . 1 . . . . . . . . 4073 1 201 . 1 1 37 37 ASN HA H 1 4.40 . . 1 . . . . . . . . 4073 1 202 . 1 1 37 37 ASN C C 13 174.88 . . 1 . . . . . . . . 4073 1 203 . 1 1 37 37 ASN CA C 13 54.08 . . 1 . . . . . . . . 4073 1 204 . 1 1 37 37 ASN CB C 13 37.43 . . 1 . . . . . . . . 4073 1 205 . 1 1 37 37 ASN N N 15 118.37 . . 1 . . . . . . . . 4073 1 206 . 1 1 38 38 LEU H H 1 7.84 . . 1 . . . . . . . . 4073 1 207 . 1 1 38 38 LEU HA H 1 4.02 . . 1 . . . . . . . . 4073 1 208 . 1 1 38 38 LEU C C 13 178.19 . . 1 . . . . . . . . 4073 1 209 . 1 1 38 38 LEU CA C 13 55.57 . . 1 . . . . . . . . 4073 1 210 . 1 1 38 38 LEU CB C 13 42.11 . . 1 . . . . . . . . 4073 1 211 . 1 1 38 38 LEU N N 15 115.97 . . 1 . . . . . . . . 4073 1 212 . 1 1 39 39 ASP H H 1 8.68 . . 1 . . . . . . . . 4073 1 213 . 1 1 39 39 ASP HA H 1 4.55 . . 1 . . . . . . . . 4073 1 214 . 1 1 39 39 ASP C C 13 174.70 . . 1 . . . . . . . . 4073 1 215 . 1 1 39 39 ASP CA C 13 53.53 . . 1 . . . . . . . . 4073 1 216 . 1 1 39 39 ASP CB C 13 39.41 . . 1 . . . . . . . . 4073 1 217 . 1 1 39 39 ASP N N 15 123.55 . . 1 . . . . . . . . 4073 1 218 . 1 1 40 40 ILE H H 1 7.67 . . 1 . . . . . . . . 4073 1 219 . 1 1 40 40 ILE HA H 1 4.20 . . 1 . . . . . . . . 4073 1 220 . 1 1 40 40 ILE C C 13 175.98 . . 1 . . . . . . . . 4073 1 221 . 1 1 40 40 ILE CA C 13 60.09 . . 1 . . . . . . . . 4073 1 222 . 1 1 40 40 ILE CB C 13 38.70 . . 1 . . . . . . . . 4073 1 223 . 1 1 40 40 ILE N N 15 124.76 . . 1 . . . . . . . . 4073 1 224 . 1 1 41 41 ASP H H 1 8.63 . . 1 . . . . . . . . 4073 1 225 . 1 1 41 41 ASP HA H 1 4.37 . . 1 . . . . . . . . 4073 1 226 . 1 1 41 41 ASP C C 13 178.43 . . 1 . . . . . . . . 4073 1 227 . 1 1 41 41 ASP CA C 13 56.93 . . 1 . . . . . . . . 4073 1 228 . 1 1 41 41 ASP CB C 13 41.64 . . 1 . . . . . . . . 4073 1 229 . 1 1 41 41 ASP N N 15 128.35 . . 1 . . . . . . . . 4073 1 230 . 1 1 42 42 GLY H H 1 9.15 . . 1 . . . . . . . . 4073 1 231 . 1 1 42 42 GLY HA2 H 1 4.11 . . 2 . . . . . . . . 4073 1 232 . 1 1 42 42 GLY HA3 H 1 3.80 . . 2 . . . . . . . . 4073 1 233 . 1 1 42 42 GLY C C 13 174.08 . . 1 . . . . . . . . 4073 1 234 . 1 1 42 42 GLY CA C 13 46.24 . . 1 . . . . . . . . 4073 1 235 . 1 1 42 42 GLY N N 15 114.75 . . 1 . . . . . . . . 4073 1 236 . 1 1 43 43 PHE H H 1 7.71 . . 1 . . . . . . . . 4073 1 237 . 1 1 43 43 PHE HA H 1 4.60 . . 1 . . . . . . . . 4073 1 238 . 1 1 43 43 PHE CA C 13 59.42 . . 1 . . . . . . . . 4073 1 239 . 1 1 43 43 PHE CB C 13 41.05 . . 1 . . . . . . . . 4073 1 240 . 1 1 43 43 PHE N N 15 121.68 . . 1 . . . . . . . . 4073 1 241 . 1 1 59 59 PHE H H 1 8.79 . . 1 . . . . . . . . 4073 1 242 . 1 1 59 59 PHE HA H 1 4.56 . . 1 . . . . . . . . 4073 1 243 . 1 1 59 59 PHE C C 13 175.60 . . 1 . . . . . . . . 4073 1 244 . 1 1 59 59 PHE CA C 13 58.59 . . 1 . . . . . . . . 4073 1 245 . 1 1 59 59 PHE CB C 13 43.53 . . 1 . . . . . . . . 4073 1 246 . 1 1 59 59 PHE N N 15 128.40 . . 1 . . . . . . . . 4073 1 247 . 1 1 60 60 GLU H H 1 9.11 . . 1 . . . . . . . . 4073 1 248 . 1 1 60 60 GLU HA H 1 4.36 . . 1 . . . . . . . . 4073 1 249 . 1 1 60 60 GLU C C 13 178.88 . . 1 . . . . . . . . 4073 1 250 . 1 1 60 60 GLU CA C 13 56.93 . . 1 . . . . . . . . 4073 1 251 . 1 1 60 60 GLU CB C 13 32.33 . . 1 . . . . . . . . 4073 1 252 . 1 1 60 60 GLU N N 15 119.55 . . 1 . . . . . . . . 4073 1 253 . 1 1 61 61 ASP H H 1 9.41 . . 1 . . . . . . . . 4073 1 254 . 1 1 61 61 ASP HA H 1 4.13 . . 1 . . . . . . . . 4073 1 255 . 1 1 61 61 ASP C C 13 177.64 . . 1 . . . . . . . . 4073 1 256 . 1 1 61 61 ASP CA C 13 59.14 . . 1 . . . . . . . . 4073 1 257 . 1 1 61 61 ASP CB C 13 41.10 . . 1 . . . . . . . . 4073 1 258 . 1 1 61 61 ASP N N 15 124.59 . . 1 . . . . . . . . 4073 1 259 . 1 1 62 62 HIS H H 1 8.55 . . 1 . . . . . . . . 4073 1 260 . 1 1 62 62 HIS HA H 1 4.52 . . 1 . . . . . . . . 4073 1 261 . 1 1 62 62 HIS C C 13 176.96 . . 1 . . . . . . . . 4073 1 262 . 1 1 62 62 HIS CA C 13 58.75 . . 1 . . . . . . . . 4073 1 263 . 1 1 62 62 HIS CB C 13 29.58 . . 1 . . . . . . . . 4073 1 264 . 1 1 62 62 HIS N N 15 114.63 . . 1 . . . . . . . . 4073 1 265 . 1 1 63 63 ILE H H 1 6.33 . . 1 . . . . . . . . 4073 1 266 . 1 1 63 63 ILE HA H 1 3.89 . . 1 . . . . . . . . 4073 1 267 . 1 1 63 63 ILE C C 13 178.13 . . 1 . . . . . . . . 4073 1 268 . 1 1 63 63 ILE CA C 13 59.92 . . 1 . . . . . . . . 4073 1 269 . 1 1 63 63 ILE CB C 13 36.53 . . 1 . . . . . . . . 4073 1 270 . 1 1 63 63 ILE N N 15 120.80 . . 1 . . . . . . . . 4073 1 271 . 1 1 64 64 TYR H H 1 8.72 . . 1 . . . . . . . . 4073 1 272 . 1 1 64 64 TYR HA H 1 3.58 . . 1 . . . . . . . . 4073 1 273 . 1 1 64 64 TYR C C 13 177.70 . . 1 . . . . . . . . 4073 1 274 . 1 1 64 64 TYR CA C 13 61.76 . . 1 . . . . . . . . 4073 1 275 . 1 1 64 64 TYR CB C 13 39.66 . . 1 . . . . . . . . 4073 1 276 . 1 1 64 64 TYR N N 15 120.57 . . 1 . . . . . . . . 4073 1 277 . 1 1 65 65 GLU H H 1 7.88 . . 1 . . . . . . . . 4073 1 278 . 1 1 65 65 GLU HA H 1 4.14 . . 1 . . . . . . . . 4073 1 279 . 1 1 65 65 GLU C C 13 176.53 . . 1 . . . . . . . . 4073 1 280 . 1 1 65 65 GLU CA C 13 58.18 . . 1 . . . . . . . . 4073 1 281 . 1 1 65 65 GLU CB C 13 30.02 . . 1 . . . . . . . . 4073 1 282 . 1 1 65 65 GLU N N 15 113.85 . . 1 . . . . . . . . 4073 1 283 . 1 1 66 66 LYS H H 1 7.22 . . 1 . . . . . . . . 4073 1 284 . 1 1 66 66 LYS HA H 1 4.48 . . 1 . . . . . . . . 4073 1 285 . 1 1 66 66 LYS C C 13 176.84 . . 1 . . . . . . . . 4073 1 286 . 1 1 66 66 LYS CA C 13 54.80 . . 1 . . . . . . . . 4073 1 287 . 1 1 66 66 LYS CB C 13 33.34 . . 1 . . . . . . . . 4073 1 288 . 1 1 66 66 LYS N N 15 116.52 . . 1 . . . . . . . . 4073 1 289 . 1 1 67 67 LEU H H 1 6.85 . . 1 . . . . . . . . 4073 1 290 . 1 1 67 67 LEU HA H 1 4.06 . . 1 . . . . . . . . 4073 1 291 . 1 1 67 67 LEU C C 13 177.19 . . 1 . . . . . . . . 4073 1 292 . 1 1 67 67 LEU CA C 13 54.69 . . 1 . . . . . . . . 4073 1 293 . 1 1 67 67 LEU CB C 13 41.50 . . 1 . . . . . . . . 4073 1 294 . 1 1 67 67 LEU N N 15 120.64 . . 1 . . . . . . . . 4073 1 295 . 1 1 68 68 ASP H H 1 9.18 . . 1 . . . . . . . . 4073 1 296 . 1 1 68 68 ASP HA H 1 4.32 . . 1 . . . . . . . . 4073 1 297 . 1 1 68 68 ASP C C 13 175.60 . . 1 . . . . . . . . 4073 1 298 . 1 1 68 68 ASP CA C 13 54.72 . . 1 . . . . . . . . 4073 1 299 . 1 1 68 68 ASP CB C 13 40.96 . . 1 . . . . . . . . 4073 1 300 . 1 1 68 68 ASP N N 15 123.38 . . 1 . . . . . . . . 4073 1 301 . 1 1 69 69 ALA H H 1 8.30 . . 1 . . . . . . . . 4073 1 302 . 1 1 69 69 ALA HA H 1 4.00 . . 1 . . . . . . . . 4073 1 303 . 1 1 69 69 ALA C C 13 178.45 . . 1 . . . . . . . . 4073 1 304 . 1 1 69 69 ALA CA C 13 52.68 . . 1 . . . . . . . . 4073 1 305 . 1 1 69 69 ALA CB C 13 18.81 . . 1 . . . . . . . . 4073 1 306 . 1 1 69 69 ALA N N 15 123.03 . . 1 . . . . . . . . 4073 1 307 . 1 1 70 70 ILE H H 1 8.52 . . 1 . . . . . . . . 4073 1 308 . 1 1 70 70 ILE HA H 1 4.67 . . 1 . . . . . . . . 4073 1 309 . 1 1 70 70 ILE C C 13 176.75 . . 1 . . . . . . . . 4073 1 310 . 1 1 70 70 ILE CA C 13 63.23 . . 1 . . . . . . . . 4073 1 311 . 1 1 70 70 ILE CB C 13 39.35 . . 1 . . . . . . . . 4073 1 312 . 1 1 70 70 ILE N N 15 125.25 . . 1 . . . . . . . . 4073 1 313 . 1 1 71 71 THR H H 1 8.25 . . 1 . . . . . . . . 4073 1 314 . 1 1 71 71 THR HA H 1 4.51 . . 1 . . . . . . . . 4073 1 315 . 1 1 71 71 THR C C 13 175.68 . . 1 . . . . . . . . 4073 1 316 . 1 1 71 71 THR CA C 13 61.18 . . 1 . . . . . . . . 4073 1 317 . 1 1 71 71 THR CB C 13 72.33 . . 1 . . . . . . . . 4073 1 318 . 1 1 71 71 THR N N 15 120.05 . . 1 . . . . . . . . 4073 1 319 . 1 1 72 72 ASP H H 1 9.12 . . 1 . . . . . . . . 4073 1 320 . 1 1 72 72 ASP HA H 1 4.31 . . 1 . . . . . . . . 4073 1 321 . 1 1 72 72 ASP C C 13 177.82 . . 1 . . . . . . . . 4073 1 322 . 1 1 72 72 ASP CA C 13 57.88 . . 1 . . . . . . . . 4073 1 323 . 1 1 72 72 ASP CB C 13 40.20 . . 1 . . . . . . . . 4073 1 324 . 1 1 72 72 ASP N N 15 123.46 . . 1 . . . . . . . . 4073 1 325 . 1 1 73 73 GLU H H 1 9.00 . . 1 . . . . . . . . 4073 1 326 . 1 1 73 73 GLU HA H 1 4.05 . . 1 . . . . . . . . 4073 1 327 . 1 1 73 73 GLU C C 13 179.58 . . 1 . . . . . . . . 4073 1 328 . 1 1 73 73 GLU CA C 13 60.74 . . 1 . . . . . . . . 4073 1 329 . 1 1 73 73 GLU CB C 13 29.32 . . 1 . . . . . . . . 4073 1 330 . 1 1 73 73 GLU N N 15 117.93 . . 1 . . . . . . . . 4073 1 331 . 1 1 74 74 GLU H H 1 7.57 . . 1 . . . . . . . . 4073 1 332 . 1 1 74 74 GLU HA H 1 4.02 . . 1 . . . . . . . . 4073 1 333 . 1 1 74 74 GLU C C 13 178.11 . . 1 . . . . . . . . 4073 1 334 . 1 1 74 74 GLU CA C 13 59.43 . . 1 . . . . . . . . 4073 1 335 . 1 1 74 74 GLU CB C 13 29.17 . . 1 . . . . . . . . 4073 1 336 . 1 1 74 74 GLU N N 15 120.30 . . 1 . . . . . . . . 4073 1 337 . 1 1 75 75 ASN H H 1 8.65 . . 1 . . . . . . . . 4073 1 338 . 1 1 75 75 ASN HA H 1 4.36 . . 1 . . . . . . . . 4073 1 339 . 1 1 75 75 ASN C C 13 177.12 . . 1 . . . . . . . . 4073 1 340 . 1 1 75 75 ASN CA C 13 57.20 . . 1 . . . . . . . . 4073 1 341 . 1 1 75 75 ASN CB C 13 39.16 . . 1 . . . . . . . . 4073 1 342 . 1 1 75 75 ASN N N 15 120.64 . . 1 . . . . . . . . 4073 1 343 . 1 1 76 76 ASP H H 1 8.37 . . 1 . . . . . . . . 4073 1 344 . 1 1 76 76 ASP HA H 1 4.32 . . 1 . . . . . . . . 4073 1 345 . 1 1 76 76 ASP C C 13 178.76 . . 1 . . . . . . . . 4073 1 346 . 1 1 76 76 ASP CA C 13 57.34 . . 1 . . . . . . . . 4073 1 347 . 1 1 76 76 ASP CB C 13 40.42 . . 1 . . . . . . . . 4073 1 348 . 1 1 76 76 ASP N N 15 117.86 . . 1 . . . . . . . . 4073 1 349 . 1 1 77 77 MET H H 1 7.05 . . 1 . . . . . . . . 4073 1 350 . 1 1 77 77 MET HA H 1 4.57 . . 1 . . . . . . . . 4073 1 351 . 1 1 77 77 MET C C 13 180.05 . . 1 . . . . . . . . 4073 1 352 . 1 1 77 77 MET CA C 13 55.78 . . 1 . . . . . . . . 4073 1 353 . 1 1 77 77 MET CB C 13 34.85 . . 1 . . . . . . . . 4073 1 354 . 1 1 77 77 MET N N 15 116.67 . . 1 . . . . . . . . 4073 1 355 . 1 1 78 78 LEU H H 1 8.93 . . 1 . . . . . . . . 4073 1 356 . 1 1 78 78 LEU HA H 1 3.83 . . 1 . . . . . . . . 4073 1 357 . 1 1 78 78 LEU C C 13 178.64 . . 1 . . . . . . . . 4073 1 358 . 1 1 78 78 LEU CA C 13 57.96 . . 1 . . . . . . . . 4073 1 359 . 1 1 78 78 LEU CB C 13 41.61 . . 1 . . . . . . . . 4073 1 360 . 1 1 78 78 LEU N N 15 124.74 . . 1 . . . . . . . . 4073 1 361 . 1 1 79 79 ASP H H 1 8.04 . . 1 . . . . . . . . 4073 1 362 . 1 1 79 79 ASP HA H 1 4.40 . . 1 . . . . . . . . 4073 1 363 . 1 1 79 79 ASP C C 13 177.78 . . 1 . . . . . . . . 4073 1 364 . 1 1 79 79 ASP CA C 13 56.91 . . 1 . . . . . . . . 4073 1 365 . 1 1 79 79 ASP CB C 13 41.24 . . 1 . . . . . . . . 4073 1 366 . 1 1 79 79 ASP N N 15 116.31 . . 1 . . . . . . . . 4073 1 367 . 1 1 80 80 LEU H H 1 7.07 . . 1 . . . . . . . . 4073 1 368 . 1 1 80 80 LEU HA H 1 4.39 . . 1 . . . . . . . . 4073 1 369 . 1 1 80 80 LEU C C 13 177.44 . . 1 . . . . . . . . 4073 1 370 . 1 1 80 80 LEU CA C 13 53.99 . . 1 . . . . . . . . 4073 1 371 . 1 1 80 80 LEU CB C 13 42.60 . . 1 . . . . . . . . 4073 1 372 . 1 1 80 80 LEU N N 15 117.42 . . 1 . . . . . . . . 4073 1 373 . 1 1 81 81 ALA H H 1 7.92 . . 1 . . . . . . . . 4073 1 374 . 1 1 81 81 ALA HA H 1 4.22 . . 1 . . . . . . . . 4073 1 375 . 1 1 81 81 ALA C C 13 177.30 . . 1 . . . . . . . . 4073 1 376 . 1 1 81 81 ALA CA C 13 52.51 . . 1 . . . . . . . . 4073 1 377 . 1 1 81 81 ALA CB C 13 19.32 . . 1 . . . . . . . . 4073 1 378 . 1 1 81 81 ALA N N 15 125.16 . . 1 . . . . . . . . 4073 1 379 . 1 1 82 82 TYR H H 1 8.43 . . 1 . . . . . . . . 4073 1 380 . 1 1 82 82 TYR HA H 1 4.46 . . 1 . . . . . . . . 4073 1 381 . 1 1 82 82 TYR C C 13 177.02 . . 1 . . . . . . . . 4073 1 382 . 1 1 82 82 TYR CA C 13 58.42 . . 1 . . . . . . . . 4073 1 383 . 1 1 82 82 TYR CB C 13 38.96 . . 1 . . . . . . . . 4073 1 384 . 1 1 82 82 TYR N N 15 123.92 . . 1 . . . . . . . . 4073 1 385 . 1 1 83 83 GLY H H 1 8.52 . . 1 . . . . . . . . 4073 1 386 . 1 1 83 83 GLY HA2 H 1 4.97 . . 2 . . . . . . . . 4073 1 387 . 1 1 83 83 GLY HA3 H 1 3.71 . . 2 . . . . . . . . 4073 1 388 . 1 1 83 83 GLY C C 13 174.76 . . 1 . . . . . . . . 4073 1 389 . 1 1 83 83 GLY CA C 13 46.55 . . 1 . . . . . . . . 4073 1 390 . 1 1 83 83 GLY N N 15 113.66 . . 1 . . . . . . . . 4073 1 391 . 1 1 84 84 LEU H H 1 7.31 . . 1 . . . . . . . . 4073 1 392 . 1 1 84 84 LEU HA H 1 3.89 . . 1 . . . . . . . . 4073 1 393 . 1 1 84 84 LEU C C 13 176.69 . . 1 . . . . . . . . 4073 1 394 . 1 1 84 84 LEU CA C 13 57.00 . . 1 . . . . . . . . 4073 1 395 . 1 1 84 84 LEU CB C 13 42.79 . . 1 . . . . . . . . 4073 1 396 . 1 1 84 84 LEU N N 15 119.14 . . 1 . . . . . . . . 4073 1 397 . 1 1 85 85 THR H H 1 8.93 . . 1 . . . . . . . . 4073 1 398 . 1 1 85 85 THR HA H 1 4.97 . . 1 . . . . . . . . 4073 1 399 . 1 1 85 85 THR C C 13 174.88 . . 1 . . . . . . . . 4073 1 400 . 1 1 85 85 THR CA C 13 60.16 . . 1 . . . . . . . . 4073 1 401 . 1 1 85 85 THR CB C 13 74.50 . . 1 . . . . . . . . 4073 1 402 . 1 1 85 85 THR N N 15 118.66 . . 1 . . . . . . . . 4073 1 403 . 1 1 86 86 ASP H H 1 8.57 . . 1 . . . . . . . . 4073 1 404 . 1 1 86 86 ASP HA H 1 4.55 . . 1 . . . . . . . . 4073 1 405 . 1 1 86 86 ASP C C 13 176.09 . . 1 . . . . . . . . 4073 1 406 . 1 1 86 86 ASP CA C 13 54.29 . . 1 . . . . . . . . 4073 1 407 . 1 1 86 86 ASP CB C 13 39.74 . . 1 . . . . . . . . 4073 1 408 . 1 1 86 86 ASP N N 15 118.69 . . 1 . . . . . . . . 4073 1 409 . 1 1 87 87 ARG H H 1 8.39 . . 1 . . . . . . . . 4073 1 410 . 1 1 87 87 ARG HA H 1 4.26 . . 1 . . . . . . . . 4073 1 411 . 1 1 87 87 ARG C C 13 175.75 . . 1 . . . . . . . . 4073 1 412 . 1 1 87 87 ARG CA C 13 53.73 . . 1 . . . . . . . . 4073 1 413 . 1 1 87 87 ARG CB C 13 30.02 . . 1 . . . . . . . . 4073 1 414 . 1 1 87 87 ARG N N 15 120.57 . . 1 . . . . . . . . 4073 1 415 . 1 1 88 88 SER H H 1 7.07 . . 1 . . . . . . . . 4073 1 416 . 1 1 88 88 SER HA H 1 5.48 . . 1 . . . . . . . . 4073 1 417 . 1 1 88 88 SER C C 13 174.64 . . 1 . . . . . . . . 4073 1 418 . 1 1 88 88 SER CA C 13 60.72 . . 1 . . . . . . . . 4073 1 419 . 1 1 88 88 SER CB C 13 65.48 . . 1 . . . . . . . . 4073 1 420 . 1 1 88 88 SER N N 15 120.81 . . 1 . . . . . . . . 4073 1 421 . 1 1 89 89 ARG H H 1 9.46 . . 1 . . . . . . . . 4073 1 422 . 1 1 89 89 ARG HA H 1 4.87 . . 1 . . . . . . . . 4073 1 423 . 1 1 89 89 ARG CA C 13 52.93 . . 1 . . . . . . . . 4073 1 424 . 1 1 89 89 ARG CB C 13 34.17 . . 1 . . . . . . . . 4073 1 425 . 1 1 89 89 ARG N N 15 118.98 . . 1 . . . . . . . . 4073 1 426 . 1 1 94 94 ILE HA H 1 4.25 . . 1 . . . . . . . . 4073 1 427 . 1 1 94 94 ILE C C 13 174.06 . . 1 . . . . . . . . 4073 1 428 . 1 1 94 94 ILE CA C 13 58.01 . . 1 . . . . . . . . 4073 1 429 . 1 1 94 94 ILE CB C 13 37.05 . . 1 . . . . . . . . 4073 1 430 . 1 1 95 95 CYS H H 1 8.20 . . 1 . . . . . . . . 4073 1 431 . 1 1 95 95 CYS HA H 1 5.00 . . 1 . . . . . . . . 4073 1 432 . 1 1 95 95 CYS C C 13 175.16 . . 1 . . . . . . . . 4073 1 433 . 1 1 95 95 CYS CA C 13 57.50 . . 1 . . . . . . . . 4073 1 434 . 1 1 95 95 CYS CB C 13 29.33 . . 1 . . . . . . . . 4073 1 435 . 1 1 95 95 CYS N N 15 124.34 . . 1 . . . . . . . . 4073 1 436 . 1 1 96 96 LEU H H 1 9.05 . . 1 . . . . . . . . 4073 1 437 . 1 1 96 96 LEU HA H 1 4.76 . . 1 . . . . . . . . 4073 1 438 . 1 1 96 96 LEU C C 13 178.97 . . 1 . . . . . . . . 4073 1 439 . 1 1 96 96 LEU CA C 13 55.64 . . 1 . . . . . . . . 4073 1 440 . 1 1 96 96 LEU CB C 13 42.46 . . 1 . . . . . . . . 4073 1 441 . 1 1 96 96 LEU N N 15 121.35 . . 1 . . . . . . . . 4073 1 442 . 1 1 97 97 THR H H 1 7.86 . . 1 . . . . . . . . 4073 1 443 . 1 1 97 97 THR HA H 1 4.68 . . 1 . . . . . . . . 4073 1 444 . 1 1 97 97 THR C C 13 175.30 . . 1 . . . . . . . . 4073 1 445 . 1 1 97 97 THR CA C 13 59.42 . . 1 . . . . . . . . 4073 1 446 . 1 1 97 97 THR CB C 13 71.69 . . 1 . . . . . . . . 4073 1 447 . 1 1 97 97 THR N N 15 114.58 . . 1 . . . . . . . . 4073 1 448 . 1 1 98 98 LYS H H 1 9.28 . . 1 . . . . . . . . 4073 1 449 . 1 1 98 98 LYS HA H 1 3.92 . . 1 . . . . . . . . 4073 1 450 . 1 1 98 98 LYS C C 13 179.19 . . 1 . . . . . . . . 4073 1 451 . 1 1 98 98 LYS CA C 13 59.55 . . 1 . . . . . . . . 4073 1 452 . 1 1 98 98 LYS CB C 13 32.08 . . 1 . . . . . . . . 4073 1 453 . 1 1 98 98 LYS N N 15 122.12 . . 1 . . . . . . . . 4073 1 454 . 1 1 99 99 SER H H 1 8.22 . . 1 . . . . . . . . 4073 1 455 . 1 1 99 99 SER HA H 1 4.30 . . 1 . . . . . . . . 4073 1 456 . 1 1 99 99 SER C C 13 174.77 . . 1 . . . . . . . . 4073 1 457 . 1 1 99 99 SER CA C 13 60.42 . . 1 . . . . . . . . 4073 1 458 . 1 1 99 99 SER CB C 13 62.69 . . 1 . . . . . . . . 4073 1 459 . 1 1 99 99 SER N N 15 113.39 . . 1 . . . . . . . . 4073 1 460 . 1 1 100 100 MET H H 1 7.73 . . 1 . . . . . . . . 4073 1 461 . 1 1 100 100 MET HA H 1 4.16 . . 1 . . . . . . . . 4073 1 462 . 1 1 100 100 MET C C 13 174.12 . . 1 . . . . . . . . 4073 1 463 . 1 1 100 100 MET CA C 13 56.92 . . 1 . . . . . . . . 4073 1 464 . 1 1 100 100 MET CB C 13 32.37 . . 1 . . . . . . . . 4073 1 465 . 1 1 100 100 MET N N 15 121.20 . . 1 . . . . . . . . 4073 1 466 . 1 1 101 101 ASP H H 1 7.27 . . 1 . . . . . . . . 4073 1 467 . 1 1 101 101 ASP HA H 1 4.41 . . 1 . . . . . . . . 4073 1 468 . 1 1 101 101 ASP C C 13 177.82 . . 1 . . . . . . . . 4073 1 469 . 1 1 101 101 ASP CA C 13 57.02 . . 1 . . . . . . . . 4073 1 470 . 1 1 101 101 ASP CB C 13 40.94 . . 1 . . . . . . . . 4073 1 471 . 1 1 101 101 ASP N N 15 118.59 . . 1 . . . . . . . . 4073 1 472 . 1 1 102 102 ASN H H 1 10.06 . . 1 . . . . . . . . 4073 1 473 . 1 1 102 102 ASN HA H 1 3.88 . . 1 . . . . . . . . 4073 1 474 . 1 1 102 102 ASN C C 13 174.34 . . 1 . . . . . . . . 4073 1 475 . 1 1 102 102 ASN CA C 13 55.90 . . 1 . . . . . . . . 4073 1 476 . 1 1 102 102 ASN CB C 13 38.01 . . 1 . . . . . . . . 4073 1 477 . 1 1 102 102 ASN N N 15 123.28 . . 1 . . . . . . . . 4073 1 478 . 1 1 103 103 MET H H 1 8.48 . . 1 . . . . . . . . 4073 1 479 . 1 1 103 103 MET HA H 1 4.70 . . 1 . . . . . . . . 4073 1 480 . 1 1 103 103 MET C C 13 173.08 . . 1 . . . . . . . . 4073 1 481 . 1 1 103 103 MET CA C 13 56.67 . . 1 . . . . . . . . 4073 1 482 . 1 1 103 103 MET CB C 13 31.45 . . 1 . . . . . . . . 4073 1 483 . 1 1 103 103 MET N N 15 118.84 . . 1 . . . . . . . . 4073 1 484 . 1 1 104 104 THR H H 1 8.69 . . 1 . . . . . . . . 4073 1 485 . 1 1 104 104 THR HA H 1 5.47 . . 1 . . . . . . . . 4073 1 486 . 1 1 104 104 THR C C 13 175.97 . . 1 . . . . . . . . 4073 1 487 . 1 1 104 104 THR CA C 13 61.83 . . 1 . . . . . . . . 4073 1 488 . 1 1 104 104 THR CB C 13 70.59 . . 1 . . . . . . . . 4073 1 489 . 1 1 104 104 THR N N 15 117.57 . . 1 . . . . . . . . 4073 1 490 . 1 1 105 105 VAL H H 1 9.19 . . 1 . . . . . . . . 4073 1 491 . 1 1 105 105 VAL HA H 1 4.62 . . 1 . . . . . . . . 4073 1 492 . 1 1 105 105 VAL CA C 13 58.32 . . 1 . . . . . . . . 4073 1 493 . 1 1 105 105 VAL CB C 13 34.48 . . 1 . . . . . . . . 4073 1 494 . 1 1 105 105 VAL N N 15 123.32 . . 1 . . . . . . . . 4073 1 495 . 1 1 106 106 ARG H H 1 8.44 . . 1 . . . . . . . . 4073 1 496 . 1 1 106 106 ARG HA H 1 4.31 . . 1 . . . . . . . . 4073 1 497 . 1 1 106 106 ARG CA C 13 54.57 . . 1 . . . . . . . . 4073 1 498 . 1 1 106 106 ARG CB C 13 33.96 . . 1 . . . . . . . . 4073 1 499 . 1 1 106 106 ARG N N 15 121.33 . . 1 . . . . . . . . 4073 1 500 . 1 1 108 108 PRO HA H 1 4.30 . . 1 . . . . . . . . 4073 1 501 . 1 1 108 108 PRO C C 13 176.32 . . 1 . . . . . . . . 4073 1 502 . 1 1 108 108 PRO CA C 13 62.95 . . 1 . . . . . . . . 4073 1 503 . 1 1 108 108 PRO CB C 13 32.38 . . 1 . . . . . . . . 4073 1 504 . 1 1 109 109 GLU H H 1 8.69 . . 1 . . . . . . . . 4073 1 505 . 1 1 109 109 GLU HA H 1 4.22 . . 1 . . . . . . . . 4073 1 506 . 1 1 109 109 GLU C C 13 176.48 . . 1 . . . . . . . . 4073 1 507 . 1 1 109 109 GLU CA C 13 57.22 . . 1 . . . . . . . . 4073 1 508 . 1 1 109 109 GLU CB C 13 30.91 . . 1 . . . . . . . . 4073 1 509 . 1 1 109 109 GLU N N 15 121.77 . . 1 . . . . . . . . 4073 1 510 . 1 1 110 110 THR H H 1 8.38 . . 1 . . . . . . . . 4073 1 511 . 1 1 110 110 THR HA H 1 4.35 . . 1 . . . . . . . . 4073 1 512 . 1 1 110 110 THR C C 13 174.09 . . 1 . . . . . . . . 4073 1 513 . 1 1 110 110 THR CA C 13 61.51 . . 1 . . . . . . . . 4073 1 514 . 1 1 110 110 THR CB C 13 70.24 . . 1 . . . . . . . . 4073 1 515 . 1 1 110 110 THR N N 15 115.08 . . 1 . . . . . . . . 4073 1 516 . 1 1 111 111 VAL H H 1 7.95 . . 1 . . . . . . . . 4073 1 517 . 1 1 111 111 VAL HA H 1 3.93 . . 1 . . . . . . . . 4073 1 518 . 1 1 111 111 VAL C C 13 175.46 . . 1 . . . . . . . . 4073 1 519 . 1 1 111 111 VAL CA C 13 61.87 . . 1 . . . . . . . . 4073 1 520 . 1 1 111 111 VAL CB C 13 33.20 . . 1 . . . . . . . . 4073 1 521 . 1 1 111 111 VAL N N 15 122.76 . . 1 . . . . . . . . 4073 1 522 . 1 1 112 112 ALA H H 1 8.34 . . 1 . . . . . . . . 4073 1 523 . 1 1 112 112 ALA HA H 1 4.24 . . 1 . . . . . . . . 4073 1 524 . 1 1 112 112 ALA C C 13 177.55 . . 1 . . . . . . . . 4073 1 525 . 1 1 112 112 ALA CA C 13 52.47 . . 1 . . . . . . . . 4073 1 526 . 1 1 112 112 ALA CB C 13 19.67 . . 1 . . . . . . . . 4073 1 527 . 1 1 112 112 ALA N N 15 129.12 . . 1 . . . . . . . . 4073 1 528 . 1 1 113 113 ASP H H 1 8.39 . . 1 . . . . . . . . 4073 1 529 . 1 1 113 113 ASP HA H 1 4.53 . . 1 . . . . . . . . 4073 1 530 . 1 1 113 113 ASP C C 13 175.09 . . 1 . . . . . . . . 4073 1 531 . 1 1 113 113 ASP CA C 13 54.62 . . 1 . . . . . . . . 4073 1 532 . 1 1 113 113 ASP CB C 13 41.16 . . 1 . . . . . . . . 4073 1 533 . 1 1 113 113 ASP N N 15 121.32 . . 1 . . . . . . . . 4073 1 534 . 1 1 114 114 ALA H H 1 7.91 . . 1 . . . . . . . . 4073 1 535 . 1 1 114 114 ALA HA H 1 4.09 . . 1 . . . . . . . . 4073 1 536 . 1 1 114 114 ALA CA C 13 54.03 . . 1 . . . . . . . . 4073 1 537 . 1 1 114 114 ALA CB C 13 20.38 . . 1 . . . . . . . . 4073 1 538 . 1 1 114 114 ALA N N 15 130.28 . . 1 . . . . . . . . 4073 1 stop_ save_