data_4944 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4944 _Entry.Title ; 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state. ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-01-22 _Entry.Accession_date 2001-01-22 _Entry.Last_release_date 2001-05-17 _Entry.Original_release_date 2001-05-17 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _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.Entry_ID 1 Doris Jacobs . M. . 4944 2 Joris Messens . . . 4944 3 Rainer Wechselberger . . . 4944 4 Elke Brosens . . . 4944 5 Lode Wyns . . . 4944 6 Rudolph Willem . . . 4944 7 Jose Martins . C. . 4944 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4944 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 244 4944 '13C chemical shifts' 358 4944 '15N chemical shifts' 122 4944 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 1 . . 2001-05-17 2001-01-22 original author . 4944 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4944 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 20 _Citation.Journal_issue 1 _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 95 _Citation.Page_last 96 _Citation.Year 2001 _Citation.Details ; See references in saveframes ref_1, ref_2, ref-3, and ref_4. ; 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.Entry_ID _Citation_author.Citation_ID 1 Doris Jacobs . M. . 4944 1 2 Joris Messens . . . 4944 1 3 Rainer Wechselberger . W. . 4944 1 4 Elke Brosens . . . 4944 1 5 Rudolph Willem . . . 4944 1 6 Lode Wyns . . . 4944 1 7 Jose Martins . C. . 4944 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID arsenate 4944 1 'arsenate reductase' 4944 1 metal-resistance 4944 1 ArsC 4944 1 thioredoxin 4944 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4944 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1409657 _Citation.Full_citation ; Ji G, Silver S. Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9474-8. ; _Citation.Title 'Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 89 _Citation.Journal_issue 20 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _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 9474 _Citation.Page_last 9478 _Citation.Year 1992 _Citation.Details ; The arsenic resistance operon of Staphylococcus aureus plasmid pI258 consists of three genes, arsR (encoding the repressor regulatory protein), arsB (the determinant of the membrane efflux protein that confers resistance by pumping arsenic from the cells), and arsC (the small gene whose protein product is required for arsenate resistance only, not for arsenite resistance). ArsC has now been shown to be an arsenate reductase, converting intracellular arsenate [As(V)] to arsenite [As(III)], which is then exported from the cells by an energy-dependent efflux process. The arsenate reductase activity was found in the soluble cytoplasmic fraction in Escherichia coli (and not associated with the periplasmic fraction or the sedimentable cell envelope). Purified ArsC protein coupled in vitro with thioredoxin plus dithiothreitol (but not 2-mercaptoethanol or reduced glutathione) to reduce arsenate to arsenite. ; 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.Entry_ID _Citation_author.Citation_ID 1 G Ji G. . . 4944 2 2 S Silver S. . . 4944 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4944 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8003493 _Citation.Full_citation ; Ji G, Garber EA, Armes LG, Chen CM, Fuchs JA, Silver S. Arsenate reductase of Staphylococcus aureus plasmid pI258. Biochemistry. 1994 Jun 14;33(23):7294-9. ; _Citation.Title 'Arsenate reductase of Staphylococcus aureus plasmid pI258.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 33 _Citation.Journal_issue 23 _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 7294 _Citation.Page_last 7299 _Citation.Year 1994 _Citation.Details ; Arsenate reductase encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 was overproduced in Escherichia coli and purified. The purified enzyme reduced radioactive arsenate to arsenite when coupled to thioredoxin, thioredoxin reductase, and NADPH. NADPH oxidation coupled to arsenate reduction also required thioredoxin and thioredoxin reductase. Glutaredoxin and reduced glutathione did not stimulate arsenate reduction. NADPH oxidation showed Michaelis-Menten kinetics with a Km of 1 microM AsO4(3-) and an apparent Vmax of 200 nmol/min per mg of protein. At high substrate concentration (above 1 mM AsO4(3-), a secondary rise in the reaction rate was observed, with a Km of 2 mM and an apparent Vmax of 450 nmol/min per mg of protein. This secondary rise also occurred upon addition of phosphate or nitrate (which were not substrates for the enzyme). Arsenite (the product of the enzyme), tellurite, and antimonite [Sb(III)] were inhibitors. Selenate (but not selenite or sulfate) was a substrate for reductase-dependent NADPH oxidation, with an apparent Km of 13 mM SeO4(2-). Arsenate reductase was purified as a monomer of 14.5 kDa, consistent with the DNA sequence. Electrospray mass spectrometry showed two molecular masses of 14,810.5 and 14,436.0 Da, suggesting that 70% of the purified protein lacked the N-terminal three amino acids; HPLC coupled to electrospray mass spectroscopy of protease digest products confirmed this conclusion and verified the entire amino acid sequence. ; 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.Entry_ID _Citation_author.Citation_ID 1 G Ji G. . . 4944 3 2 'E A' Garber E. A. . 4944 3 3 'L G' Armes L. G. . 4944 3 4 'C M' Chen C. M. . 4944 3 5 'J A' Fuchs J. A. . 4944 3 6 S Silver S. . . 4944 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4944 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10681053 _Citation.Full_citation ; Messens J, Hayburn G, Brosens E, Laus G, Wyns L. Development of a downstream process for the isolation of Staphylococcus aureus arsenate reductase overproduced in Escherichia coli. J Chromatogr B Biomed Sci Appl. 2000 Jan 14;737(1-2):167-78. ; _Citation.Title 'Development of a downstream process for the isolation of Staphylococcus aureus arsenate reductase overproduced in Escherichia coli.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Chromatogr. B Biomed. Sci. Appl.' _Citation.Journal_name_full 'Journal of chromatography. B, Biomedical sciences and applications' _Citation.Journal_volume 737 _Citation.Journal_issue 1-2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1387-2273 _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 167 _Citation.Page_last 178 _Citation.Year 2000 _Citation.Details ; Arsenate reductase (ArsC) encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 reduces intracellular As(V) (arsenate) to the more toxic As(III) (arsenite). In order to study the structure of ArsC and to unravel biochemical and physical properties of this redox enzyme, wild type enzyme and a number of cysteine mutants were overproduced soluble in Escherichia coli. In this paper we describe a novel purification method to obtain high production levels of highly pure enzyme. A reversed-phase method was developed to separate and analyze the many different forms of ArsC. The oxidation state and the methionine oxidized forms were determined by mass spectroscopy. ; 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.Entry_ID _Citation_author.Citation_ID 1 J Messens J. . . 4944 4 2 G Hayburn G. . . 4944 4 3 E Brosens E. . . 4944 4 4 G Laus G. . . 4944 4 5 L Wyns L. . . 4944 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4944 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10606519 _Citation.Full_citation ; Messens J, Hayburn G, Desmyter A, Laus G, Wyns L. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry. 1999 Dec 21;38(51):16857-65. ; _Citation.Title 'The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 38 _Citation.Journal_issue 51 _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 16857 _Citation.Page_last 16865 _Citation.Year 1999 _Citation.Details ; Arsenate reductase (ArsC) encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 reduces intracellular As(V) (arsenate) to the more toxic As(III) (arsenite), which is subsequently extruded from the cell. ArsC couples to thioredoxin, thioredoxin reductase, and NADPH to be enzymatically active. A novel purification method leads to high production levels of highly pure enzyme. A reverse phase method was introduced to systematically analyze and control the oxidation status of the enzyme. The essential cysteinyl residues and redox couple in arsenate reductase were identified by a combination of site-specific mutagenesis and endoprotease-digest mass spectroscopy analysis. The secondary structures, as determined with CD, of wild-type ArsC and its Cys mutants showed a relatively high helical content, independent of the redox status. Mutation of Cys 10, 82, and 89 led to redox-inactive enzymes. ArsC was oxidized in a single catalytic cycle and subsequently digested with endoproteinases ArgC, AspN, and GluC. From the peptide-mass profiles, cysteines 82 and 89 were identified as the redox couple of ArsC necessary to reduce arsenate to arsenite. ; 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.Entry_ID _Citation_author.Citation_ID 1 J Messens J. . . 4944 5 2 G Hayburn G. . . 4944 5 3 A Desmyter A. . . 4944 5 4 G Laus G. . . 4944 5 5 L Wyns L. . . 4944 5 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_ArsC _Assembly.Sf_category assembly _Assembly.Sf_framecode system_ArsC _Assembly.Entry_ID 4944 _Assembly.ID 1 _Assembly.Name 'Arsenate reductase' _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 no _Assembly.Thiol_state 'all free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4944 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 'arsenate reductase' 1 $ArsC . . . native . . . . . 4944 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Arsenate reductase' system 4944 1 ArsC abbreviation 4944 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'arsenate reductase' 4944 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ArsC _Entity.Sf_category entity _Entity.Sf_framecode ArsC _Entity.Entry_ID 4944 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Arsenate reductase' _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 ; MDKKTIYFICTGNSCRSQMA EGWGKEILGEGWNVYSAGIE THGVNPKAIEAMKEVDIDIS NHTSDLIDNDILKQSDLVVT LCSDADNNCPILPPNVKKEH WGFDDPAGKEWSEFQRVRDE IKLAIEKFKLR ; _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 131 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14812 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The N-terminal segment contains a sequence identical to the conserved consensus sequence in low molecular weight tyrosine phosphatase. C82 and C89 have been identified as the redox pair involved in arsenate reduction. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1JF8 . "X-ray Structure Of Reduced C10s, C15a Arsenate Reductase From Pi258" . . . . . 100.00 131 98.47 98.47 2.25e-89 . . . . 4944 1 2 no PDB 1JFV . "X-Ray Structure Of Oxidised C10s, C15a Arsenate Reductase From Pi258" . . . . . 100.00 131 96.95 96.95 3.17e-87 . . . . 4944 1 3 no PDB 1LJL . "Wild Type Pi258 S. Aureus Arsenate Reductase" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 4 no PDB 1LJU . "X-Ray Structure Of C15a Arsenate Reductase From Pi258 Complexed With Arsenite" . . . . . 100.00 131 98.47 98.47 4.78e-89 . . . . 4944 1 5 no PDB 1LK0 . "Disulfide Intermediate Of C89l Arsenate Reductase From Pi258" . . . . . 100.00 131 99.24 99.24 5.93e-90 . . . . 4944 1 6 no PDB 1RXE . "Arsc Complexed With Mnb" . . . . . 100.00 131 97.71 97.71 1.54e-88 . . . . 4944 1 7 no PDB 1RXI . "Pi258 Arsenate Reductase (Arsc) Triple Mutant C10sC15AC82S" . . . . . 100.00 131 97.71 97.71 1.54e-88 . . . . 4944 1 8 no PDB 2CD7 . "Staphylococcus Aureus Pi258 Arsenate Reductase (Arsc) H62q Mutant" . . . . . 100.00 131 99.24 99.24 2.50e-90 . . . . 4944 1 9 no PDB 2FXI . "Arsenate Reductase (Arsc From Pi258) C10sC15A DOUBLE Mutant With Sulfate In Its Active Site" . . . . . 100.00 131 98.47 98.47 2.25e-89 . . . . 4944 1 10 no DBJ BAB43887 . "arsenate reductase [Staphylococcus aureus subsp. aureus N315]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 11 no DBJ BAC54538 . "unnamed protein product [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 12 no DBJ BAE18778 . "arsenate reductase [Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305]" . . . . . 100.00 131 96.95 99.24 1.64e-88 . . . . 4944 1 13 no DBJ BAE92851 . "arsenic reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 14 no DBJ BAG12261 . "arsenate reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 15 no EMBL CAG39708 . "arsenate reductase [Staphylococcus aureus subsp. aureus MRSA252]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 16 no GB AAA25638 . "arsenate reductase [Plasmid pI258]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 17 no GB ACZ58845 . "Arsenate reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 18 no GB ACZ68457 . "Arsenate reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 19 no GB ACZ68855 . "Arsenate reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 20 no GB ACZ68904 . "Arsenate reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 21 no REF NP_395554 . "arsenate reductase [Staphylococcus aureus subsp. aureus N315]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 22 no REF WP_000358995 . "arsenate reductase [Staphylococcus aureus]" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 23 no REF WP_002452591 . "arsenate reductase [Staphylococcus capitis]" . . . . . 61.07 80 97.50 100.00 2.73e-48 . . . . 4944 1 24 no REF WP_002508683 . "arsenate reductase [Staphylococcus sp. OJ82]" . . . . . 100.00 131 96.95 98.47 2.43e-88 . . . . 4944 1 25 no REF WP_003756625 . "MULTISPECIES: arsenate reductase [Bacillales]" . . . . . 100.00 131 99.24 100.00 1.69e-90 . . . . 4944 1 26 no SP P0A005 . "RecName: Full=Protein ArsC; AltName: Full=Arsenate reductase; AltName: Full=Arsenical pump modifier; AltName: Full=Low molecula" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 27 no SP P0A006 . "RecName: Full=Protein ArsC; AltName: Full=Arsenate reductase; AltName: Full=Arsenical pump modifier; AltName: Full=Low molecula" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 28 no SP Q49WS7 . "RecName: Full=Protein ArsC 1; AltName: Full=Arsenate reductase 1; AltName: Full=Arsenical pump modifier 1; AltName: Full=Low mo" . . . . . 100.00 131 96.95 99.24 1.64e-88 . . . . 4944 1 29 no SP Q6GIZ3 . "RecName: Full=Protein ArsC; AltName: Full=Arsenate reductase; AltName: Full=Arsenical pump modifier; AltName: Full=Low molecula" . . . . . 100.00 131 100.00 100.00 2.76e-91 . . . . 4944 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Arsenate reductase' common 4944 1 ArsC abbreviation 4944 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 . MET . 4944 1 2 . ASP . 4944 1 3 . LYS . 4944 1 4 . LYS . 4944 1 5 . THR . 4944 1 6 . ILE . 4944 1 7 . TYR . 4944 1 8 . PHE . 4944 1 9 . ILE . 4944 1 10 . CYS . 4944 1 11 . THR . 4944 1 12 . GLY . 4944 1 13 . ASN . 4944 1 14 . SER . 4944 1 15 . CYS . 4944 1 16 . ARG . 4944 1 17 . SER . 4944 1 18 . GLN . 4944 1 19 . MET . 4944 1 20 . ALA . 4944 1 21 . GLU . 4944 1 22 . GLY . 4944 1 23 . TRP . 4944 1 24 . GLY . 4944 1 25 . LYS . 4944 1 26 . GLU . 4944 1 27 . ILE . 4944 1 28 . LEU . 4944 1 29 . GLY . 4944 1 30 . GLU . 4944 1 31 . GLY . 4944 1 32 . TRP . 4944 1 33 . ASN . 4944 1 34 . VAL . 4944 1 35 . TYR . 4944 1 36 . SER . 4944 1 37 . ALA . 4944 1 38 . GLY . 4944 1 39 . ILE . 4944 1 40 . GLU . 4944 1 41 . THR . 4944 1 42 . HIS . 4944 1 43 . GLY . 4944 1 44 . VAL . 4944 1 45 . ASN . 4944 1 46 . PRO . 4944 1 47 . LYS . 4944 1 48 . ALA . 4944 1 49 . ILE . 4944 1 50 . GLU . 4944 1 51 . ALA . 4944 1 52 . MET . 4944 1 53 . LYS . 4944 1 54 . GLU . 4944 1 55 . VAL . 4944 1 56 . ASP . 4944 1 57 . ILE . 4944 1 58 . ASP . 4944 1 59 . ILE . 4944 1 60 . SER . 4944 1 61 . ASN . 4944 1 62 . HIS . 4944 1 63 . THR . 4944 1 64 . SER . 4944 1 65 . ASP . 4944 1 66 . LEU . 4944 1 67 . ILE . 4944 1 68 . ASP . 4944 1 69 . ASN . 4944 1 70 . ASP . 4944 1 71 . ILE . 4944 1 72 . LEU . 4944 1 73 . LYS . 4944 1 74 . GLN . 4944 1 75 . SER . 4944 1 76 . ASP . 4944 1 77 . LEU . 4944 1 78 . VAL . 4944 1 79 . VAL . 4944 1 80 . THR . 4944 1 81 . LEU . 4944 1 82 . CYS . 4944 1 83 . SER . 4944 1 84 . ASP . 4944 1 85 . ALA . 4944 1 86 . ASP . 4944 1 87 . ASN . 4944 1 88 . ASN . 4944 1 89 . CYS . 4944 1 90 . PRO . 4944 1 91 . ILE . 4944 1 92 . LEU . 4944 1 93 . PRO . 4944 1 94 . PRO . 4944 1 95 . ASN . 4944 1 96 . VAL . 4944 1 97 . LYS . 4944 1 98 . LYS . 4944 1 99 . GLU . 4944 1 100 . HIS . 4944 1 101 . TRP . 4944 1 102 . GLY . 4944 1 103 . PHE . 4944 1 104 . ASP . 4944 1 105 . ASP . 4944 1 106 . PRO . 4944 1 107 . ALA . 4944 1 108 . GLY . 4944 1 109 . LYS . 4944 1 110 . GLU . 4944 1 111 . TRP . 4944 1 112 . SER . 4944 1 113 . GLU . 4944 1 114 . PHE . 4944 1 115 . GLN . 4944 1 116 . ARG . 4944 1 117 . VAL . 4944 1 118 . ARG . 4944 1 119 . ASP . 4944 1 120 . GLU . 4944 1 121 . ILE . 4944 1 122 . LYS . 4944 1 123 . LEU . 4944 1 124 . ALA . 4944 1 125 . ILE . 4944 1 126 . GLU . 4944 1 127 . LYS . 4944 1 128 . PHE . 4944 1 129 . LYS . 4944 1 130 . LEU . 4944 1 131 . ARG . 4944 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 . MET 1 1 4944 1 . ASP 2 2 4944 1 . LYS 3 3 4944 1 . LYS 4 4 4944 1 . THR 5 5 4944 1 . ILE 6 6 4944 1 . TYR 7 7 4944 1 . PHE 8 8 4944 1 . ILE 9 9 4944 1 . CYS 10 10 4944 1 . THR 11 11 4944 1 . GLY 12 12 4944 1 . ASN 13 13 4944 1 . SER 14 14 4944 1 . CYS 15 15 4944 1 . ARG 16 16 4944 1 . SER 17 17 4944 1 . GLN 18 18 4944 1 . MET 19 19 4944 1 . ALA 20 20 4944 1 . GLU 21 21 4944 1 . GLY 22 22 4944 1 . TRP 23 23 4944 1 . GLY 24 24 4944 1 . LYS 25 25 4944 1 . GLU 26 26 4944 1 . ILE 27 27 4944 1 . LEU 28 28 4944 1 . GLY 29 29 4944 1 . GLU 30 30 4944 1 . GLY 31 31 4944 1 . TRP 32 32 4944 1 . ASN 33 33 4944 1 . VAL 34 34 4944 1 . TYR 35 35 4944 1 . SER 36 36 4944 1 . ALA 37 37 4944 1 . GLY 38 38 4944 1 . ILE 39 39 4944 1 . GLU 40 40 4944 1 . THR 41 41 4944 1 . HIS 42 42 4944 1 . GLY 43 43 4944 1 . VAL 44 44 4944 1 . ASN 45 45 4944 1 . PRO 46 46 4944 1 . LYS 47 47 4944 1 . ALA 48 48 4944 1 . ILE 49 49 4944 1 . GLU 50 50 4944 1 . ALA 51 51 4944 1 . MET 52 52 4944 1 . LYS 53 53 4944 1 . GLU 54 54 4944 1 . VAL 55 55 4944 1 . ASP 56 56 4944 1 . ILE 57 57 4944 1 . ASP 58 58 4944 1 . ILE 59 59 4944 1 . SER 60 60 4944 1 . ASN 61 61 4944 1 . HIS 62 62 4944 1 . THR 63 63 4944 1 . SER 64 64 4944 1 . ASP 65 65 4944 1 . LEU 66 66 4944 1 . ILE 67 67 4944 1 . ASP 68 68 4944 1 . ASN 69 69 4944 1 . ASP 70 70 4944 1 . ILE 71 71 4944 1 . LEU 72 72 4944 1 . LYS 73 73 4944 1 . GLN 74 74 4944 1 . SER 75 75 4944 1 . ASP 76 76 4944 1 . LEU 77 77 4944 1 . VAL 78 78 4944 1 . VAL 79 79 4944 1 . THR 80 80 4944 1 . LEU 81 81 4944 1 . CYS 82 82 4944 1 . SER 83 83 4944 1 . ASP 84 84 4944 1 . ALA 85 85 4944 1 . ASP 86 86 4944 1 . ASN 87 87 4944 1 . ASN 88 88 4944 1 . CYS 89 89 4944 1 . PRO 90 90 4944 1 . ILE 91 91 4944 1 . LEU 92 92 4944 1 . PRO 93 93 4944 1 . PRO 94 94 4944 1 . ASN 95 95 4944 1 . VAL 96 96 4944 1 . LYS 97 97 4944 1 . LYS 98 98 4944 1 . GLU 99 99 4944 1 . HIS 100 100 4944 1 . TRP 101 101 4944 1 . GLY 102 102 4944 1 . PHE 103 103 4944 1 . ASP 104 104 4944 1 . ASP 105 105 4944 1 . PRO 106 106 4944 1 . ALA 107 107 4944 1 . GLY 108 108 4944 1 . LYS 109 109 4944 1 . GLU 110 110 4944 1 . TRP 111 111 4944 1 . SER 112 112 4944 1 . GLU 113 113 4944 1 . PHE 114 114 4944 1 . GLN 115 115 4944 1 . ARG 116 116 4944 1 . VAL 117 117 4944 1 . ARG 118 118 4944 1 . ASP 119 119 4944 1 . GLU 120 120 4944 1 . ILE 121 121 4944 1 . LYS 122 122 4944 1 . LEU 123 123 4944 1 . ALA 124 124 4944 1 . ILE 125 125 4944 1 . GLU 126 126 4944 1 . LYS 127 127 4944 1 . PHE 128 128 4944 1 . LYS 129 129 4944 1 . LEU 130 130 4944 1 . ARG 131 131 4944 1 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 4944 _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.Subvariant _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.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $ArsC . 1280 . . 'Staphylococcus aureus' 'Staphylococcus aureus' . . Eubacteria . Staphylococcus aureus . . . . . . . . . . . . . . pI258 . ars . . . . 4944 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 4944 _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_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _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.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $ArsC . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 . . . . . . . . . . . . plasmid . . pET11a . . . . . . 4944 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4944 _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 'Arsenate reductase' '[U-95% 13C; U-98% 15N]' . . 1 $ArsC . . 1.8 . . mM . . . . 4944 1 2 DTT . . . . . . . 1.0 . . mM . . . . 4944 1 3 EDTA . . . . . . . 0.1 . . mM . . . . 4944 1 4 K2SO4 . . . . . . . 50 . . mM . . . . 4944 1 5 'potassium phosphate buffer' . . . . . . . 50 . . mM . . . . 4944 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4944 _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 'Arsenate reductase' '[U-98% 15N]' . . 1 $ArsC . . 1.8 . . mM . . . . 4944 2 2 DTT . . . . . . . 1.0 . . mM . . . . 4944 2 3 EDTA . . . . . . . 0.1 . . mM . . . . 4944 2 4 K2SO4 . . . . . . . 50 . . mM . . . . 4944 2 5 'potassium phosphate buffer' . . . . . . . 50 . . mM . . . . 4944 2 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4944 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; ArsC is sensitive to oxidation. Therefore all sample preparation was performed under reducing conditions, i.e. using argon flushed solutions to which DTT was added, at all times ; 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 6.7 0.1 n/a 4944 1 temperature 298 0.5 K 4944 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 4944 _Software.ID 1 _Software.Name FELIX _Software.Version 97.0 _Software.Details 'commercial software from MSI (San Diege, CA)' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 4944 1 'manual peak picking' 4944 1 'manual assignment' 4944 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4944 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4944 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 4944 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _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 4944 _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 NMR_spectrometer_1 Bruker AMX . 500 . . . 4944 1 2 NMR_spectrometer_2 Bruker DRX . 600 . . . 4944 1 3 NMR_spectrometer_3 Varian Inova . 750 . . . 4944 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 4944 _Experiment_list.ID 1 _Experiment_list.Details . 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 '1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 2 '1H-15N HSQC-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 3 '1H-15N HSQC-NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 4 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 5 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 6 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 7 HN(CA)CO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 8 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 9 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4944 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-15N HSQC-TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '1H-15N HSQC-NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HN(CA)CO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 4944 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4944 _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.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct . . . . . . . . . . 4944 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4944 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4944 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 4944 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_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 '1H-15N HSQC' . . . 4944 1 2 '1H-15N HSQC-TOCSY' . . . 4944 1 3 '1H-15N HSQC-NOESY' . . . 4944 1 4 HNCA . . . 4944 1 5 HNCO . . . 4944 1 6 HN(CO)CA . . . 4944 1 7 HN(CA)CO . . . 4944 1 8 CBCA(CO)NH . . . 4944 1 9 HNCACB . . . 4944 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 1 1 MET C C 13 174.67 0.2 . 1 . . . . . . . . 4944 1 2 . 1 1 1 1 MET CA C 13 57.36 0.2 . 1 . . . . . . . . 4944 1 3 . 1 1 1 1 MET CB C 13 40.92 0.2 . 1 . . . . . . . . 4944 1 4 . 1 1 2 2 ASP H H 1 7.93 0.2 . 1 . . . . . . . . 4944 1 5 . 1 1 2 2 ASP HA H 1 4.38 0.02 . 1 . . . . . . . . 4944 1 6 . 1 1 2 2 ASP C C 13 176.78 0.2 . 1 . . . . . . . . 4944 1 7 . 1 1 2 2 ASP CA C 13 54.11 0.2 . 1 . . . . . . . . 4944 1 8 . 1 1 2 2 ASP N N 15 116.82 0.2 . 1 . . . . . . . . 4944 1 9 . 1 1 2 2 ASP CB C 13 38.02 0.2 . 1 . . . . . . . . 4944 1 10 . 1 1 3 3 LYS H H 1 8.29 0.2 . 1 . . . . . . . . 4944 1 11 . 1 1 3 3 LYS HA H 1 4.11 0.02 . 1 . . . . . . . . 4944 1 12 . 1 1 3 3 LYS C C 13 174.2 0.2 . 1 . . . . . . . . 4944 1 13 . 1 1 3 3 LYS CA C 13 55.52 0.2 . 1 . . . . . . . . 4944 1 14 . 1 1 3 3 LYS N N 15 122.57 0.2 . 1 . . . . . . . . 4944 1 15 . 1 1 3 3 LYS CB C 13 33.76 0.2 . 1 . . . . . . . . 4944 1 16 . 1 1 4 4 LYS H H 1 7.23 0.2 . 1 . . . . . . . . 4944 1 17 . 1 1 4 4 LYS HA H 1 4.27 0.02 . 1 . . . . . . . . 4944 1 18 . 1 1 4 4 LYS C C 13 171.62 0.2 . 1 . . . . . . . . 4944 1 19 . 1 1 4 4 LYS CA C 13 54.51 0.2 . 1 . . . . . . . . 4944 1 20 . 1 1 4 4 LYS N N 15 124.3 0.2 . 1 . . . . . . . . 4944 1 21 . 1 1 4 4 LYS CB C 13 32.75 0.2 . 1 . . . . . . . . 4944 1 22 . 1 1 5 5 THR H H 1 9.89 0.2 . 1 . . . . . . . . 4944 1 23 . 1 1 5 5 THR HA H 1 5.56 0.02 . 1 . . . . . . . . 4944 1 24 . 1 1 5 5 THR C C 13 167.17 0.2 . 1 . . . . . . . . 4944 1 25 . 1 1 5 5 THR CA C 13 62.1 0.2 . 1 . . . . . . . . 4944 1 26 . 1 1 5 5 THR N N 15 119.12 0.2 . 1 . . . . . . . . 4944 1 27 . 1 1 5 5 THR CB C 13 70.2 0.2 . 1 . . . . . . . . 4944 1 28 . 1 1 6 6 ILE H H 1 9.25 0.2 . 1 . . . . . . . . 4944 1 29 . 1 1 6 6 ILE HA H 1 5.46 0.02 . 1 . . . . . . . . 4944 1 30 . 1 1 6 6 ILE C C 13 172.79 0.2 . 1 . . . . . . . . 4944 1 31 . 1 1 6 6 ILE CA C 13 57.01 0.2 . 1 . . . . . . . . 4944 1 32 . 1 1 6 6 ILE N N 15 130.95 0.2 . 1 . . . . . . . . 4944 1 33 . 1 1 6 6 ILE CB C 13 39.83 0.2 . 1 . . . . . . . . 4944 1 34 . 1 1 7 7 TYR H H 1 8.23 0.2 . 1 . . . . . . . . 4944 1 35 . 1 1 7 7 TYR HA H 1 5.31 0.02 . 1 . . . . . . . . 4944 1 36 . 1 1 7 7 TYR C C 13 173.26 0.2 . 1 . . . . . . . . 4944 1 37 . 1 1 7 7 TYR CA C 13 49.95 0.2 . 1 . . . . . . . . 4944 1 38 . 1 1 7 7 TYR N N 15 130.71 0.2 . 1 . . . . . . . . 4944 1 39 . 1 1 7 7 TYR CB C 13 39.33 0.2 . 1 . . . . . . . . 4944 1 40 . 1 1 8 8 PHE H H 1 8.98 0.2 . 1 . . . . . . . . 4944 1 41 . 1 1 8 8 PHE HA H 1 4.98 0.02 . 1 . . . . . . . . 4944 1 42 . 1 1 8 8 PHE CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 43 . 1 1 8 8 PHE N N 15 126.02 0.2 . 1 . . . . . . . . 4944 1 44 . 1 1 8 8 PHE CB C 13 39.83 0.2 . 1 . . . . . . . . 4944 1 45 . 1 1 9 9 ILE H H 1 9.16 0.2 . 1 . . . . . . . . 4944 1 46 . 1 1 9 9 ILE HA H 1 5.56 0.02 . 1 . . . . . . . . 4944 1 47 . 1 1 9 9 ILE CA C 13 57.04 0.2 . 1 . . . . . . . . 4944 1 48 . 1 1 9 9 ILE N N 15 122.08 0.2 . 1 . . . . . . . . 4944 1 49 . 1 1 9 9 ILE CB C 13 39.83 0.2 . 1 . . . . . . . . 4944 1 50 . 1 1 10 10 CYS H H 1 8.51 0.2 . 1 . . . . . . . . 4944 1 51 . 1 1 10 10 CYS HA H 1 4.6 0.02 . 1 . . . . . . . . 4944 1 52 . 1 1 10 10 CYS CA C 13 56.03 0.2 . 1 . . . . . . . . 4944 1 53 . 1 1 10 10 CYS N N 15 127.38 0.2 . 1 . . . . . . . . 4944 1 54 . 1 1 10 10 CYS CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 55 . 1 1 11 11 THR H H 1 8.56 0.2 . 1 . . . . . . . . 4944 1 56 . 1 1 11 11 THR CA C 13 64.63 0.2 . 1 . . . . . . . . 4944 1 57 . 1 1 11 11 THR N N 15 117.03 0.2 . 1 . . . . . . . . 4944 1 58 . 1 1 11 11 THR CB C 13 66.66 0.2 . 1 . . . . . . . . 4944 1 59 . 1 1 12 12 GLY H H 1 8.11 0.2 . 1 . . . . . . . . 4944 1 60 . 1 1 12 12 GLY CA C 13 41.86 0.2 . 1 . . . . . . . . 4944 1 61 . 1 1 12 12 GLY N N 15 110.13 0.2 . 1 . . . . . . . . 4944 1 62 . 1 1 13 13 ASN H H 1 8.06 0.2 . 1 . . . . . . . . 4944 1 63 . 1 1 13 13 ASN CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 64 . 1 1 13 13 ASN N N 15 118.26 0.2 . 1 . . . . . . . . 4944 1 65 . 1 1 13 13 ASN CB C 13 38.82 0.2 . 1 . . . . . . . . 4944 1 66 . 1 1 14 14 SER H H 1 8.61 0.2 . 1 . . . . . . . . 4944 1 67 . 1 1 14 14 SER CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 68 . 1 1 14 14 SER N N 15 117.15 0.2 . 1 . . . . . . . . 4944 1 69 . 1 1 14 14 SER CB C 13 64.63 0.2 . 1 . . . . . . . . 4944 1 70 . 1 1 15 15 CYS H H 1 9.23 0.2 . 1 . . . . . . . . 4944 1 71 . 1 1 15 15 CYS CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 72 . 1 1 15 15 CYS N N 15 120.36 0.2 . 1 . . . . . . . . 4944 1 73 . 1 1 15 15 CYS CB C 13 27.18 0.2 . 1 . . . . . . . . 4944 1 74 . 1 1 16 16 ARG H H 1 10.5 0.2 . 1 . . . . . . . . 4944 1 75 . 1 1 16 16 ARG CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 76 . 1 1 16 16 ARG N N 15 127.13 0.2 . 1 . . . . . . . . 4944 1 77 . 1 1 16 16 ARG CB C 13 30.72 0.2 . 1 . . . . . . . . 4944 1 78 . 1 1 17 17 SER H H 1 9.61 0.2 . 1 . . . . . . . . 4944 1 79 . 1 1 17 17 SER CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 80 . 1 1 17 17 SER N N 15 113.33 0.2 . 1 . . . . . . . . 4944 1 81 . 1 1 17 17 SER CB C 13 60.08 0.2 . 1 . . . . . . . . 4944 1 82 . 1 1 18 18 GLN H H 1 6.04 0.2 . 1 . . . . . . . . 4944 1 83 . 1 1 18 18 GLN HA H 1 4.44 0.02 . 1 . . . . . . . . 4944 1 84 . 1 1 18 18 GLN C C 13 173.26 0.2 . 1 . . . . . . . . 4944 1 85 . 1 1 18 18 GLN CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 86 . 1 1 18 18 GLN N N 15 120.85 0.2 . 1 . . . . . . . . 4944 1 87 . 1 1 18 18 GLN CB C 13 26.17 0.2 . 1 . . . . . . . . 4944 1 88 . 1 1 19 19 MET H H 1 8.27 0.2 . 1 . . . . . . . . 4944 1 89 . 1 1 19 19 MET HA H 1 3.87 0.02 . 1 . . . . . . . . 4944 1 90 . 1 1 19 19 MET C C 13 177.48 0.2 . 1 . . . . . . . . 4944 1 91 . 1 1 19 19 MET CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 92 . 1 1 19 19 MET N N 15 119.49 0.2 . 1 . . . . . . . . 4944 1 93 . 1 1 19 19 MET CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 94 . 1 1 20 20 ALA H H 1 8.38 0.2 . 1 . . . . . . . . 4944 1 95 . 1 1 20 20 ALA HA H 1 3.58 0.02 . 1 . . . . . . . . 4944 1 96 . 1 1 20 20 ALA C C 13 178.42 0.2 . 1 . . . . . . . . 4944 1 97 . 1 1 20 20 ALA CA C 13 54 0.2 . 1 . . . . . . . . 4944 1 98 . 1 1 20 20 ALA N N 15 121.46 0.2 . 1 . . . . . . . . 4944 1 99 . 1 1 20 20 ALA CB C 13 15.03 0.2 . 1 . . . . . . . . 4944 1 100 . 1 1 21 21 GLU H H 1 7.83 0.2 . 1 . . . . . . . . 4944 1 101 . 1 1 21 21 GLU HA H 1 3.88 0.02 . 1 . . . . . . . . 4944 1 102 . 1 1 21 21 GLU C C 13 178.42 0.2 . 1 . . . . . . . . 4944 1 103 . 1 1 21 21 GLU CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 104 . 1 1 21 21 GLU N N 15 119.49 0.2 . 1 . . . . . . . . 4944 1 105 . 1 1 21 21 GLU CB C 13 28.19 0.2 . 1 . . . . . . . . 4944 1 106 . 1 1 22 22 GLY H H 1 8.37 0.2 . 1 . . . . . . . . 4944 1 107 . 1 1 22 22 GLY HA2 H 1 3.83 0.02 . 2 . . . . . . . . 4944 1 108 . 1 1 22 22 GLY HA3 H 1 3.27 0.02 . 2 . . . . . . . . 4944 1 109 . 1 1 22 22 GLY C C 13 174.67 0.2 . 1 . . . . . . . . 4944 1 110 . 1 1 22 22 GLY CA C 13 46.41 0.2 . 1 . . . . . . . . 4944 1 111 . 1 1 22 22 GLY N N 15 105.69 0.2 . 1 . . . . . . . . 4944 1 112 . 1 1 23 23 TRP H H 1 8.92 0.2 . 1 . . . . . . . . 4944 1 113 . 1 1 23 23 TRP HA H 1 4.8 0.02 . 1 . . . . . . . . 4944 1 114 . 1 1 23 23 TRP C C 13 180.06 0.2 . 1 . . . . . . . . 4944 1 115 . 1 1 23 23 TRP CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 116 . 1 1 23 23 TRP N N 15 121.71 0.2 . 1 . . . . . . . . 4944 1 117 . 1 1 23 23 TRP CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 118 . 1 1 24 24 GLY H H 1 9.42 0.2 . 1 . . . . . . . . 4944 1 119 . 1 1 24 24 GLY HA2 H 1 3.72 0.02 . 2 . . . . . . . . 4944 1 120 . 1 1 24 24 GLY HA3 H 1 2.44 0.02 . 2 . . . . . . . . 4944 1 121 . 1 1 24 24 GLY C C 13 173.5 0.2 . 1 . . . . . . . . 4944 1 122 . 1 1 24 24 GLY CA C 13 46.5 0.2 . 1 . . . . . . . . 4944 1 123 . 1 1 24 24 GLY N N 15 109.02 0.2 . 1 . . . . . . . . 4944 1 124 . 1 1 25 25 LYS H H 1 8.36 0.2 . 1 . . . . . . . . 4944 1 125 . 1 1 25 25 LYS HA H 1 4.09 0.02 . 1 . . . . . . . . 4944 1 126 . 1 1 25 25 LYS C C 13 179.12 0.2 . 1 . . . . . . . . 4944 1 127 . 1 1 25 25 LYS CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 128 . 1 1 25 25 LYS N N 15 122.7 0.2 . 1 . . . . . . . . 4944 1 129 . 1 1 25 25 LYS CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 130 . 1 1 26 26 GLU H H 1 7.14 0.2 . 1 . . . . . . . . 4944 1 131 . 1 1 26 26 GLU HA H 1 4.29 0.02 . 1 . . . . . . . . 4944 1 132 . 1 1 26 26 GLU C C 13 178.19 0.2 . 1 . . . . . . . . 4944 1 133 . 1 1 26 26 GLU CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 134 . 1 1 26 26 GLU N N 15 118.88 0.2 . 1 . . . . . . . . 4944 1 135 . 1 1 26 26 GLU CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 136 . 1 1 27 27 ILE H H 1 8.97 0.2 . 1 . . . . . . . . 4944 1 137 . 1 1 27 27 ILE HA H 1 4.03 0.02 . 1 . . . . . . . . 4944 1 138 . 1 1 27 27 ILE C C 13 178.19 0.2 . 1 . . . . . . . . 4944 1 139 . 1 1 27 27 ILE CA C 13 62.58 0.2 . 1 . . . . . . . . 4944 1 140 . 1 1 27 27 ILE N N 15 118.38 0.2 . 1 . . . . . . . . 4944 1 141 . 1 1 27 27 ILE CB C 13 38.82 0.2 . 1 . . . . . . . . 4944 1 142 . 1 1 28 28 LEU H H 1 8.7 0.2 . 1 . . . . . . . . 4944 1 143 . 1 1 28 28 LEU HA H 1 4.43 0.02 . 1 . . . . . . . . 4944 1 144 . 1 1 28 28 LEU C C 13 181.6 0.2 . 1 . . . . . . . . 4944 1 145 . 1 1 28 28 LEU CA C 13 54 0.2 . 1 . . . . . . . . 4944 1 146 . 1 1 28 28 LEU N N 15 117.89 0.2 . 1 . . . . . . . . 4944 1 147 . 1 1 28 28 LEU CB C 13 38.82 0.2 . 1 . . . . . . . . 4944 1 148 . 1 1 29 29 GLY H H 1 7.07 0.2 . 1 . . . . . . . . 4944 1 149 . 1 1 29 29 GLY HA2 H 1 4.22 0.02 . 1 . . . . . . . . 4944 1 150 . 1 1 29 29 GLY HA3 H 1 4.22 0.02 . 1 . . . . . . . . 4944 1 151 . 1 1 29 29 GLY C C 13 173.26 0.2 . 1 . . . . . . . . 4944 1 152 . 1 1 29 29 GLY CA C 13 45.46 0.2 . 1 . . . . . . . . 4944 1 153 . 1 1 29 29 GLY N N 15 105.69 0.2 . 1 . . . . . . . . 4944 1 154 . 1 1 30 30 GLU H H 1 8.49 0.2 . 1 . . . . . . . . 4944 1 155 . 1 1 30 30 GLU HA H 1 4.21 0.02 . 1 . . . . . . . . 4944 1 156 . 1 1 30 30 GLU C C 13 177.48 0.2 . 1 . . . . . . . . 4944 1 157 . 1 1 30 30 GLU CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 158 . 1 1 30 30 GLU N N 15 119.12 0.2 . 1 . . . . . . . . 4944 1 159 . 1 1 30 30 GLU CB C 13 28.19 0.2 . 1 . . . . . . . . 4944 1 160 . 1 1 31 31 GLY H H 1 8.42 0.2 . 1 . . . . . . . . 4944 1 161 . 1 1 31 31 GLY HA2 H 1 4.32 0.02 . 2 . . . . . . . . 4944 1 162 . 1 1 31 31 GLY HA3 H 1 3.74 0.02 . 2 . . . . . . . . 4944 1 163 . 1 1 31 31 GLY C C 13 171.39 0.2 . 1 . . . . . . . . 4944 1 164 . 1 1 31 31 GLY CA C 13 43.88 0.2 . 1 . . . . . . . . 4944 1 165 . 1 1 31 31 GLY N N 15 106.06 0.2 . 1 . . . . . . . . 4944 1 166 . 1 1 32 32 TRP H H 1 8.04 0.2 . 1 . . . . . . . . 4944 1 167 . 1 1 32 32 TRP HA H 1 5.33 0.02 . 1 . . . . . . . . 4944 1 168 . 1 1 32 32 TRP C C 13 175.14 0.2 . 1 . . . . . . . . 4944 1 169 . 1 1 32 32 TRP CA C 13 55.02 0.2 . 1 . . . . . . . . 4944 1 170 . 1 1 32 32 TRP N N 15 120.97 0.2 . 1 . . . . . . . . 4944 1 171 . 1 1 32 32 TRP CB C 13 30.22 0.2 . 1 . . . . . . . . 4944 1 172 . 1 1 33 33 ASN H H 1 9.9 0.2 . 1 . . . . . . . . 4944 1 173 . 1 1 33 33 ASN HA H 1 4.96 0.02 . 1 . . . . . . . . 4944 1 174 . 1 1 33 33 ASN C C 13 172.09 0.2 . 1 . . . . . . . . 4944 1 175 . 1 1 33 33 ASN CA C 13 51.47 0.2 . 1 . . . . . . . . 4944 1 176 . 1 1 33 33 ASN N N 15 122.2 0.2 . 1 . . . . . . . . 4944 1 177 . 1 1 33 33 ASN CB C 13 38.82 0.2 . 1 . . . . . . . . 4944 1 178 . 1 1 34 34 VAL H H 1 8.27 0.2 . 1 . . . . . . . . 4944 1 179 . 1 1 34 34 VAL HA H 1 4.68 0.02 . 1 . . . . . . . . 4944 1 180 . 1 1 34 34 VAL C C 13 173.5 0.2 . 1 . . . . . . . . 4944 1 181 . 1 1 34 34 VAL CA C 13 59.57 0.2 . 1 . . . . . . . . 4944 1 182 . 1 1 34 34 VAL N N 15 124.67 0.2 . 1 . . . . . . . . 4944 1 183 . 1 1 34 34 VAL CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 184 . 1 1 35 35 TYR H H 1 8.38 0.2 . 1 . . . . . . . . 4944 1 185 . 1 1 35 35 TYR HA H 1 5.12 0.02 . 1 . . . . . . . . 4944 1 186 . 1 1 35 35 TYR C C 13 173.73 0.2 . 1 . . . . . . . . 4944 1 187 . 1 1 35 35 TYR CA C 13 54 0.2 . 1 . . . . . . . . 4944 1 188 . 1 1 35 35 TYR N N 15 125.41 0.2 . 1 . . . . . . . . 4944 1 189 . 1 1 35 35 TYR CB C 13 42.87 0.2 . 1 . . . . . . . . 4944 1 190 . 1 1 36 36 SER H H 1 9.4 0.2 . 1 . . . . . . . . 4944 1 191 . 1 1 36 36 SER HA H 1 6.15 0.02 . 1 . . . . . . . . 4944 1 192 . 1 1 36 36 SER C C 13 171.39 0.2 . 1 . . . . . . . . 4944 1 193 . 1 1 36 36 SER CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 194 . 1 1 36 36 SER N N 15 116.53 0.2 . 1 . . . . . . . . 4944 1 195 . 1 1 36 36 SER CB C 13 67.67 0.2 . 1 . . . . . . . . 4944 1 196 . 1 1 37 37 ALA H H 1 8.87 0.2 . 1 . . . . . . . . 4944 1 197 . 1 1 37 37 ALA HA H 1 3.83 0.02 . 1 . . . . . . . . 4944 1 198 . 1 1 37 37 ALA C C 13 180.1 0.2 . 1 . . . . . . . . 4944 1 199 . 1 1 37 37 ALA CA C 13 50.46 0.2 . 1 . . . . . . . . 4944 1 200 . 1 1 37 37 ALA N N 15 123.07 0.2 . 1 . . . . . . . . 4944 1 201 . 1 1 37 37 ALA CB C 13 23.13 0.2 . 1 . . . . . . . . 4944 1 202 . 1 1 38 38 GLY H H 1 8.62 0.2 . 1 . . . . . . . . 4944 1 203 . 1 1 38 38 GLY HA2 H 1 4.94 0.02 . 2 . . . . . . . . 4944 1 204 . 1 1 38 38 GLY HA3 H 1 3.31 0.02 . 2 . . . . . . . . 4944 1 205 . 1 1 38 38 GLY CA C 13 41.35 0.2 . 1 . . . . . . . . 4944 1 206 . 1 1 38 38 GLY N N 15 104.83 0.2 . 1 . . . . . . . . 4944 1 207 . 1 1 39 39 ILE CA C 13 62.61 0.2 . 1 . . . . . . . . 4944 1 208 . 1 1 39 39 ILE CB C 13 37.3 0.2 . 1 . . . . . . . . 4944 1 209 . 1 1 40 40 GLU H H 1 8.13 0.2 . 1 . . . . . . . . 4944 1 210 . 1 1 40 40 GLU CA C 13 52.99 0.2 . 1 . . . . . . . . 4944 1 211 . 1 1 40 40 GLU N N 15 117.4 0.2 . 1 . . . . . . . . 4944 1 212 . 1 1 40 40 GLU CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 213 . 1 1 41 41 THR H H 1 8 0.2 . 1 . . . . . . . . 4944 1 214 . 1 1 41 41 THR CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 215 . 1 1 41 41 THR N N 15 109.63 0.2 . 1 . . . . . . . . 4944 1 216 . 1 1 41 41 THR CB C 13 69.19 0.2 . 1 . . . . . . . . 4944 1 217 . 1 1 43 43 GLY H H 1 7.54 0.2 . 1 . . . . . . . . 4944 1 218 . 1 1 43 43 GLY HA2 H 1 4.47 0.02 . 2 . . . . . . . . 4944 1 219 . 1 1 43 43 GLY HA3 H 1 3.85 0.02 . 2 . . . . . . . . 4944 1 220 . 1 1 43 43 GLY C C 13 170.92 0.2 . 1 . . . . . . . . 4944 1 221 . 1 1 43 43 GLY CA C 13 43.38 0.2 . 1 . . . . . . . . 4944 1 222 . 1 1 43 43 GLY N N 15 109.26 0.2 . 1 . . . . . . . . 4944 1 223 . 1 1 44 44 VAL H H 1 8.84 0.2 . 1 . . . . . . . . 4944 1 224 . 1 1 44 44 VAL HA H 1 3.82 0.02 . 1 . . . . . . . . 4944 1 225 . 1 1 44 44 VAL C C 13 175.37 0.2 . 1 . . . . . . . . 4944 1 226 . 1 1 44 44 VAL CA C 13 63.12 0.2 . 1 . . . . . . . . 4944 1 227 . 1 1 44 44 VAL N N 15 122.7 0.2 . 1 . . . . . . . . 4944 1 228 . 1 1 44 44 VAL CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 229 . 1 1 45 45 ASN H H 1 8.62 0.2 . 1 . . . . . . . . 4944 1 230 . 1 1 45 45 ASN HA H 1 4.51 0.02 . 1 . . . . . . . . 4944 1 231 . 1 1 45 45 ASN C C 13 174.67 0.2 . 1 . . . . . . . . 4944 1 232 . 1 1 45 45 ASN CA C 13 50.46 0.2 . 1 . . . . . . . . 4944 1 233 . 1 1 45 45 ASN N N 15 131.08 0.2 . 1 . . . . . . . . 4944 1 234 . 1 1 45 45 ASN CB C 13 38.82 0.2 . 1 . . . . . . . . 4944 1 235 . 1 1 46 46 PRO C C 13 180.29 0.2 . 1 . . . . . . . . 4944 1 236 . 1 1 46 46 PRO CA C 13 64.13 0.2 . 1 . . . . . . . . 4944 1 237 . 1 1 46 46 PRO CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 238 . 1 1 47 47 LYS H H 1 8.55 0.2 . 1 . . . . . . . . 4944 1 239 . 1 1 47 47 LYS HA H 1 3.97 0.02 . 1 . . . . . . . . 4944 1 240 . 1 1 47 47 LYS C C 13 180.06 0.2 . 1 . . . . . . . . 4944 1 241 . 1 1 47 47 LYS CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 242 . 1 1 47 47 LYS N N 15 118.14 0.2 . 1 . . . . . . . . 4944 1 243 . 1 1 47 47 LYS CB C 13 30.72 0.2 . 1 . . . . . . . . 4944 1 244 . 1 1 48 48 ALA H H 1 7.84 0.2 . 1 . . . . . . . . 4944 1 245 . 1 1 48 48 ALA HA H 1 4.22 0.02 . 1 . . . . . . . . 4944 1 246 . 1 1 48 48 ALA C C 13 181.48 0.2 . 1 . . . . . . . . 4944 1 247 . 1 1 48 48 ALA CA C 13 53.60 0.2 . 1 . . . . . . . . 4944 1 248 . 1 1 48 48 ALA N N 15 122.57 0.2 . 1 . . . . . . . . 4944 1 249 . 1 1 48 48 ALA CB C 13 17.56 0.2 . 1 . . . . . . . . 4944 1 250 . 1 1 49 49 ILE H H 1 7.25 0.2 . 1 . . . . . . . . 4944 1 251 . 1 1 49 49 ILE HA H 1 3.29 0.02 . 1 . . . . . . . . 4944 1 252 . 1 1 49 49 ILE C C 13 175.84 0.2 . 1 . . . . . . . . 4944 1 253 . 1 1 49 49 ILE CA C 13 64.13 0.2 . 1 . . . . . . . . 4944 1 254 . 1 1 49 49 ILE N N 15 118.51 0.2 . 1 . . . . . . . . 4944 1 255 . 1 1 49 49 ILE CB C 13 36.29 0.2 . 1 . . . . . . . . 4944 1 256 . 1 1 50 50 GLU H H 1 8.09 0.2 . 1 . . . . . . . . 4944 1 257 . 1 1 50 50 GLU HA H 1 3.97 0.02 . 1 . . . . . . . . 4944 1 258 . 1 1 50 50 GLU C C 13 179.82 0.2 . 1 . . . . . . . . 4944 1 259 . 1 1 50 50 GLU CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 260 . 1 1 50 50 GLU N N 15 122.57 0.2 . 1 . . . . . . . . 4944 1 261 . 1 1 50 50 GLU CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 262 . 1 1 51 51 ALA H H 1 8.71 0.2 . 1 . . . . . . . . 4944 1 263 . 1 1 51 51 ALA HA H 1 4.2 0.02 . 1 . . . . . . . . 4944 1 264 . 1 1 51 51 ALA C C 13 181.7 0.2 . 1 . . . . . . . . 4944 1 265 . 1 1 51 51 ALA CA C 13 54.51 0.2 . 1 . . . . . . . . 4944 1 266 . 1 1 51 51 ALA N N 15 123.93 0.2 . 1 . . . . . . . . 4944 1 267 . 1 1 51 51 ALA CB C 13 16.04 0.2 . 1 . . . . . . . . 4944 1 268 . 1 1 52 52 MET H H 1 7.63 0.2 . 1 . . . . . . . . 4944 1 269 . 1 1 52 52 MET HA H 1 4.5 0.02 . 1 . . . . . . . . 4944 1 270 . 1 1 52 52 MET C C 13 178.89 0.2 . 1 . . . . . . . . 4944 1 271 . 1 1 52 52 MET CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 272 . 1 1 52 52 MET N N 15 116.17 0.2 . 1 . . . . . . . . 4944 1 273 . 1 1 52 52 MET CB C 13 27.68 0.2 . 1 . . . . . . . . 4944 1 274 . 1 1 53 53 LYS H H 1 8.13 0.2 . 1 . . . . . . . . 4944 1 275 . 1 1 53 53 LYS HA H 1 3.88 0.02 . 1 . . . . . . . . 4944 1 276 . 1 1 53 53 LYS C C 13 181.47 0.2 . 1 . . . . . . . . 4944 1 277 . 1 1 53 53 LYS CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 278 . 1 1 53 53 LYS N N 15 124.91 0.2 . 1 . . . . . . . . 4944 1 279 . 1 1 53 53 LYS CB C 13 30.68 0.2 . 1 . . . . . . . . 4944 1 280 . 1 1 54 54 GLU H H 1 7.59 0.2 . 1 . . . . . . . . 4944 1 281 . 1 1 54 54 GLU HA H 1 4.15 0.02 . 1 . . . . . . . . 4944 1 282 . 1 1 54 54 GLU C C 13 177.72 0.2 . 1 . . . . . . . . 4944 1 283 . 1 1 54 54 GLU CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 284 . 1 1 54 54 GLU N N 15 119.25 0.2 . 1 . . . . . . . . 4944 1 285 . 1 1 54 54 GLU CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 286 . 1 1 55 55 VAL H H 1 7.17 0.2 . 1 . . . . . . . . 4944 1 287 . 1 1 55 55 VAL HA H 1 4.61 0.02 . 1 . . . . . . . . 4944 1 288 . 1 1 55 55 VAL C C 13 171.62 0.2 . 1 . . . . . . . . 4944 1 289 . 1 1 55 55 VAL CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 290 . 1 1 55 55 VAL N N 15 110.13 0.2 . 1 . . . . . . . . 4944 1 291 . 1 1 55 55 VAL CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 292 . 1 1 56 56 ASP H H 1 7.78 0.2 . 1 . . . . . . . . 4944 1 293 . 1 1 56 56 ASP HA H 1 4.22 0.02 . 1 . . . . . . . . 4944 1 294 . 1 1 56 56 ASP C C 13 173.27 0.2 . 1 . . . . . . . . 4944 1 295 . 1 1 56 56 ASP CA C 13 54.51 0.2 . 1 . . . . . . . . 4944 1 296 . 1 1 56 56 ASP N N 15 115.67 0.2 . 1 . . . . . . . . 4944 1 297 . 1 1 56 56 ASP CB C 13 37.81 0.2 . 1 . . . . . . . . 4944 1 298 . 1 1 57 57 ILE H H 1 7.76 0.2 . 1 . . . . . . . . 4944 1 299 . 1 1 57 57 ILE HA H 1 4.06 0.02 . 1 . . . . . . . . 4944 1 300 . 1 1 57 57 ILE C C 13 172.56 0.2 . 1 . . . . . . . . 4944 1 301 . 1 1 57 57 ILE CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 302 . 1 1 57 57 ILE N N 15 120.11 0.2 . 1 . . . . . . . . 4944 1 303 . 1 1 57 57 ILE CB C 13 37.81 0.2 . 1 . . . . . . . . 4944 1 304 . 1 1 58 58 ASP H H 1 8.82 0.2 . 1 . . . . . . . . 4944 1 305 . 1 1 58 58 ASP HA H 1 4.5 0.02 . 1 . . . . . . . . 4944 1 306 . 1 1 58 58 ASP C C 13 176.78 0.2 . 1 . . . . . . . . 4944 1 307 . 1 1 58 58 ASP CA C 13 51.47 0.2 . 1 . . . . . . . . 4944 1 308 . 1 1 58 58 ASP N N 15 128.49 0.2 . 1 . . . . . . . . 4944 1 309 . 1 1 58 58 ASP CB C 13 39.83 0.2 . 1 . . . . . . . . 4944 1 310 . 1 1 59 59 ILE H H 1 8.32 0.2 . 1 . . . . . . . . 4944 1 311 . 1 1 59 59 ILE HA H 1 4.16 0.02 . 1 . . . . . . . . 4944 1 312 . 1 1 59 59 ILE C C 13 175.84 0.2 . 1 . . . . . . . . 4944 1 313 . 1 1 59 59 ILE CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 314 . 1 1 59 59 ILE N N 15 120.97 0.2 . 1 . . . . . . . . 4944 1 315 . 1 1 59 59 ILE CB C 13 35.28 0.2 . 1 . . . . . . . . 4944 1 316 . 1 1 60 60 SER H H 1 8.71 0.2 . 1 . . . . . . . . 4944 1 317 . 1 1 60 60 SER HA H 1 4.77 0.02 . 1 . . . . . . . . 4944 1 318 . 1 1 60 60 SER C C 13 173.5 0.2 . 1 . . . . . . . . 4944 1 319 . 1 1 60 60 SER CA C 13 60.58 0.2 . 1 . . . . . . . . 4944 1 320 . 1 1 60 60 SER N N 15 120.23 0.2 . 1 . . . . . . . . 4944 1 321 . 1 1 60 60 SER CB C 13 61.6 0.2 . 1 . . . . . . . . 4944 1 322 . 1 1 61 61 ASN H H 1 8.3 0.2 . 1 . . . . . . . . 4944 1 323 . 1 1 61 61 ASN HA H 1 5.05 0.02 . 1 . . . . . . . . 4944 1 324 . 1 1 61 61 ASN C C 13 175.14 0.2 . 1 . . . . . . . . 4944 1 325 . 1 1 61 61 ASN CA C 13 51.47 0.2 . 1 . . . . . . . . 4944 1 326 . 1 1 61 61 ASN N N 15 118.63 0.2 . 1 . . . . . . . . 4944 1 327 . 1 1 61 61 ASN CB C 13 37.3 0.2 . 1 . . . . . . . . 4944 1 328 . 1 1 62 62 HIS H H 1 7.63 0.2 . 1 . . . . . . . . 4944 1 329 . 1 1 62 62 HIS HA H 1 4.65 0.02 . 1 . . . . . . . . 4944 1 330 . 1 1 62 62 HIS C C 13 173.96 0.2 . 1 . . . . . . . . 4944 1 331 . 1 1 62 62 HIS CA C 13 55.02 0.2 . 1 . . . . . . . . 4944 1 332 . 1 1 62 62 HIS N N 15 121.96 0.2 . 1 . . . . . . . . 4944 1 333 . 1 1 62 62 HIS CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 334 . 1 1 63 63 THR H H 1 8.84 0.2 . 1 . . . . . . . . 4944 1 335 . 1 1 63 63 THR HA H 1 4.43 0.02 . 1 . . . . . . . . 4944 1 336 . 1 1 63 63 THR C C 13 172.33 0.2 . 1 . . . . . . . . 4944 1 337 . 1 1 63 63 THR CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 338 . 1 1 63 63 THR N N 15 112.34 0.2 . 1 . . . . . . . . 4944 1 339 . 1 1 63 63 THR CB C 13 68.68 0.2 . 1 . . . . . . . . 4944 1 340 . 1 1 64 64 SER H H 1 8.62 0.2 . 1 . . . . . . . . 4944 1 341 . 1 1 64 64 SER HA H 1 4.8 0.02 . 1 . . . . . . . . 4944 1 342 . 1 1 64 64 SER C C 13 171.39 0.2 . 1 . . . . . . . . 4944 1 343 . 1 1 64 64 SER CA C 13 55.02 0.2 . 1 . . . . . . . . 4944 1 344 . 1 1 64 64 SER N N 15 119.49 0.2 . 1 . . . . . . . . 4944 1 345 . 1 1 64 64 SER CB C 13 62.61 0.2 . 1 . . . . . . . . 4944 1 346 . 1 1 65 65 ASP H H 1 10.28 0.2 . 1 . . . . . . . . 4944 1 347 . 1 1 65 65 ASP HA H 1 5.09 0.02 . 1 . . . . . . . . 4944 1 348 . 1 1 65 65 ASP CA C 13 52.99 0.2 . 1 . . . . . . . . 4944 1 349 . 1 1 65 65 ASP N N 15 132.07 0.2 . 1 . . . . . . . . 4944 1 350 . 1 1 65 65 ASP CB C 13 45.4 0.2 . 1 . . . . . . . . 4944 1 351 . 1 1 66 66 LEU H H 1 8.07 0.2 . 1 . . . . . . . . 4944 1 352 . 1 1 66 66 LEU HA H 1 4.91 0.02 . 1 . . . . . . . . 4944 1 353 . 1 1 66 66 LEU C C 13 179.59 0.2 . 1 . . . . . . . . 4944 1 354 . 1 1 66 66 LEU CA C 13 52.49 0.2 . 1 . . . . . . . . 4944 1 355 . 1 1 66 66 LEU N N 15 121.96 0.2 . 1 . . . . . . . . 4944 1 356 . 1 1 66 66 LEU CB C 13 41.86 0.2 . 1 . . . . . . . . 4944 1 357 . 1 1 67 67 ILE H H 1 7.87 0.2 . 1 . . . . . . . . 4944 1 358 . 1 1 67 67 ILE HA H 1 3.34 0.02 . 1 . . . . . . . . 4944 1 359 . 1 1 67 67 ILE C C 13 173.03 0.2 . 1 . . . . . . . . 4944 1 360 . 1 1 67 67 ILE CA C 13 62.61 0.2 . 1 . . . . . . . . 4944 1 361 . 1 1 67 67 ILE N N 15 122.08 0.2 . 1 . . . . . . . . 4944 1 362 . 1 1 67 67 ILE CB C 13 36.8 0.2 . 1 . . . . . . . . 4944 1 363 . 1 1 68 68 ASP H H 1 8.32 0.2 . 1 . . . . . . . . 4944 1 364 . 1 1 68 68 ASP HA H 1 4.8 0.02 . 1 . . . . . . . . 4944 1 365 . 1 1 68 68 ASP C C 13 176.31 0.2 . 1 . . . . . . . . 4944 1 366 . 1 1 68 68 ASP CA C 13 50.97 0.2 . 1 . . . . . . . . 4944 1 367 . 1 1 68 68 ASP N N 15 130.21 0.2 . 1 . . . . . . . . 4944 1 368 . 1 1 68 68 ASP CB C 13 41.86 0.2 . 1 . . . . . . . . 4944 1 369 . 1 1 69 69 ASN H H 1 9.12 0.2 . 1 . . . . . . . . 4944 1 370 . 1 1 69 69 ASN HA H 1 4.3 0.02 . 1 . . . . . . . . 4944 1 371 . 1 1 69 69 ASN C C 13 177.25 0.2 . 1 . . . . . . . . 4944 1 372 . 1 1 69 69 ASN CA C 13 55.02 0.2 . 1 . . . . . . . . 4944 1 373 . 1 1 69 69 ASN N N 15 127.25 0.2 . 1 . . . . . . . . 4944 1 374 . 1 1 69 69 ASN CB C 13 37.81 0.2 . 1 . . . . . . . . 4944 1 375 . 1 1 70 70 ASP H H 1 8.51 0.2 . 1 . . . . . . . . 4944 1 376 . 1 1 70 70 ASP HA H 1 4.41 0.02 . 1 . . . . . . . . 4944 1 377 . 1 1 70 70 ASP C C 13 179.36 0.2 . 1 . . . . . . . . 4944 1 378 . 1 1 70 70 ASP CA C 13 56.03 0.2 . 1 . . . . . . . . 4944 1 379 . 1 1 70 70 ASP N N 15 120.35 0.2 . 1 . . . . . . . . 4944 1 380 . 1 1 70 70 ASP CB C 13 38.82 0.2 . 1 . . . . . . . . 4944 1 381 . 1 1 71 71 ILE H H 1 7.37 0.2 . 1 . . . . . . . . 4944 1 382 . 1 1 71 71 ILE HA H 1 3.35 0.02 . 1 . . . . . . . . 4944 1 383 . 1 1 71 71 ILE C C 13 181 0.2 . 1 . . . . . . . . 4944 1 384 . 1 1 71 71 ILE CA C 13 62.61 0.2 . 1 . . . . . . . . 4944 1 385 . 1 1 71 71 ILE N N 15 122.08 0.2 . 1 . . . . . . . . 4944 1 386 . 1 1 71 71 ILE CB C 13 35.28 0.2 . 1 . . . . . . . . 4944 1 387 . 1 1 72 72 LEU H H 1 8.14 0.2 . 1 . . . . . . . . 4944 1 388 . 1 1 72 72 LEU HA H 1 3.88 0.02 . 1 . . . . . . . . 4944 1 389 . 1 1 72 72 LEU C C 13 179.83 0.2 . 1 . . . . . . . . 4944 1 390 . 1 1 72 72 LEU CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 391 . 1 1 72 72 LEU N N 15 122.94 0.2 . 1 . . . . . . . . 4944 1 392 . 1 1 72 72 LEU CB C 13 41.35 0.2 . 1 . . . . . . . . 4944 1 393 . 1 1 73 73 LYS H H 1 7.42 0.2 . 1 . . . . . . . . 4944 1 394 . 1 1 73 73 LYS HA H 1 3.98 0.02 . 1 . . . . . . . . 4944 1 395 . 1 1 73 73 LYS C C 13 177.01 0.2 . 1 . . . . . . . . 4944 1 396 . 1 1 73 73 LYS CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 397 . 1 1 73 73 LYS N N 15 113.33 0.2 . 1 . . . . . . . . 4944 1 398 . 1 1 73 73 LYS CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 399 . 1 1 74 74 GLN H H 1 7.18 0.2 . 1 . . . . . . . . 4944 1 400 . 1 1 74 74 GLN HA H 1 4.33 0.02 . 1 . . . . . . . . 4944 1 401 . 1 1 74 74 GLN C C 13 175.61 0.2 . 1 . . . . . . . . 4944 1 402 . 1 1 74 74 GLN CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 403 . 1 1 74 74 GLN N N 15 117.03 0.2 . 1 . . . . . . . . 4944 1 404 . 1 1 74 74 GLN CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 405 . 1 1 75 75 SER H H 1 7.32 0.2 . 1 . . . . . . . . 4944 1 406 . 1 1 75 75 SER HA H 1 3.94 0.02 . 1 . . . . . . . . 4944 1 407 . 1 1 75 75 SER C C 13 171.62 0.2 . 1 . . . . . . . . 4944 1 408 . 1 1 75 75 SER CA C 13 60.58 0.2 . 1 . . . . . . . . 4944 1 409 . 1 1 75 75 SER N N 15 118.38 0.2 . 1 . . . . . . . . 4944 1 410 . 1 1 75 75 SER CB C 13 62.6 0.2 . 1 . . . . . . . . 4944 1 411 . 1 1 76 76 ASP H H 1 9.12 0.2 . 1 . . . . . . . . 4944 1 412 . 1 1 76 76 ASP HA H 1 4.66 0.02 . 1 . . . . . . . . 4944 1 413 . 1 1 76 76 ASP C C 13 175.84 0.2 . 1 . . . . . . . . 4944 1 414 . 1 1 76 76 ASP CA C 13 55.52 0.2 . 1 . . . . . . . . 4944 1 415 . 1 1 76 76 ASP N N 15 123.81 0.2 . 1 . . . . . . . . 4944 1 416 . 1 1 76 76 ASP CB C 13 41.35 0.2 . 1 . . . . . . . . 4944 1 417 . 1 1 77 77 LEU H H 1 7.8 0.2 . 1 . . . . . . . . 4944 1 418 . 1 1 77 77 LEU HA H 1 4.41 0.02 . 1 . . . . . . . . 4944 1 419 . 1 1 77 77 LEU C C 13 171.16 0.2 . 1 . . . . . . . . 4944 1 420 . 1 1 77 77 LEU CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 421 . 1 1 77 77 LEU N N 15 121.59 0.2 . 1 . . . . . . . . 4944 1 422 . 1 1 77 77 LEU CB C 13 44.39 0.2 . 1 . . . . . . . . 4944 1 423 . 1 1 78 78 VAL H H 1 8.82 0.2 . 1 . . . . . . . . 4944 1 424 . 1 1 78 78 VAL HA H 1 4.71 0.02 . 1 . . . . . . . . 4944 1 425 . 1 1 78 78 VAL C C 13 172.09 0.2 . 1 . . . . . . . . 4944 1 426 . 1 1 78 78 VAL CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 427 . 1 1 78 78 VAL N N 15 128.49 0.2 . 1 . . . . . . . . 4944 1 428 . 1 1 78 78 VAL CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 429 . 1 1 79 79 VAL H H 1 8.42 0.2 . 1 . . . . . . . . 4944 1 430 . 1 1 79 79 VAL HA H 1 4.7 0.02 . 1 . . . . . . . . 4944 1 431 . 1 1 79 79 VAL C C 13 176.08 0.2 . 1 . . . . . . . . 4944 1 432 . 1 1 79 79 VAL CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 433 . 1 1 79 79 VAL N N 15 127.74 0.2 . 1 . . . . . . . . 4944 1 434 . 1 1 79 79 VAL CB C 13 32.75 0.2 . 1 . . . . . . . . 4944 1 435 . 1 1 80 80 THR H H 1 8.9 0.2 . 1 . . . . . . . . 4944 1 436 . 1 1 80 80 THR HA H 1 5.31 0.02 . 1 . . . . . . . . 4944 1 437 . 1 1 80 80 THR C C 13 175.84 0.2 . 1 . . . . . . . . 4944 1 438 . 1 1 80 80 THR CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 439 . 1 1 80 80 THR N N 15 117.89 0.2 . 1 . . . . . . . . 4944 1 440 . 1 1 80 80 THR CB C 13 68.18 0.2 . 1 . . . . . . . . 4944 1 441 . 1 1 81 81 LEU H H 1 7.95 0.2 . 1 . . . . . . . . 4944 1 442 . 1 1 81 81 LEU HA H 1 5.8 0.02 . 1 . . . . . . . . 4944 1 443 . 1 1 81 81 LEU CA C 13 55.02 0.2 . 1 . . . . . . . . 4944 1 444 . 1 1 81 81 LEU N N 15 121.59 0.2 . 1 . . . . . . . . 4944 1 445 . 1 1 81 81 LEU CB C 13 43.38 0.2 . 1 . . . . . . . . 4944 1 446 . 1 1 82 82 CYS H H 1 7.63 0.2 . 1 . . . . . . . . 4944 1 447 . 1 1 82 82 CYS HA H 1 4.46 0.02 . 1 . . . . . . . . 4944 1 448 . 1 1 82 82 CYS C C 13 171.86 0.2 . 1 . . . . . . . . 4944 1 449 . 1 1 82 82 CYS CA C 13 56.03 0.2 . 1 . . . . . . . . 4944 1 450 . 1 1 82 82 CYS N N 15 107.54 0.2 . 1 . . . . . . . . 4944 1 451 . 1 1 82 82 CYS CB C 13 29.71 0.2 . 1 . . . . . . . . 4944 1 452 . 1 1 83 83 SER HA H 1 4.54 0.02 . 1 . . . . . . . . 4944 1 453 . 1 1 83 83 SER C C 13 175.61 0.2 . 1 . . . . . . . . 4944 1 454 . 1 1 83 83 SER CA C 13 61.6 0.2 . 1 . . . . . . . . 4944 1 455 . 1 1 83 83 SER CB C 13 61.6 0.2 . 1 . . . . . . . . 4944 1 456 . 1 1 84 84 ASP H H 1 8.74 0.2 . 1 . . . . . . . . 4944 1 457 . 1 1 84 84 ASP HA H 1 4.4 0.02 . 1 . . . . . . . . 4944 1 458 . 1 1 84 84 ASP C C 13 176.08 0.2 . 1 . . . . . . . . 4944 1 459 . 1 1 84 84 ASP CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 460 . 1 1 84 84 ASP N N 15 122.7 0.2 . 1 . . . . . . . . 4944 1 461 . 1 1 84 84 ASP CB C 13 39.83 0.2 . 1 . . . . . . . . 4944 1 462 . 1 1 85 85 ALA H H 1 7.58 0.2 . 1 . . . . . . . . 4944 1 463 . 1 1 85 85 ALA HA H 1 4.22 0.02 . 1 . . . . . . . . 4944 1 464 . 1 1 85 85 ALA C C 13 177.95 0.2 . 1 . . . . . . . . 4944 1 465 . 1 1 85 85 ALA CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 466 . 1 1 85 85 ALA N N 15 122.08 0.2 . 1 . . . . . . . . 4944 1 467 . 1 1 85 85 ALA CB C 13 17.56 0.2 . 1 . . . . . . . . 4944 1 468 . 1 1 86 86 ASP H H 1 7.91 0.2 . 1 . . . . . . . . 4944 1 469 . 1 1 86 86 ASP HA H 1 4.38 0.02 . 1 . . . . . . . . 4944 1 470 . 1 1 86 86 ASP C C 13 175.84 0.2 . 1 . . . . . . . . 4944 1 471 . 1 1 86 86 ASP CA C 13 57.04 0.2 . 1 . . . . . . . . 4944 1 472 . 1 1 86 86 ASP N N 15 118.38 0.2 . 1 . . . . . . . . 4944 1 473 . 1 1 86 86 ASP CB C 13 40.84 0.2 . 1 . . . . . . . . 4944 1 474 . 1 1 87 87 ASN H H 1 8.29 0.2 . 1 . . . . . . . . 4944 1 475 . 1 1 87 87 ASN HA H 1 4.44 0.02 . 1 . . . . . . . . 4944 1 476 . 1 1 87 87 ASN C C 13 173.97 0.2 . 1 . . . . . . . . 4944 1 477 . 1 1 87 87 ASN CA C 13 54 0.2 . 1 . . . . . . . . 4944 1 478 . 1 1 87 87 ASN N N 15 116.29 0.2 . 1 . . . . . . . . 4944 1 479 . 1 1 87 87 ASN CB C 13 37.3 0.2 . 1 . . . . . . . . 4944 1 480 . 1 1 88 88 ASN H H 1 7.51 0.2 . 1 . . . . . . . . 4944 1 481 . 1 1 88 88 ASN HA H 1 4.61 0.02 . 1 . . . . . . . . 4944 1 482 . 1 1 88 88 ASN C C 13 175.37 0.2 . 1 . . . . . . . . 4944 1 483 . 1 1 88 88 ASN CA C 13 52.07 0.2 . 1 . . . . . . . . 4944 1 484 . 1 1 88 88 ASN N N 15 116.78 0.2 . 1 . . . . . . . . 4944 1 485 . 1 1 88 88 ASN CB C 13 38.31 0.2 . 1 . . . . . . . . 4944 1 486 . 1 1 89 89 CYS H H 1 7.16 0.2 . 1 . . . . . . . . 4944 1 487 . 1 1 89 89 CYS HA H 1 4.9 0.02 . 1 . . . . . . . . 4944 1 488 . 1 1 89 89 CYS CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 489 . 1 1 89 89 CYS N N 15 123.93 0.2 . 1 . . . . . . . . 4944 1 490 . 1 1 89 89 CYS CB C 13 26.17 0.2 . 1 . . . . . . . . 4944 1 491 . 1 1 90 90 PRO C C 13 173.5 0.2 . 1 . . . . . . . . 4944 1 492 . 1 1 90 90 PRO CA C 13 61.6 0.2 . 1 . . . . . . . . 4944 1 493 . 1 1 90 90 PRO CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 494 . 1 1 91 91 ILE H H 1 7.99 0.2 . 1 . . . . . . . . 4944 1 495 . 1 1 91 91 ILE HA H 1 3.99 0.02 . 1 . . . . . . . . 4944 1 496 . 1 1 91 91 ILE C C 13 175.37 0.2 . 1 . . . . . . . . 4944 1 497 . 1 1 91 91 ILE CA C 13 58.59 0.2 . 1 . . . . . . . . 4944 1 498 . 1 1 91 91 ILE N N 15 121.34 0.2 . 1 . . . . . . . . 4944 1 499 . 1 1 91 91 ILE CB C 13 34.09 0.2 . 1 . . . . . . . . 4944 1 500 . 1 1 92 92 LEU H H 1 8.28 0.2 . 1 . . . . . . . . 4944 1 501 . 1 1 92 92 LEU HA H 1 4.68 0.02 . 1 . . . . . . . . 4944 1 502 . 1 1 92 92 LEU C C 13 173.03 0.2 . 1 . . . . . . . . 4944 1 503 . 1 1 92 92 LEU CA C 13 50.97 0.2 . 1 . . . . . . . . 4944 1 504 . 1 1 92 92 LEU N N 15 129.47 0.2 . 1 . . . . . . . . 4944 1 505 . 1 1 92 92 LEU CB C 13 40.33 0.2 . 1 . . . . . . . . 4944 1 506 . 1 1 94 94 PRO C C 13 176.31 0.2 . 1 . . . . . . . . 4944 1 507 . 1 1 94 94 PRO CA C 13 63.12 0.2 . 1 . . . . . . . . 4944 1 508 . 1 1 94 94 PRO CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 509 . 1 1 95 95 ASN H H 1 8.36 0.2 . 1 . . . . . . . . 4944 1 510 . 1 1 95 95 ASN HA H 1 4.55 0.02 . 1 . . . . . . . . 4944 1 511 . 1 1 95 95 ASN C C 13 173.5 0.2 . 1 . . . . . . . . 4944 1 512 . 1 1 95 95 ASN CA C 13 52.99 0.2 . 1 . . . . . . . . 4944 1 513 . 1 1 95 95 ASN N N 15 113.58 0.2 . 1 . . . . . . . . 4944 1 514 . 1 1 95 95 ASN CB C 13 36.29 0.2 . 1 . . . . . . . . 4944 1 515 . 1 1 96 96 VAL H H 1 7.42 0.2 . 1 . . . . . . . . 4944 1 516 . 1 1 96 96 VAL HA H 1 4.02 0.02 . 1 . . . . . . . . 4944 1 517 . 1 1 96 96 VAL C C 13 173.97 0.2 . 1 . . . . . . . . 4944 1 518 . 1 1 96 96 VAL CA C 13 62.1 0.2 . 1 . . . . . . . . 4944 1 519 . 1 1 96 96 VAL N N 15 123.44 0.2 . 1 . . . . . . . . 4944 1 520 . 1 1 96 96 VAL CB C 13 31.73 0.2 . 1 . . . . . . . . 4944 1 521 . 1 1 97 97 LYS H H 1 7.56 0.2 . 1 . . . . . . . . 4944 1 522 . 1 1 97 97 LYS HA H 1 4.27 0.02 . 1 . . . . . . . . 4944 1 523 . 1 1 97 97 LYS C C 13 173.5 0.2 . 1 . . . . . . . . 4944 1 524 . 1 1 97 97 LYS CA C 13 54.51 0.2 . 1 . . . . . . . . 4944 1 525 . 1 1 97 97 LYS N N 15 128.86 0.2 . 1 . . . . . . . . 4944 1 526 . 1 1 97 97 LYS CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 527 . 1 1 98 98 LYS H H 1 8.29 0.2 . 1 . . . . . . . . 4944 1 528 . 1 1 98 98 LYS HA H 1 6.03 0.02 . 1 . . . . . . . . 4944 1 529 . 1 1 98 98 LYS C C 13 175.37 0.2 . 1 . . . . . . . . 4944 1 530 . 1 1 98 98 LYS CA C 13 52.99 0.2 . 1 . . . . . . . . 4944 1 531 . 1 1 98 98 LYS N N 15 123.56 0.2 . 1 . . . . . . . . 4944 1 532 . 1 1 98 98 LYS CB C 13 33.76 0.2 . 1 . . . . . . . . 4944 1 533 . 1 1 99 99 GLU H H 1 8.96 0.2 . 1 . . . . . . . . 4944 1 534 . 1 1 99 99 GLU HA H 1 4.5 0.02 . 1 . . . . . . . . 4944 1 535 . 1 1 99 99 GLU C C 13 171.62 0.2 . 1 . . . . . . . . 4944 1 536 . 1 1 99 99 GLU CA C 13 54 0.2 . 1 . . . . . . . . 4944 1 537 . 1 1 99 99 GLU N N 15 126.02 0.2 . 1 . . . . . . . . 4944 1 538 . 1 1 99 99 GLU CB C 13 34.27 0.2 . 1 . . . . . . . . 4944 1 539 . 1 1 100 100 HIS H H 1 8.6 0.2 . 1 . . . . . . . . 4944 1 540 . 1 1 100 100 HIS HA H 1 5.38 0.02 . 1 . . . . . . . . 4944 1 541 . 1 1 100 100 HIS C C 13 172.8 0.2 . 1 . . . . . . . . 4944 1 542 . 1 1 100 100 HIS CA C 13 52.49 0.2 . 1 . . . . . . . . 4944 1 543 . 1 1 100 100 HIS N N 15 121.09 0.2 . 1 . . . . . . . . 4944 1 544 . 1 1 100 100 HIS CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 545 . 1 1 101 101 TRP H H 1 8.41 0.2 . 1 . . . . . . . . 4944 1 546 . 1 1 101 101 TRP HA H 1 4.85 0.02 . 1 . . . . . . . . 4944 1 547 . 1 1 101 101 TRP CA C 13 50.97 0.2 . 1 . . . . . . . . 4944 1 548 . 1 1 101 101 TRP N N 15 132.31 0.2 . 1 . . . . . . . . 4944 1 549 . 1 1 101 101 TRP CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 550 . 1 1 102 102 GLY H H 1 7.35 0.2 . 1 . . . . . . . . 4944 1 551 . 1 1 102 102 GLY HA2 H 1 3.77 0.02 . 2 . . . . . . . . 4944 1 552 . 1 1 102 102 GLY HA3 H 1 3.16 0.02 . 2 . . . . . . . . 4944 1 553 . 1 1 102 102 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4944 1 554 . 1 1 102 102 GLY N N 15 106.06 0.2 . 1 . . . . . . . . 4944 1 555 . 1 1 103 103 PHE H H 1 8.04 0.2 . 1 . . . . . . . . 4944 1 556 . 1 1 103 103 PHE HA H 1 4.7 0.02 . 1 . . . . . . . . 4944 1 557 . 1 1 103 103 PHE C C 13 173.03 0.2 . 1 . . . . . . . . 4944 1 558 . 1 1 103 103 PHE CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 559 . 1 1 103 103 PHE N N 15 121.09 0.2 . 1 . . . . . . . . 4944 1 560 . 1 1 103 103 PHE CB C 13 42.36 0.2 . 1 . . . . . . . . 4944 1 561 . 1 1 104 104 ASP H H 1 9.4 0.2 . 1 . . . . . . . . 4944 1 562 . 1 1 104 104 ASP HA H 1 4.32 0.02 . 1 . . . . . . . . 4944 1 563 . 1 1 104 104 ASP C C 13 176.78 0.2 . 1 . . . . . . . . 4944 1 564 . 1 1 104 104 ASP CA C 13 52.99 0.2 . 1 . . . . . . . . 4944 1 565 . 1 1 104 104 ASP N N 15 127.13 0.2 . 1 . . . . . . . . 4944 1 566 . 1 1 104 104 ASP CB C 13 39.83 0.2 . 1 . . . . . . . . 4944 1 567 . 1 1 105 105 ASP H H 1 8.51 0.2 . 1 . . . . . . . . 4944 1 568 . 1 1 105 105 ASP HA H 1 4.31 0.02 . 1 . . . . . . . . 4944 1 569 . 1 1 105 105 ASP CA C 13 49.45 0.2 . 1 . . . . . . . . 4944 1 570 . 1 1 105 105 ASP N N 15 119.61 0.2 . 1 . . . . . . . . 4944 1 571 . 1 1 105 105 ASP CB C 13 40.84 0.2 . 1 . . . . . . . . 4944 1 572 . 1 1 106 106 PRO C C 13 181 0.2 . 1 . . . . . . . . 4944 1 573 . 1 1 106 106 PRO CA C 13 61.6 0.2 . 1 . . . . . . . . 4944 1 574 . 1 1 106 106 PRO CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 575 . 1 1 107 107 ALA H H 1 7.65 0.2 . 1 . . . . . . . . 4944 1 576 . 1 1 107 107 ALA HA H 1 4.24 0.02 . 1 . . . . . . . . 4944 1 577 . 1 1 107 107 ALA C C 13 172.09 0.2 . 1 . . . . . . . . 4944 1 578 . 1 1 107 107 ALA CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 579 . 1 1 107 107 ALA N N 15 122.2 0.2 . 1 . . . . . . . . 4944 1 580 . 1 1 107 107 ALA CB C 13 17.56 0.2 . 1 . . . . . . . . 4944 1 581 . 1 1 108 108 GLY H H 1 8.92 0.2 . 1 . . . . . . . . 4944 1 582 . 1 1 108 108 GLY HA2 H 1 4.1 0.02 . 2 . . . . . . . . 4944 1 583 . 1 1 108 108 GLY HA3 H 1 3.85 0.02 . 2 . . . . . . . . 4944 1 584 . 1 1 108 108 GLY C C 13 171.39 0.2 . 1 . . . . . . . . 4944 1 585 . 1 1 108 108 GLY CA C 13 44.39 0.2 . 1 . . . . . . . . 4944 1 586 . 1 1 108 108 GLY N N 15 111.36 0.2 . 1 . . . . . . . . 4944 1 587 . 1 1 109 109 LYS H H 1 8.16 0.2 . 1 . . . . . . . . 4944 1 588 . 1 1 109 109 LYS HA H 1 4.64 0.02 . 1 . . . . . . . . 4944 1 589 . 1 1 109 109 LYS C C 13 174.91 0.2 . 1 . . . . . . . . 4944 1 590 . 1 1 109 109 LYS CA C 13 52.99 0.2 . 1 . . . . . . . . 4944 1 591 . 1 1 109 109 LYS N N 15 121.09 0.2 . 1 . . . . . . . . 4944 1 592 . 1 1 109 109 LYS CB C 13 32.24 0.2 . 1 . . . . . . . . 4944 1 593 . 1 1 110 110 GLU H H 1 8.58 0.2 . 1 . . . . . . . . 4944 1 594 . 1 1 110 110 GLU HA H 1 4.39 0.02 . 1 . . . . . . . . 4944 1 595 . 1 1 110 110 GLU C C 13 177.01 0.2 . 1 . . . . . . . . 4944 1 596 . 1 1 110 110 GLU CA C 13 55.02 0.2 . 1 . . . . . . . . 4944 1 597 . 1 1 110 110 GLU N N 15 118.38 0.2 . 1 . . . . . . . . 4944 1 598 . 1 1 110 110 GLU CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 599 . 1 1 111 111 TRP H H 1 8.96 0.2 . 1 . . . . . . . . 4944 1 600 . 1 1 111 111 TRP HA H 1 4.8 0.02 . 1 . . . . . . . . 4944 1 601 . 1 1 111 111 TRP C C 13 177.48 0.2 . 1 . . . . . . . . 4944 1 602 . 1 1 111 111 TRP CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 603 . 1 1 111 111 TRP N N 15 124.42 0.2 . 1 . . . . . . . . 4944 1 604 . 1 1 111 111 TRP CB C 13 29.2 0.2 . 1 . . . . . . . . 4944 1 605 . 1 1 112 112 SER H H 1 8.71 0.2 . 1 . . . . . . . . 4944 1 606 . 1 1 112 112 SER HA H 1 4.43 0.02 . 1 . . . . . . . . 4944 1 607 . 1 1 112 112 SER C C 13 177.95 0.2 . 1 . . . . . . . . 4944 1 608 . 1 1 112 112 SER CA C 13 59.57 0.2 . 1 . . . . . . . . 4944 1 609 . 1 1 112 112 SER N N 15 112.47 0.2 . 1 . . . . . . . . 4944 1 610 . 1 1 112 112 SER CB C 13 61.09 0.2 . 1 . . . . . . . . 4944 1 611 . 1 1 113 113 GLU H H 1 8.06 0.2 . 1 . . . . . . . . 4944 1 612 . 1 1 113 113 GLU HA H 1 4.5 0.02 . 1 . . . . . . . . 4944 1 613 . 1 1 113 113 GLU C C 13 179.36 0.2 . 1 . . . . . . . . 4944 1 614 . 1 1 113 113 GLU CA C 13 56.53 0.2 . 1 . . . . . . . . 4944 1 615 . 1 1 113 113 GLU N N 15 123.81 0.2 . 1 . . . . . . . . 4944 1 616 . 1 1 113 113 GLU CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 617 . 1 1 114 114 PHE H H 1 7.41 0.2 . 1 . . . . . . . . 4944 1 618 . 1 1 114 114 PHE HA H 1 3.45 0.02 . 1 . . . . . . . . 4944 1 619 . 1 1 114 114 PHE C C 13 178.65 0.2 . 1 . . . . . . . . 4944 1 620 . 1 1 114 114 PHE CA C 13 62.1 0.2 . 1 . . . . . . . . 4944 1 621 . 1 1 114 114 PHE N N 15 120.72 0.2 . 1 . . . . . . . . 4944 1 622 . 1 1 114 114 PHE CB C 13 37.81 0.2 . 1 . . . . . . . . 4944 1 623 . 1 1 115 115 GLN H H 1 7.26 0.2 . 1 . . . . . . . . 4944 1 624 . 1 1 115 115 GLN HA H 1 3.2 0.02 . 1 . . . . . . . . 4944 1 625 . 1 1 115 115 GLN C C 13 175.84 0.2 . 1 . . . . . . . . 4944 1 626 . 1 1 115 115 GLN CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 627 . 1 1 115 115 GLN N N 15 116.16 0.2 . 1 . . . . . . . . 4944 1 628 . 1 1 115 115 GLN CB C 13 28.19 0.2 . 1 . . . . . . . . 4944 1 629 . 1 1 116 116 ARG H H 1 8.01 0.2 . 1 . . . . . . . . 4944 1 630 . 1 1 116 116 ARG HA H 1 3.81 0.02 . 1 . . . . . . . . 4944 1 631 . 1 1 116 116 ARG C C 13 179.83 0.2 . 1 . . . . . . . . 4944 1 632 . 1 1 116 116 ARG CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 633 . 1 1 116 116 ARG N N 15 118.88 0.2 . 1 . . . . . . . . 4944 1 634 . 1 1 116 116 ARG CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 635 . 1 1 117 117 VAL H H 1 7.93 0.2 . 1 . . . . . . . . 4944 1 636 . 1 1 117 117 VAL HA H 1 4.19 0.02 . 1 . . . . . . . . 4944 1 637 . 1 1 117 117 VAL C C 13 177.01 0.2 . 1 . . . . . . . . 4944 1 638 . 1 1 117 117 VAL CA C 13 66.15 0.2 . 1 . . . . . . . . 4944 1 639 . 1 1 117 117 VAL N N 15 119.98 0.2 . 1 . . . . . . . . 4944 1 640 . 1 1 117 117 VAL CB C 13 30.72 0.2 . 1 . . . . . . . . 4944 1 641 . 1 1 118 118 ARG H H 1 7.85 0.2 . 1 . . . . . . . . 4944 1 642 . 1 1 118 118 ARG HA H 1 4.06 0.02 . 1 . . . . . . . . 4944 1 643 . 1 1 118 118 ARG C C 13 180.29 0.2 . 1 . . . . . . . . 4944 1 644 . 1 1 118 118 ARG CA C 13 59.57 0.2 . 1 . . . . . . . . 4944 1 645 . 1 1 118 118 ARG N N 15 120.23 0.2 . 1 . . . . . . . . 4944 1 646 . 1 1 118 118 ARG CB C 13 30.2 0.2 . 1 . . . . . . . . 4944 1 647 . 1 1 119 119 ASP H H 1 8.02 0.2 . 1 . . . . . . . . 4944 1 648 . 1 1 119 119 ASP HA H 1 4.6 0.02 . 1 . . . . . . . . 4944 1 649 . 1 1 119 119 ASP C C 13 179.83 0.2 . 1 . . . . . . . . 4944 1 650 . 1 1 119 119 ASP CA C 13 56.03 0.2 . 1 . . . . . . . . 4944 1 651 . 1 1 119 119 ASP N N 15 122.45 0.2 . 1 . . . . . . . . 4944 1 652 . 1 1 119 119 ASP CB C 13 38.31 0.2 . 1 . . . . . . . . 4944 1 653 . 1 1 120 120 GLU H H 1 8.6 0.2 . 1 . . . . . . . . 4944 1 654 . 1 1 120 120 GLU HA H 1 3.98 0.02 . 1 . . . . . . . . 4944 1 655 . 1 1 120 120 GLU C C 13 181.7 0.2 . 1 . . . . . . . . 4944 1 656 . 1 1 120 120 GLU CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 657 . 1 1 120 120 GLU N N 15 126.02 0.2 . 1 . . . . . . . . 4944 1 658 . 1 1 120 120 GLU CB C 13 28.7 0.2 . 1 . . . . . . . . 4944 1 659 . 1 1 121 121 ILE H H 1 8.15 0.2 . 1 . . . . . . . . 4944 1 660 . 1 1 121 121 ILE HA H 1 3.3 0.02 . 1 . . . . . . . . 4944 1 661 . 1 1 121 121 ILE C C 13 176.54 0.2 . 1 . . . . . . . . 4944 1 662 . 1 1 121 121 ILE CA C 13 64.63 0.2 . 1 . . . . . . . . 4944 1 663 . 1 1 121 121 ILE N N 15 123.93 0.2 . 1 . . . . . . . . 4944 1 664 . 1 1 121 121 ILE CB C 13 35.78 0.2 . 1 . . . . . . . . 4944 1 665 . 1 1 122 122 LYS H H 1 7.2 0.2 . 1 . . . . . . . . 4944 1 666 . 1 1 122 122 LYS HA H 1 3.87 0.02 . 1 . . . . . . . . 4944 1 667 . 1 1 122 122 LYS C C 13 177.48 0.2 . 1 . . . . . . . . 4944 1 668 . 1 1 122 122 LYS CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 669 . 1 1 122 122 LYS N N 15 121.22 0.2 . 1 . . . . . . . . 4944 1 670 . 1 1 122 122 LYS CB C 13 31.23 0.2 . 1 . . . . . . . . 4944 1 671 . 1 1 123 123 LEU H H 1 7.17 0.2 . 1 . . . . . . . . 4944 1 672 . 1 1 123 123 LEU HA H 1 3.91 0.02 . 1 . . . . . . . . 4944 1 673 . 1 1 123 123 LEU C C 13 179.36 0.2 . 1 . . . . . . . . 4944 1 674 . 1 1 123 123 LEU CA C 13 56.02 0.2 . 1 . . . . . . . . 4944 1 675 . 1 1 123 123 LEU N N 15 117.77 0.2 . 1 . . . . . . . . 4944 1 676 . 1 1 123 123 LEU CB C 13 40.34 0.2 . 1 . . . . . . . . 4944 1 677 . 1 1 124 124 ALA H H 1 7.61 0.2 . 1 . . . . . . . . 4944 1 678 . 1 1 124 124 ALA HA H 1 3.78 0.02 . 1 . . . . . . . . 4944 1 679 . 1 1 124 124 ALA C C 13 182.4 0.2 . 1 . . . . . . . . 4944 1 680 . 1 1 124 124 ALA CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 681 . 1 1 124 124 ALA N N 15 121.34 0.2 . 1 . . . . . . . . 4944 1 682 . 1 1 124 124 ALA CB C 13 17.06 0.2 . 1 . . . . . . . . 4944 1 683 . 1 1 125 125 ILE H H 1 7.99 0.2 . 1 . . . . . . . . 4944 1 684 . 1 1 125 125 ILE HA H 1 3.76 0.02 . 1 . . . . . . . . 4944 1 685 . 1 1 125 125 ILE C C 13 177.24 0.2 . 1 . . . . . . . . 4944 1 686 . 1 1 125 125 ILE CA C 13 64.13 0.2 . 1 . . . . . . . . 4944 1 687 . 1 1 125 125 ILE N N 15 121.83 0.2 . 1 . . . . . . . . 4944 1 688 . 1 1 125 125 ILE CB C 13 35.78 0.2 . 1 . . . . . . . . 4944 1 689 . 1 1 126 126 GLU H H 1 8.66 0.2 . 1 . . . . . . . . 4944 1 690 . 1 1 126 126 GLU HA H 1 3.81 0.02 . 1 . . . . . . . . 4944 1 691 . 1 1 126 126 GLU C C 13 181 0.2 . 1 . . . . . . . . 4944 1 692 . 1 1 126 126 GLU CA C 13 59.07 0.2 . 1 . . . . . . . . 4944 1 693 . 1 1 126 126 GLU N N 15 122.57 0.2 . 1 . . . . . . . . 4944 1 694 . 1 1 126 126 GLU CB C 13 28.19 0.2 . 1 . . . . . . . . 4944 1 695 . 1 1 127 127 LYS H H 1 8.19 0.2 . 1 . . . . . . . . 4944 1 696 . 1 1 127 127 LYS HA H 1 3.86 0.02 . 1 . . . . . . . . 4944 1 697 . 1 1 127 127 LYS C C 13 181 0.2 . 1 . . . . . . . . 4944 1 698 . 1 1 127 127 LYS CA C 13 58.05 0.2 . 1 . . . . . . . . 4944 1 699 . 1 1 127 127 LYS N N 15 118.51 0.2 . 1 . . . . . . . . 4944 1 700 . 1 1 127 127 LYS CB C 13 30.72 0.2 . 1 . . . . . . . . 4944 1 701 . 1 1 128 128 PHE H H 1 7.79 0.2 . 1 . . . . . . . . 4944 1 702 . 1 1 128 128 PHE HA H 1 4.04 0.02 . 1 . . . . . . . . 4944 1 703 . 1 1 128 128 PHE C C 13 177.48 0.2 . 1 . . . . . . . . 4944 1 704 . 1 1 128 128 PHE CA C 13 60.08 0.2 . 1 . . . . . . . . 4944 1 705 . 1 1 128 128 PHE N N 15 122.94 0.2 . 1 . . . . . . . . 4944 1 706 . 1 1 128 128 PHE CB C 13 38.31 0.2 . 1 . . . . . . . . 4944 1 707 . 1 1 129 129 LYS H H 1 8.04 0.2 . 1 . . . . . . . . 4944 1 708 . 1 1 129 129 LYS HA H 1 4.42 0.02 . 1 . . . . . . . . 4944 1 709 . 1 1 129 129 LYS C C 13 176.55 0.2 . 1 . . . . . . . . 4944 1 710 . 1 1 129 129 LYS CA C 13 57.55 0.2 . 1 . . . . . . . . 4944 1 711 . 1 1 129 129 LYS N N 15 120.97 0.2 . 1 . . . . . . . . 4944 1 712 . 1 1 129 129 LYS CB C 13 31.73 0.2 . 1 . . . . . . . . 4944 1 713 . 1 1 130 130 LEU H H 1 7.04 0.2 . 1 . . . . . . . . 4944 1 714 . 1 1 130 130 LEU HA H 1 4.23 0.02 . 1 . . . . . . . . 4944 1 715 . 1 1 130 130 LEU C C 13 176.55 0.2 . 1 . . . . . . . . 4944 1 716 . 1 1 130 130 LEU CA C 13 53.5 0.2 . 1 . . . . . . . . 4944 1 717 . 1 1 130 130 LEU N N 15 117.4 0.2 . 1 . . . . . . . . 4944 1 718 . 1 1 130 130 LEU CB C 13 41.35 0.2 . 1 . . . . . . . . 4944 1 719 . 1 1 131 131 ARG H H 1 7.17 0.2 . 1 . . . . . . . . 4944 1 720 . 1 1 131 131 ARG HA H 1 3.79 0.02 . 1 . . . . . . . . 4944 1 721 . 1 1 131 131 ARG C C 13 184.51 0.2 . 1 . . . . . . . . 4944 1 722 . 1 1 131 131 ARG CA C 13 58.56 0.2 . 1 . . . . . . . . 4944 1 723 . 1 1 131 131 ARG N N 15 126.39 0.2 . 1 . . . . . . . . 4944 1 724 . 1 1 131 131 ARG CB C 13 29.71 0.2 . 1 . . . . . . . . 4944 1 stop_ save_