data_4554 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4554 _Entry.Title ; Backbone HN, N, Ca, C' and Cb assignments of the 19 kDa DHFR/NADPH complex at 9C and pH 7.6 ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-12-10 _Entry.Accession_date 1999-12-13 _Entry.Last_release_date 2000-04-03 _Entry.Original_release_date 2000-04-03 _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 Eduardo Zaborowski . . . 4554 2 John Chung . . . 4554 3 Gerard Kroon . . . 4554 4 H. Dyson . Jane . 4554 5 Peter Wright . E. . 4554 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4554 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 147 4554 '13C chemical shifts' 449 4554 '15N chemical shifts' 147 4554 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 . . 2000-04-03 1999-12-10 original author . 4554 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4554 _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: Backbone HN, N, Ca, C' and Cb assignments of the 19 kDa DHFR/NADPH complex at 9C and pH 7.6 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of Biomolecular NMR' _Citation.Journal_volume 16 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 349 _Citation.Page_last 350 _Citation.Year 2000 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Eduardo Zaborowski . . . 4554 1 2 John Chung . . . 4554 1 3 Gerard Kroon . . . 4554 1 4 H. Dyson . Jane . 4554 1 5 Peter Wright . E. . 4554 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'dihydrofolate reductase' 4554 1 'cofactor complex' 4554 1 NADPH 4554 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4554 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Hsu, M.C., Ho, Y., Huang, F.Y.(1998) Journal of the Chinese Chemical Society, 45, 115-121. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4554 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 3307916 _Citation.Full_citation ; Fierke, C.A., Johnson, K.A., Benkovic, S.J.(1987) Biochemistry, 26, 4085-4092. ; _Citation.Title 'Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 26 _Citation.Journal_issue 13 _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 4085 _Citation.Page_last 4092 _Citation.Year 1987 _Citation.Details ; A kinetic scheme is presented for Escherichia coli dihydrofolate reductase that predicts steady-state kinetic parameters and full time course kinetics under a variety of substrate concentrations and pHs. This scheme was derived from measuring association and dissociation rate constants and pre-steady-state transients by using stopped-flow fluorescence and absorbance spectroscopy. The binding kinetics suggest that during steady-state turnover product dissociation follows a specific, preferred pathway in which tetrahydrofolate (H4F) dissociation occurs after NADPH replaces NADP+ in the ternary complex. This step, H4F dissociation from the E X NADPH X H4F ternary complex, is proposed to be the rate-limiting step for steady-state turnover at low pH because koff = VM. The rate constant for hydride transfer from NADPH to dihydrofolate (H2F), measured by pre-steady-state transients, has a deuterium isotope effect of 3 and is rapid, khyd = 950 s-1, essentially irreversible, Keq = 1700, and pH dependent, pKa = 6.5, reflecting ionization of a single group in the active site. This scheme accounts for the apparent pKa = 8.4 observed in the steady state as due to a change in the rate-determining step from product release at low pH to hydride transfer above pH 8.4. This kinetic scheme is a necessary background to analyze the effects of single amino acid substitutions on individual rate constants. ; 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 C.A. Fierke C. A. . 4554 3 2 K.A. Johnson K. A. . 4554 3 3 S.J. Benkovic S. J. . 4554 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4554 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9012674 _Citation.Full_citation ; Sawaya, M.R., Kraut, J.(1997) Biochemistry, 36, 586-603. ; _Citation.Title 'Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 36 _Citation.Journal_issue 3 _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 586 _Citation.Page_last 603 _Citation.Year 1997 _Citation.Details ; The reaction catalyzed by Escherichia coli dihydrofolate reductase (ecDHFR) cycles through five detectable kinetic intermediates: holoenzyme, Michaelis complex, ternary product complex, tetrahydrofolate (THF) binary complex, and THF.NADPH complex. Isomorphous crystal structures analogous to these five intermediates and to the transition state (as represented by the methotrexate-NADPH complex) have been used to assemble a 2.1 A resolution movie depicting loop and subdomain movements during the catalytic cycle (see Supporting Information). The structures suggest that the M20 loop is predominantly closed over the reactants in the holoenzyme, Michaelis, and transition state complexes. But, during the remainder of the cycle, when nicotinamide is not bound, the loop occludes (protrudes into) the nicotinamide-ribose binding pocket. Upon changing from the closed to the occluded conformation, the central portion of the loop rearranges from beta-sheet to 3(10) helix. The change may occur by way of an irregularly structured open loop conformation, which could transiently admit a water molecule into position to protonate N5 of dihydrofolate. From the Michaelis to the transition state analogue complex, rotation between two halves of ecDHFR, the adenosine binding subdomain and loop subdomain, closes the (p-aminobenzoyl)glutamate (pABG) binding crevice by approximately 0.5 A. Resulting enhancement of contacts with the pABG moiety may stabilize puckering at C6 of the pteridine ring in the transition state. The subdomain rotation is further adjusted by cofactor-induced movements (approximately 0.5 A) of helices B and C, producing a larger pABG cleft in the THF.NADPH analogue complex than in the THF analogue complex. Such movements may explain how THF release is assisted by NADPH binding. Subdomain rotation is not observed in vertebrate DHFR structures, but an analogous loop movement (residues 59-70) appears to similarly adjust the pABG cleft width, suggesting that these movements are important for catalysis. Loop movement, also unobserved in vertebrate DHFR structures, may preferentially weaken NADP+ vs NADPH binding in ecDHFR, an evolutionary adaptation to reduce product inhibition in the NADP+ rich environment of prokaryotes. ; 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 M.R. Sawaya M. R. . 4554 4 2 J. Kraut J. . . 4554 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4554 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Oppenheimer, N.J.(1982) in The Pyridine Nucleotide Coenzymes (Everse, J., Anderson, B., You, K., Eds), 51-89, Academic Press, New York 36, 586-603. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4554 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Rafter, G.W. and Colowick, S.P. (1957) in Methods in Enzymology, 3, 887-890. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 4554 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8477186 _Citation.Full_citation ; Grzesiek, S. and Bax, A. (1993) J. Biomol. NMR, 3, 185-204. ; _Citation.Title 'Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 3 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 185 _Citation.Page_last 204 _Citation.Year 1993 _Citation.Details ; Experiments and procedures are described that greatly alleviate the sequential assignment process of uniformly 13C/15N-enriched proteins by determining the type of amino acid from experiments that correlate side chain with backbone amide resonances. A recently proposed 3D NMR experiment, CBCA(CO)NH, correlates C alpha and C beta resonances to the backbone amide 1H and 15N resonances of the next residue (Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc., 114, 6291-6293). An extension of this experiment is described which correlates the proton H beta and H alpha resonances to the amide 1H and 15N resonances of the next amino acid, and a detailed product operator description is given. A simple 2D-edited constant-time HSQC experiment is described which rapidly identifies H beta and C beta resonances of aromatic or Asn/Asp residues. The extent to which combined knowledge of the C alpha and C beta chemical shift values determines the amino acid type is investigated, and it is demonstrated that the combined C alpha and C beta chemical shifts of three or four adjacent residues usually are sufficient for defining a unique position in the protein 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 S. Grzesiek S. . . 4554 7 2 A. Bax A. . . 4554 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 4554 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Yamazaki, T., Lee, W., Arrowsmith, C.H., Muhandiram, D.R. and Kay, L.E. (1994) Journal of the American Chemical Society, 116, 11655-11666. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 4554 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7669761 _Citation.Full_citation ; Epstein, D.M., Benkovic, S.J. and Wright, P.E. (1995) Biochemistry, 34, 11037-11048. ; _Citation.Title 'Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 34 _Citation.Journal_issue 35 _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 11037 _Citation.Page_last 11048 _Citation.Year 1995 _Citation.Details ; Backbone and tryptophan side-chain dynamics of uniformly 15N-labeled Escherichia coli dihydrofolate reductase were determined for the binary folate complex. The 15N T1 and T2 relaxation times and [1H]-15N heteronuclear NOEs were measured for 118 protonated backbone nitrogen atoms. The generalized order parameter (S2), the effective correlation time for internal motions (tau e), and the contribution to spin-spin relaxation through 15N exchange broadening (Rex) were determined for each residue by model-free analysis. Back-calculation of the relaxation rates for each resonance showed that the calculated dynamical parameters accurately predict the experimental data. Diverse dynamical features were evident in the DHFR backbone. Six sites exhibited order parameters significantly below the weighted mean S2 value (for the complex) of 0.81 +/- 0.002: residues G67 and D69 of the adenosine binding domain, and "hinge" residues K38 and V88, exhibited low S2 (0.29 < or = S2 < or = 0.6) and high tau e values (700 ps < or = tau e < or = 2 ns), as did sites within the beta A-alpha B loop and the beta F-beta G loop. Thus, large amplitude backbone motions, on the picosecond and nanosecond time scales, occurred at regions implicated in transition-state stabilization and in ligand-dependent conformational change. Significant Rex values (> or = 1 s-1) were determined for 45% of assigned resonances, many of which arise from residues surrounding the folate binding site. The mean S2 values of the occupied folate binding site and the unoccupied NADPH binding site were similar, indicating the backbone of the latter is at least as conformationally restricted as that of the occupied folate site. We conclude that the observed time-dependent structural fluctuations of the binary complex are in fact associated with catalytic properties of the molecule. ; 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 D.M. Epstein D. M. . 4554 9 2 S.J. Benkovic S. J. . 4554 9 3 P.E. Wright P. E. . 4554 9 stop_ save_ save_ref_9 _Citation.Sf_category citations _Citation.Sf_framecode ref_9 _Citation.Entry_ID 4554 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8019142 _Citation.Full_citation ; Falzone, C.J., Cavanagh, J., Cowart, M., Palmer III, A.G., Matthews, C.R., Benkovic, S.J. and Wright, P.E. (1994) Journal of Biomolecular NMR, 4, 349-366. ; _Citation.Title '1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 4 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 349 _Citation.Page_last 366 _Citation.Year 1994 _Citation.Details ; By using fully 15N- and 15N/13C-labeled Escherichia coli dihydrofolate reductase, the sequence-specific 1H and 15N NMR assignments were achieved for 95% of the backbone resonances and for 90% of the 13C alpha resonances in the binary folate complex. These assignments were made through a variety of three-dimensional proton-detected 15N and 13C experiments. A smaller but significant subset of side-chain 1H and 13C assignments were also determined. In this complex, only one 15N or 13C resonance was detected per 15N or 13C protein nucleus, which indicated a single conformation. Proton-detected 13C experiments were also performed with unlabeled DHFR, complexed with 13C-7/13C-9 folate to probe for multiple conformations of the substrate in its binary complex. As was found for the protein resonances, only a single bound resonance corresponding to a productive conformation could be detected for C-7. These results are consistent with an earlier report based on 1H NMR data [Falzone, C.J. et al. (1990) Biochemistry, 29, 9667-9677] and suggest that the E. coli enzyme is not involved in any catalytically unproductive binding modes in the binary complex. This feature of the E. coli enzyme seems to be unique among the bacterial forms of DHFR that have been studied to date. ; 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 C.J. Falzone C. J. . 4554 10 2 J. Cavanagh J. . . 4554 10 3 M. Cowart M. . . 4554 10 4 A.G. Palmer A. G. 3rd 4554 10 5 C.R. Matthews C. R. . 4554 10 6 S.J. Benkovic S. J. . 4554 10 7 P.E. Wright P. E. . 4554 10 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_DHFR_NADPH _Assembly.Sf_category assembly _Assembly.Sf_framecode DHFR_NADPH _Assembly.Entry_ID 4554 _Assembly.ID 1 _Assembly.Name 'Dihydrofolate reductase complex with NADPH cofactor' _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 1.5.1.3 _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 4554 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 DHFR 1 $DHFR . . . native . . . . . 4554 1 2 NADPH 2 $NDP . . . native . . . . . 4554 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Dihydrofolate reductase complex with NADPH cofactor' system 4554 1 DHFR_NADPH abbreviation 4554 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID reductase 4554 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DHFR _Entity.Sf_category entity _Entity.Sf_framecode DHFR _Entity.Entry_ID 4554 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Dihydrofolate 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 ; MISLIAALAVDRVIGMENAM PWNLPADLAWFKRNTLNKPV IMGRHTWESIGRPLPGRKNI ILSSQPGTDDRVTWVKSVDE AIAACGDVPEIMVIGGGRVY EQFLPKAQKLYLTHIDAEVE GDTHFPDYEPDDWESVFSEF HDADAQNSHSYCFEILERR ; _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 159 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 18200 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 BMRB 11492 . Dihydrofolate_Reductase_from_E._coli . . . . . 100.00 158 99.37 99.37 2.64e-111 . . . . 4554 1 2 no BMRB 25019 . DHFR . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 3 no PDB 1DDR . "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Urea" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 4 no PDB 1DDS . "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 5 no PDB 1DHI . "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" . . . . . 100.00 159 98.74 99.37 2.47e-112 . . . . 4554 1 6 no PDB 1DHJ . "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" . . . . . 100.00 159 98.11 98.74 3.29e-111 . . . . 4554 1 7 no PDB 1DRA . "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" . . . . . 100.00 159 98.74 100.00 1.84e-112 . . . . 4554 1 8 no PDB 1DRB . "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" . . . . . 100.00 159 98.74 99.37 1.01e-111 . . . . 4554 1 9 no PDB 1DRE . "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 10 no PDB 1DRH . "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 11 no PDB 1DYH . "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 12 no PDB 1DYI . "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 13 no PDB 1DYJ . "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 14 no PDB 1JOL . "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 15 no PDB 1JOM . "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 16 no PDB 1RA1 . "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 17 no PDB 1RA2 . "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 18 no PDB 1RA3 . "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 19 no PDB 1RA8 . "Dihydrofolate Reductase Complexed With Folate And 2- Monophosphoadenosine 5'-diphosphoribose" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 20 no PDB 1RA9 . "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 21 no PDB 1RB2 . "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 22 no PDB 1RB3 . "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 23 no PDB 1RC4 . "Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized " . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 24 no PDB 1RD7 . "Dihydrofolate Reductase Complexed With Folate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 25 no PDB 1RE7 . "Dihydrofolate Reductase Complexed With Folate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 26 no PDB 1RF7 . "Structure Of Dihydrofolate Reductase Complexed With Dihydrofolate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 27 no PDB 1RG7 . "Dihydrofolate Reductase Complexed With Methotrexate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 28 no PDB 1RH3 . "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 29 no PDB 1RX1 . "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (reduced Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 30 no PDB 1RX2 . "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 31 no PDB 1RX3 . "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 32 no PDB 1RX4 . "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And 2'-monophosphoadenosine 5'- Diphosphorib" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 33 no PDB 1RX5 . "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 34 no PDB 1RX6 . "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosph" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 35 no PDB 1RX7 . "Structure Of Dihydrofolate Reductase Complexed With Folate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 36 no PDB 1RX8 . "Dihydrofolate Reductase Complexed With Folate And 2'- Monophosphoadenosine 5'-Diphosphoribose" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 37 no PDB 1RX9 . "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 38 no PDB 1TDR . "Expression, Characterization, And Crystallographic Analysis Of Telluromethionyl Dihydrofolate Reductase" . . . . . 100.00 159 98.74 100.00 1.46e-112 . . . . 4554 1 39 no PDB 2ANO . "Crystal Structure Of E.coli Dihydrofolate Reductase In Complex With Nadph And The Inhibitor Ms-sh08-17" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 40 no PDB 2ANQ . "Crystal Structure Of E.coli Dhfr In Complex With Nadph And The Inhibitor Compound 10a." . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 41 no PDB 2DRC . "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" . . . . . 100.00 159 98.74 100.00 4.22e-112 . . . . 4554 1 42 no PDB 2INQ . "Neutron Crystal Structure Of Escherichia Coli Dihydrofolate Reductase Bound To The Anti-Cancer Drug, Methotrexate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 43 no PDB 3DAU . "Crystal Structure Of The Ternary Mtx Nadph Complex Of Escherichia Coli Dihydrofolate Reductase" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 44 no PDB 3DRC . "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 45 no PDB 3K74 . "Disruption Of Protein Dynamics By An Allosteric Effector Antibody" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 46 no PDB 3KFY . "Dynamic Switching And Partial Occupancies Of A Small Molecule Inhibitor Complex Of Dhfr" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 47 no PDB 3OCH . "Chemically Self-Assembled Antibody Nanorings (Csans): Design And Characterization Of An Anti-Cd3 Igm Biomimetic" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 48 no PDB 3QL0 . "Crystal Structure Of N23pp/s148a Mutant Of E. Coli Dihydrofolate Reductase" . . . . . 100.63 160 98.13 98.75 3.90e-110 . . . . 4554 1 49 no PDB 3QL3 . "Re-refined Coordinates For Pdb Entry 1rx2" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 50 no PDB 3QYL . "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 51 no PDB 3QYO . "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 52 no PDB 3R33 . "Evidence For Dynamic Motion In Proteins As A Mechanism For Ligand Dissociation" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 53 no PDB 4DFR . "Crystal Structures Of Escherichia Coli And Lactobacillus Casei Dihydrofolate Reductase Refined At 1.7 Angstroms Resolution. I. " . . . . . 100.00 159 98.74 100.00 1.46e-112 . . . . 4554 1 54 no PDB 4EIG . "Ca1698 Camel Antibody Fragment In Complex With Dhfr" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 55 no PDB 4EIZ . "Structure Of Nb113 Bound To Apodhfr" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 56 no PDB 4EJ1 . "Binding Of Nb113 Camelid Antibody Fragment With The Binary Dhfr:folate Complex" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 57 no PDB 4FHB . "Enhancing Dhfr Catalysis By Binding Of An Allosteric Regulator Nanobody (nb179)" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 58 no PDB 4I13 . "Nanobody Ca1697 Binding To The Dhfr.folate Binary Complex" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 59 no PDB 4I1N . "R104a-ca1697 Nanobody Binding To The Binary Dhfr.folate Complex" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 60 no PDB 4KJJ . "Cryogenic Wt Dhfr" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 61 no PDB 4KJK . "Room Temperature Wt Dhfr" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 62 no PDB 4KJL . "Room Temperature N23pps148a Dhfr" . . . . . 100.63 160 98.13 98.75 3.90e-110 . . . . 4554 1 63 no PDB 4NX6 . "Single Room Temperature Model Of Dhfr" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 64 no PDB 4NX7 . "Single Cryogenic Temperature Model Of Dhfr" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 65 no PDB 4P3Q . "Room-temperature Wt Dhfr, Time-averaged Ensemble" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 66 no PDB 4P3R . "Cryogenic Wt Dhfr, Time-averaged Ensemble" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 67 no PDB 4P66 . "Electrostatics Of Active Site Microenvironments Of E. Coli Dhfr" . . . . . 100.00 159 98.11 98.11 1.26e-110 . . . . 4554 1 68 no PDB 4P68 . "Electrostatics Of Active Site Microenvironments For E. Coli Dhfr" . . . . . 100.00 159 98.11 98.11 1.05e-110 . . . . 4554 1 69 no PDB 4PSS . "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 100k" . . . . . 100.00 159 99.37 99.37 2.24e-112 . . . . 4554 1 70 no PDB 4PST . "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 277 K" . . . . . 100.00 159 99.37 99.37 2.24e-112 . . . . 4554 1 71 no PDB 4PSY . "100k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" . . . . . 100.00 159 99.37 99.37 2.24e-112 . . . . 4554 1 72 no PDB 4PTH . "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 100k" . . . . . 100.00 159 99.37 99.37 2.24e-112 . . . . 4554 1 73 no PDB 4PTJ . "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 277k" . . . . . 100.00 159 99.37 99.37 2.24e-112 . . . . 4554 1 74 no PDB 4QLE . "Crystal Structure Of I14a Dhfr Mutant Complexed With Folate And Nadp+" . . . . . 100.00 159 99.37 99.37 4.16e-113 . . . . 4554 1 75 no PDB 4QLF . "Crystal Structure Of I14g Dhfr Mutant Complexed With Folate And Nadp+" . . . . . 100.00 159 99.37 99.37 1.32e-112 . . . . 4554 1 76 no PDB 4QLG . "Crystal Structure Of I14v Dhfr Mutant Complexed With Folate And Nadp+" . . . . . 100.00 159 99.37 100.00 1.10e-113 . . . . 4554 1 77 no PDB 4RGC . "277k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" . . . . . 100.00 159 99.37 99.37 2.24e-112 . . . . 4554 1 78 no PDB 5CC9 . "L28f E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucleotide" . . . . . 100.00 159 99.37 99.37 2.57e-113 . . . . 4554 1 79 no PDB 5CCC . "Wild-type E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucle" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 80 no PDB 5DFR . "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 81 no PDB 6DFR . "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 82 no PDB 7DFR . "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " . . . . . 100.00 159 99.37 100.00 4.07e-113 . . . . 4554 1 83 no DBJ BAA05974 . "fusion protein, composed of HCV p21 (NS2), E.coli dihydroforate reductase, substrate polypeptide for HCV serine proteinase and " . . . . . 99.37 847 100.00 100.00 1.22e-105 . . . . 4554 1 84 no DBJ BAB33474 . "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 159 99.37 99.37 2.47e-112 . . . . 4554 1 85 no DBJ BAB96616 . "dihydrofolate reductase [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 86 no DBJ BAG75573 . "dihydrofolate reductase [Escherichia coli SE11]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 87 no DBJ BAI23410 . "dihydrofolate reductase [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 88 no EMBL CAA28755 . "unnamed protein product [Escherichia coli]" . . . . . 100.00 159 98.74 99.37 5.37e-112 . . . . 4554 1 89 no EMBL CAD01243 . "dihydrofolate reductase type I [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 159 97.48 98.74 7.29e-112 . . . . 4554 1 90 no EMBL CAP74618 . "Dihydrofolate reductase [Escherichia coli LF82]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 91 no EMBL CAQ30568 . "dihydrofolate reductase [Escherichia coli BL21(DE3)]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 92 no EMBL CAQ87642 . "dihydrofolate reductase [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 93 no GB AAA87976 . "dihydrofolate reductase [Escherichia coli]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 94 no GB AAC73159 . "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 95 no GB AAG54351 . "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 159 99.37 99.37 2.47e-112 . . . . 4554 1 96 no GB AAN41711 . "dihydrofolate reductase type I [Shigella flexneri 2a str. 301]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 97 no GB AAN78554 . "Dihydrofolate reductase [Escherichia coli CFT073]" . . . . . 100.00 204 100.00 100.00 1.02e-113 . . . . 4554 1 98 no PIR AC0513 . "dihydrofolate reductase type I [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 159 97.48 98.74 7.29e-112 . . . . 4554 1 99 no REF NP_308078 . "dihydrofolate reductase [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 159 99.37 99.37 2.47e-112 . . . . 4554 1 100 no REF NP_414590 . "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 101 no REF NP_454699 . "dihydrofolate reductase type I [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 159 97.48 98.74 7.29e-112 . . . . 4554 1 102 no REF NP_706004 . "dihydrofolate reductase [Shigella flexneri 2a str. 301]" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 103 no REF WP_000378105 . "MULTISPECIES: dihydrofolate reductase [Proteobacteria]" . . . . . 100.00 196 100.00 100.00 1.21e-113 . . . . 4554 1 104 no SP P0ABQ4 . "RecName: Full=Dihydrofolate reductase" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 105 no SP P0ABQ5 . "RecName: Full=Dihydrofolate reductase" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 106 no SP P0ABQ6 . "RecName: Full=Dihydrofolate reductase" . . . . . 100.00 159 100.00 100.00 6.63e-114 . . . . 4554 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Dihydrofolate reductase' common 4554 1 DHFR abbreviation 4554 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 . 4554 1 2 . ILE . 4554 1 3 . SER . 4554 1 4 . LEU . 4554 1 5 . ILE . 4554 1 6 . ALA . 4554 1 7 . ALA . 4554 1 8 . LEU . 4554 1 9 . ALA . 4554 1 10 . VAL . 4554 1 11 . ASP . 4554 1 12 . ARG . 4554 1 13 . VAL . 4554 1 14 . ILE . 4554 1 15 . GLY . 4554 1 16 . MET . 4554 1 17 . GLU . 4554 1 18 . ASN . 4554 1 19 . ALA . 4554 1 20 . MET . 4554 1 21 . PRO . 4554 1 22 . TRP . 4554 1 23 . ASN . 4554 1 24 . LEU . 4554 1 25 . PRO . 4554 1 26 . ALA . 4554 1 27 . ASP . 4554 1 28 . LEU . 4554 1 29 . ALA . 4554 1 30 . TRP . 4554 1 31 . PHE . 4554 1 32 . LYS . 4554 1 33 . ARG . 4554 1 34 . ASN . 4554 1 35 . THR . 4554 1 36 . LEU . 4554 1 37 . ASN . 4554 1 38 . LYS . 4554 1 39 . PRO . 4554 1 40 . VAL . 4554 1 41 . ILE . 4554 1 42 . MET . 4554 1 43 . GLY . 4554 1 44 . ARG . 4554 1 45 . HIS . 4554 1 46 . THR . 4554 1 47 . TRP . 4554 1 48 . GLU . 4554 1 49 . SER . 4554 1 50 . ILE . 4554 1 51 . GLY . 4554 1 52 . ARG . 4554 1 53 . PRO . 4554 1 54 . LEU . 4554 1 55 . PRO . 4554 1 56 . GLY . 4554 1 57 . ARG . 4554 1 58 . LYS . 4554 1 59 . ASN . 4554 1 60 . ILE . 4554 1 61 . ILE . 4554 1 62 . LEU . 4554 1 63 . SER . 4554 1 64 . SER . 4554 1 65 . GLN . 4554 1 66 . PRO . 4554 1 67 . GLY . 4554 1 68 . THR . 4554 1 69 . ASP . 4554 1 70 . ASP . 4554 1 71 . ARG . 4554 1 72 . VAL . 4554 1 73 . THR . 4554 1 74 . TRP . 4554 1 75 . VAL . 4554 1 76 . LYS . 4554 1 77 . SER . 4554 1 78 . VAL . 4554 1 79 . ASP . 4554 1 80 . GLU . 4554 1 81 . ALA . 4554 1 82 . ILE . 4554 1 83 . ALA . 4554 1 84 . ALA . 4554 1 85 . CYS . 4554 1 86 . GLY . 4554 1 87 . ASP . 4554 1 88 . VAL . 4554 1 89 . PRO . 4554 1 90 . GLU . 4554 1 91 . ILE . 4554 1 92 . MET . 4554 1 93 . VAL . 4554 1 94 . ILE . 4554 1 95 . GLY . 4554 1 96 . GLY . 4554 1 97 . GLY . 4554 1 98 . ARG . 4554 1 99 . VAL . 4554 1 100 . TYR . 4554 1 101 . GLU . 4554 1 102 . GLN . 4554 1 103 . PHE . 4554 1 104 . LEU . 4554 1 105 . PRO . 4554 1 106 . LYS . 4554 1 107 . ALA . 4554 1 108 . GLN . 4554 1 109 . LYS . 4554 1 110 . LEU . 4554 1 111 . TYR . 4554 1 112 . LEU . 4554 1 113 . THR . 4554 1 114 . HIS . 4554 1 115 . ILE . 4554 1 116 . ASP . 4554 1 117 . ALA . 4554 1 118 . GLU . 4554 1 119 . VAL . 4554 1 120 . GLU . 4554 1 121 . GLY . 4554 1 122 . ASP . 4554 1 123 . THR . 4554 1 124 . HIS . 4554 1 125 . PHE . 4554 1 126 . PRO . 4554 1 127 . ASP . 4554 1 128 . TYR . 4554 1 129 . GLU . 4554 1 130 . PRO . 4554 1 131 . ASP . 4554 1 132 . ASP . 4554 1 133 . TRP . 4554 1 134 . GLU . 4554 1 135 . SER . 4554 1 136 . VAL . 4554 1 137 . PHE . 4554 1 138 . SER . 4554 1 139 . GLU . 4554 1 140 . PHE . 4554 1 141 . HIS . 4554 1 142 . ASP . 4554 1 143 . ALA . 4554 1 144 . ASP . 4554 1 145 . ALA . 4554 1 146 . GLN . 4554 1 147 . ASN . 4554 1 148 . SER . 4554 1 149 . HIS . 4554 1 150 . SER . 4554 1 151 . TYR . 4554 1 152 . CYS . 4554 1 153 . PHE . 4554 1 154 . GLU . 4554 1 155 . ILE . 4554 1 156 . LEU . 4554 1 157 . GLU . 4554 1 158 . ARG . 4554 1 159 . ARG . 4554 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 4554 1 . ILE 2 2 4554 1 . SER 3 3 4554 1 . LEU 4 4 4554 1 . ILE 5 5 4554 1 . ALA 6 6 4554 1 . ALA 7 7 4554 1 . LEU 8 8 4554 1 . ALA 9 9 4554 1 . VAL 10 10 4554 1 . ASP 11 11 4554 1 . ARG 12 12 4554 1 . VAL 13 13 4554 1 . ILE 14 14 4554 1 . GLY 15 15 4554 1 . MET 16 16 4554 1 . GLU 17 17 4554 1 . ASN 18 18 4554 1 . ALA 19 19 4554 1 . MET 20 20 4554 1 . PRO 21 21 4554 1 . TRP 22 22 4554 1 . ASN 23 23 4554 1 . LEU 24 24 4554 1 . PRO 25 25 4554 1 . ALA 26 26 4554 1 . ASP 27 27 4554 1 . LEU 28 28 4554 1 . ALA 29 29 4554 1 . TRP 30 30 4554 1 . PHE 31 31 4554 1 . LYS 32 32 4554 1 . ARG 33 33 4554 1 . ASN 34 34 4554 1 . THR 35 35 4554 1 . LEU 36 36 4554 1 . ASN 37 37 4554 1 . LYS 38 38 4554 1 . PRO 39 39 4554 1 . VAL 40 40 4554 1 . ILE 41 41 4554 1 . MET 42 42 4554 1 . GLY 43 43 4554 1 . ARG 44 44 4554 1 . HIS 45 45 4554 1 . THR 46 46 4554 1 . TRP 47 47 4554 1 . GLU 48 48 4554 1 . SER 49 49 4554 1 . ILE 50 50 4554 1 . GLY 51 51 4554 1 . ARG 52 52 4554 1 . PRO 53 53 4554 1 . LEU 54 54 4554 1 . PRO 55 55 4554 1 . GLY 56 56 4554 1 . ARG 57 57 4554 1 . LYS 58 58 4554 1 . ASN 59 59 4554 1 . ILE 60 60 4554 1 . ILE 61 61 4554 1 . LEU 62 62 4554 1 . SER 63 63 4554 1 . SER 64 64 4554 1 . GLN 65 65 4554 1 . PRO 66 66 4554 1 . GLY 67 67 4554 1 . THR 68 68 4554 1 . ASP 69 69 4554 1 . ASP 70 70 4554 1 . ARG 71 71 4554 1 . VAL 72 72 4554 1 . THR 73 73 4554 1 . TRP 74 74 4554 1 . VAL 75 75 4554 1 . LYS 76 76 4554 1 . SER 77 77 4554 1 . VAL 78 78 4554 1 . ASP 79 79 4554 1 . GLU 80 80 4554 1 . ALA 81 81 4554 1 . ILE 82 82 4554 1 . ALA 83 83 4554 1 . ALA 84 84 4554 1 . CYS 85 85 4554 1 . GLY 86 86 4554 1 . ASP 87 87 4554 1 . VAL 88 88 4554 1 . PRO 89 89 4554 1 . GLU 90 90 4554 1 . ILE 91 91 4554 1 . MET 92 92 4554 1 . VAL 93 93 4554 1 . ILE 94 94 4554 1 . GLY 95 95 4554 1 . GLY 96 96 4554 1 . GLY 97 97 4554 1 . ARG 98 98 4554 1 . VAL 99 99 4554 1 . TYR 100 100 4554 1 . GLU 101 101 4554 1 . GLN 102 102 4554 1 . PHE 103 103 4554 1 . LEU 104 104 4554 1 . PRO 105 105 4554 1 . LYS 106 106 4554 1 . ALA 107 107 4554 1 . GLN 108 108 4554 1 . LYS 109 109 4554 1 . LEU 110 110 4554 1 . TYR 111 111 4554 1 . LEU 112 112 4554 1 . THR 113 113 4554 1 . HIS 114 114 4554 1 . ILE 115 115 4554 1 . ASP 116 116 4554 1 . ALA 117 117 4554 1 . GLU 118 118 4554 1 . VAL 119 119 4554 1 . GLU 120 120 4554 1 . GLY 121 121 4554 1 . ASP 122 122 4554 1 . THR 123 123 4554 1 . HIS 124 124 4554 1 . PHE 125 125 4554 1 . PRO 126 126 4554 1 . ASP 127 127 4554 1 . TYR 128 128 4554 1 . GLU 129 129 4554 1 . PRO 130 130 4554 1 . ASP 131 131 4554 1 . ASP 132 132 4554 1 . TRP 133 133 4554 1 . GLU 134 134 4554 1 . SER 135 135 4554 1 . VAL 136 136 4554 1 . PHE 137 137 4554 1 . SER 138 138 4554 1 . GLU 139 139 4554 1 . PHE 140 140 4554 1 . HIS 141 141 4554 1 . ASP 142 142 4554 1 . ALA 143 143 4554 1 . ASP 144 144 4554 1 . ALA 145 145 4554 1 . GLN 146 146 4554 1 . ASN 147 147 4554 1 . SER 148 148 4554 1 . HIS 149 149 4554 1 . SER 150 150 4554 1 . TYR 151 151 4554 1 . CYS 152 152 4554 1 . PHE 153 153 4554 1 . GLU 154 154 4554 1 . ILE 155 155 4554 1 . LEU 156 156 4554 1 . GLU 157 157 4554 1 . ARG 158 158 4554 1 . ARG 159 159 4554 1 stop_ save_ save_NDP _Entity.Sf_category entity _Entity.Sf_framecode NDP _Entity.Entry_ID 4554 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name NDP _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID NDP _Entity.Nonpolymer_comp_label $chem_comp_NDP _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . NDP . 4554 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4554 _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 $DHFR . 562 . . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli K12 . . . . . . . . . . . . . pET-22b+ . . . . . . 4554 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 4554 _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 $DHFR . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli K12 . . . . . . . . . . . . plasmid . . pET-22b+ . . . . . . 4554 1 2 2 $NDP . vendor . . . . . . . . . . . . . . . . . . . . . . . . Sigma . 'Enzymatically reduced' . . 4554 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_NDP _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_NDP _Chem_comp.Entry_ID 4554 _Chem_comp.ID NDP _Chem_comp.Provenance . _Chem_comp.Name 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code NDP _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code NDP _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C21 H30 N7 O17 P3' _Chem_comp.Formula_weight 745.421 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1DGF _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 09:25:37 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O SMILES_CANONICAL CACTVS 3.341 4554 NDP NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O SMILES CACTVS 3.341 4554 NDP c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4554 NDP c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N SMILES 'OpenEye OEToolkits' 1.5.0 4554 NDP InChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 InChI InChI 1.03 4554 NDP ACFIXJIJDZMPPO-NNYOXOHSSA-N InChIKey InChI 1.03 4554 NDP stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '[[(2R,3S,4R,5R)-5-(3-aminocarbonyl-4H-pyridin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4554 NDP stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID PA . PA . . P . . S 0 . . . . no no . . . . 14.861 . 11.692 . 80.503 . -1.275 0.043 -0.038 1 . 4554 NDP O1A . O1A . . O . . N 0 . . . . no no . . . . 14.841 . 12.028 . 81.946 . -1.710 -1.293 -0.500 2 . 4554 NDP O2A . O2A . . O . . N 0 . . . . no no . . . . 15.549 . 10.473 . 80.008 . -2.565 0.915 0.371 3 . 4554 NDP O5B . O5B . . O . . N 0 . . . . no no . . . . 15.390 . 12.960 . 79.658 . -0.479 0.787 -1.223 4 . 4554 NDP C5B . C5B . . C . . N 0 . . . . no no . . . . 15.048 . 14.291 . 80.053 . -1.385 0.901 -2.322 5 . 4554 NDP C4B . C4B . . C . . R 0 . . . . no no . . . . 15.898 . 15.228 . 79.208 . -0.687 1.603 -3.489 6 . 4554 NDP O4B . O4B . . O . . N 0 . . . . no no . . . . 15.467 . 16.583 . 79.405 . 0.439 0.824 -3.924 7 . 4554 NDP C3B . C3B . . C . . R 0 . . . . no no . . . . 17.372 . 15.169 . 79.595 . -1.654 1.723 -4.682 8 . 4554 NDP O3B . O3B . . O . . N 0 . . . . no no . . . . 18.120 . 14.349 . 78.693 . -1.863 3.094 -5.029 9 . 4554 NDP C2B . C2B . . C . . R 0 . . . . no no . . . . 17.842 . 16.619 . 79.536 . -0.927 0.977 -5.832 10 . 4554 NDP O2B . O2B . . O . . N 0 . . . . no no . . . . 18.974 . 16.882 . 78.682 . -1.073 1.680 -7.068 11 . 4554 NDP C1B . C1B . . C . . R 0 . . . . no no . . . . 16.607 . 17.414 . 79.124 . 0.546 1.001 -5.353 12 . 4554 NDP N9A . N9A . . N . . N 0 . . . . yes no . . . . 16.449 . 18.688 . 79.870 . 1.304 -0.099 -5.954 13 . 4554 NDP C8A . C8A . . C . . N 0 . . . . yes no . . . . 16.645 . 18.917 . 81.183 . 1.388 -1.374 -5.479 14 . 4554 NDP N7A . N7A . . N . . N 0 . . . . yes no . . . . 16.316 . 20.173 . 81.516 . 2.145 -2.090 -6.259 15 . 4554 NDP C5A . C5A . . C . . N 0 . . . . yes no . . . . 15.904 . 20.700 . 80.370 . 2.594 -1.322 -7.280 16 . 4554 NDP C6A . C6A . . C . . N 0 . . . . yes no . . . . 15.427 . 22.002 . 80.198 . 3.422 -1.544 -8.394 17 . 4554 NDP N6A . N6A . . N . . N 0 . . . . no no . . . . 15.438 . 22.917 . 81.172 . 3.976 -2.791 -8.627 18 . 4554 NDP N1A . N1A . . N . . N 0 . . . . yes no . . . . 15.048 . 22.316 . 78.931 . 3.659 -0.530 -9.219 19 . 4554 NDP C2A . C2A . . C . . N 0 . . . . yes no . . . . 15.134 . 21.440 . 77.919 . 3.134 0.662 -9.005 20 . 4554 NDP N3A . N3A . . N . . N 0 . . . . yes no . . . . 15.591 . 20.197 . 78.097 . 2.354 0.916 -7.976 21 . 4554 NDP C4A . C4A . . C . . N 0 . . . . yes no . . . . 15.981 . 19.802 . 79.324 . 2.056 -0.037 -7.100 22 . 4554 NDP O3 . O3 . . O . . N 0 . . . . no no . . . . 13.327 . 11.628 . 80.057 . -0.309 -0.118 1.238 23 . 4554 NDP PN . PN . . P . . S 0 . . . . no no . . . . 12.528 . 11.132 . 78.764 . -1.165 -0.865 2.378 24 . 4554 NDP O1N . O1N . . O . . N 0 . . . . no no . . . . 13.486 . 10.811 . 77.681 . -2.352 -0.049 2.718 25 . 4554 NDP O2N . O2N . . O . . N 0 . . . . no no . . . . 11.586 . 10.083 . 79.201 . -1.640 -2.304 1.835 26 . 4554 NDP O5D . O5D . . O . . N 0 . . . . no no . . . . 11.722 . 12.466 . 78.364 . -0.255 -1.061 3.692 27 . 4554 NDP C5D . C5D . . C . . N 0 . . . . no no . . . . 10.803 . 13.113 . 79.263 . -1.066 -1.726 4.661 28 . 4554 NDP C4D . C4D . . C . . R 0 . . . . no no . . . . 10.675 . 14.572 . 78.840 . -0.257 -1.944 5.941 29 . 4554 NDP O4D . O4D . . O . . N 0 . . . . no no . . . . 11.988 . 15.188 . 78.828 . 0.150 -0.676 6.500 30 . 4554 NDP C3D . C3D . . C . . S 0 . . . . no no . . . . 10.133 . 14.710 . 77.427 . -1.136 -2.592 7.033 31 . 4554 NDP O3D . O3D . . O . . N 0 . . . . no no . . . . 8.701 . 14.684 . 77.373 . -0.916 -4.003 7.081 32 . 4554 NDP C2D . C2D . . C . . R 0 . . . . no no . . . . 10.734 . 16.055 . 77.007 . -0.661 -1.924 8.345 33 . 4554 NDP O2D . O2D . . O . . N 0 . . . . no no . . . . 9.893 . 17.147 . 77.361 . -0.136 -2.903 9.244 34 . 4554 NDP C1D . C1D . . C . . R 0 . . . . no no . . . . 12.058 . 16.172 . 77.760 . 0.446 -0.949 7.887 35 . 4554 NDP N1N . N1N . . N . . N 0 . . . . no no . . . . 13.254 . 15.953 . 76.900 . 0.394 0.286 8.672 36 . 4554 NDP C2N . C2N . . C . . N 0 . . . . no no . . . . 13.460 . 14.684 . 76.332 . 1.485 0.682 9.394 37 . 4554 NDP C3N . C3N . . C . . N 0 . . . . no no . . . . 14.497 . 14.477 . 75.434 . 1.592 1.952 9.826 38 . 4554 NDP C7N . C7N . . C . . N 0 . . . . no no . . . . 14.570 . 13.149 . 74.676 . 2.727 2.334 10.580 39 . 4554 NDP O7N . O7N . . O . . N 0 . . . . no no . . . . 15.195 . 13.084 . 73.617 . 3.594 1.517 10.831 40 . 4554 NDP N7N . N7N . . N . . N 0 . . . . no no . . . . 13.875 . 12.134 . 75.201 . 2.848 3.602 11.019 41 . 4554 NDP C4N . C4N . . C . . N 0 . . . . no no . . . . 15.372 . 15.535 . 75.135 . 0.528 2.970 9.530 42 . 4554 NDP C5N . C5N . . C . . N 0 . . . . no no . . . . 15.197 . 16.797 . 75.724 . -0.737 2.307 9.075 43 . 4554 NDP C6N . C6N . . C . . N 0 . . . . no no . . . . 14.129 . 17.013 . 76.594 . -0.762 1.053 8.683 44 . 4554 NDP P2B . P2B . . P . . N 0 . . . . no no . . . . 20.498 . 16.705 . 79.233 . -1.639 0.622 -8.141 45 . 4554 NDP O1X . O1X . . O . . N 0 . . . . no no . . . . 20.729 . 15.259 . 78.980 . -2.944 0.099 -7.677 46 . 4554 NDP O2X . O2X . . O . . N 0 . . . . no no . . . . 20.487 . 17.102 . 80.666 . -1.829 1.351 -9.564 47 . 4554 NDP O3X . O3X . . O . . N 0 . . . . no no . . . . 21.297 . 17.612 . 78.377 . -0.597 -0.594 -8.296 48 . 4554 NDP HOA2 . HOA2 . . H . . N 0 . . . . no no . . . . 15.561 . 10.257 . 79.082 . -2.238 1.777 0.665 49 . 4554 NDP H51A . H51A . . H . . N 0 . . . . no no . . . . 13.955 . 14.504 . 79.983 . -1.703 -0.093 -2.635 50 . 4554 NDP H52A . H52A . . H . . N 0 . . . . no no . . . . 15.155 . 14.466 . 81.148 . -2.256 1.481 -2.017 51 . 4554 NDP H4B . H4B . . H . . N 0 . . . . no no . . . . 15.777 . 14.903 . 78.148 . -0.355 2.594 -3.179 52 . 4554 NDP H3B . H3B . . H . . N 0 . . . . no no . . . . 17.519 . 14.715 . 80.602 . -2.604 1.239 -4.454 53 . 4554 NDP HO3A . HO3A . . H . . N 0 . . . . no no . . . . 19.038 . 14.312 . 78.934 . -2.317 3.505 -4.281 54 . 4554 NDP H2B . H2B . . H . . N 0 . . . . no no . . . . 18.244 . 16.917 . 80.532 . -1.290 -0.046 -5.924 55 . 4554 NDP H1B . H1B . . H . . N 0 . . . . no no . . . . 16.706 . 17.682 . 78.046 . 1.011 1.958 -5.588 56 . 4554 NDP H8A . H8A . . H . . N 0 . . . . no no . . . . 17.027 . 18.168 . 81.897 . 0.898 -1.737 -4.588 57 . 4554 NDP H61A . H61A . . H . . N 0 . . . . no no . . . . 15.089 . 23.867 . 81.046 . 4.545 -2.932 -9.399 58 . 4554 NDP H62A . H62A . . H . . N 0 . . . . no no . . . . 16.396 . 22.986 . 81.514 . 3.795 -3.524 -8.018 59 . 4554 NDP H2A . H2A . . H . . N 0 . . . . no no . . . . 14.819 . 21.751 . 76.908 . 3.354 1.459 -9.700 60 . 4554 NDP H21N . H21N . . H . . N 0 . . . . no no . . . . 11.111 . 9.788 . 78.433 . -0.838 -2.803 1.626 61 . 4554 NDP H51N . H51N . . H . . N 0 . . . . no no . . . . 9.818 . 12.593 . 79.320 . -1.388 -2.690 4.267 62 . 4554 NDP H52N . H52N . . H . . N 0 . . . . no no . . . . 11.094 . 12.998 . 80.333 . -1.941 -1.115 4.884 63 . 4554 NDP H4D . H4D . . H . . N 0 . . . . no no . . . . 9.980 . 15.056 . 79.565 . 0.614 -2.566 5.737 64 . 4554 NDP H3D . H3D . . H . . N 0 . . . . no no . . . . 10.407 . 13.867 . 76.750 . -2.189 -2.377 6.853 65 . 4554 NDP HO3N . HO3N . . H . . N 0 . . . . no no . . . . 8.362 . 14.770 . 76.489 . -1.489 -4.352 7.777 66 . 4554 NDP H2D . H2D . . H . . N 0 . . . . no no . . . . 10.861 . 16.092 . 75.899 . -1.480 -1.377 8.813 67 . 4554 NDP HO2N . HO2N . . H . . N 0 . . . . no no . . . . 10.265 . 17.981 . 77.100 . -0.857 -3.514 9.444 68 . 4554 NDP H1D . H1D . . H . . N 0 . . . . no no . . . . 12.186 . 17.209 . 78.147 . 1.426 -1.417 7.981 69 . 4554 NDP H2N . H2N . . H . . N 0 . . . . no no . . . . 12.799 . 13.840 . 76.594 . 2.266 -0.028 9.619 70 . 4554 NDP H71N . H71N . . H . . N 0 . . . . no no . . . . 13.357 . 12.187 . 76.078 . 3.626 3.864 11.535 71 . 4554 NDP H72N . H72N . . H . . N 0 . . . . no no . . . . 13.923 . 11.249 . 74.695 . 2.159 4.254 10.815 72 . 4554 NDP H41N . H41N . . H . . N 0 . . . . no no . . . . 16.413 . 15.195 . 75.342 . 0.325 3.556 10.426 73 . 4554 NDP H42N . H42N . . H . . N 0 . . . . no no . . . . 15.393 . 15.667 . 74.028 . 0.888 3.634 8.743 74 . 4554 NDP H5N . H5N . . H . . N 0 . . . . no no . . . . 15.898 . 17.618 . 75.503 . -1.656 2.876 9.075 75 . 4554 NDP H6N . H6N . . H . . N 0 . . . . no no . . . . 13.977 . 18.012 . 77.035 . -1.695 0.614 8.363 76 . 4554 NDP HOP2 . HOP2 . . H . . N 0 . . . . no no . . . . 21.375 . 16.998 . 80.987 . -2.169 0.684 -10.176 77 . 4554 NDP HOP3 . HOP3 . . H . . N 0 . . . . no no . . . . 22.185 . 17.508 . 78.698 . 0.236 -0.211 -8.599 78 . 4554 NDP stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . DOUB PA O1A no N 1 . 4554 NDP 2 . SING PA O2A no N 2 . 4554 NDP 3 . SING PA O5B no N 3 . 4554 NDP 4 . SING PA O3 no N 4 . 4554 NDP 5 . SING O2A HOA2 no N 5 . 4554 NDP 6 . SING O5B C5B no N 6 . 4554 NDP 7 . SING C5B C4B no N 7 . 4554 NDP 8 . SING C5B H51A no N 8 . 4554 NDP 9 . SING C5B H52A no N 9 . 4554 NDP 10 . SING C4B O4B no N 10 . 4554 NDP 11 . SING C4B C3B no N 11 . 4554 NDP 12 . SING C4B H4B no N 12 . 4554 NDP 13 . SING O4B C1B no N 13 . 4554 NDP 14 . SING C3B O3B no N 14 . 4554 NDP 15 . SING C3B C2B no N 15 . 4554 NDP 16 . SING C3B H3B no N 16 . 4554 NDP 17 . SING O3B HO3A no N 17 . 4554 NDP 18 . SING C2B O2B no N 18 . 4554 NDP 19 . SING C2B C1B no N 19 . 4554 NDP 20 . SING C2B H2B no N 20 . 4554 NDP 21 . SING O2B P2B no N 21 . 4554 NDP 22 . SING C1B N9A no N 22 . 4554 NDP 23 . SING C1B H1B no N 23 . 4554 NDP 24 . SING N9A C8A yes N 24 . 4554 NDP 25 . SING N9A C4A yes N 25 . 4554 NDP 26 . DOUB C8A N7A yes N 26 . 4554 NDP 27 . SING C8A H8A no N 27 . 4554 NDP 28 . SING N7A C5A yes N 28 . 4554 NDP 29 . SING C5A C6A yes N 29 . 4554 NDP 30 . DOUB C5A C4A yes N 30 . 4554 NDP 31 . SING C6A N6A no N 31 . 4554 NDP 32 . DOUB C6A N1A yes N 32 . 4554 NDP 33 . SING N6A H61A no N 33 . 4554 NDP 34 . SING N6A H62A no N 34 . 4554 NDP 35 . SING N1A C2A yes N 35 . 4554 NDP 36 . DOUB C2A N3A yes N 36 . 4554 NDP 37 . SING C2A H2A no N 37 . 4554 NDP 38 . SING N3A C4A yes N 38 . 4554 NDP 39 . SING O3 PN no N 39 . 4554 NDP 40 . DOUB PN O1N no N 40 . 4554 NDP 41 . SING PN O2N no N 41 . 4554 NDP 42 . SING PN O5D no N 42 . 4554 NDP 43 . SING O2N H21N no N 43 . 4554 NDP 44 . SING O5D C5D no N 44 . 4554 NDP 45 . SING C5D C4D no N 45 . 4554 NDP 46 . SING C5D H51N no N 46 . 4554 NDP 47 . SING C5D H52N no N 47 . 4554 NDP 48 . SING C4D O4D no N 48 . 4554 NDP 49 . SING C4D C3D no N 49 . 4554 NDP 50 . SING C4D H4D no N 50 . 4554 NDP 51 . SING O4D C1D no N 51 . 4554 NDP 52 . SING C3D O3D no N 52 . 4554 NDP 53 . SING C3D C2D no N 53 . 4554 NDP 54 . SING C3D H3D no N 54 . 4554 NDP 55 . SING O3D HO3N no N 55 . 4554 NDP 56 . SING C2D O2D no N 56 . 4554 NDP 57 . SING C2D C1D no N 57 . 4554 NDP 58 . SING C2D H2D no N 58 . 4554 NDP 59 . SING O2D HO2N no N 59 . 4554 NDP 60 . SING C1D N1N no N 60 . 4554 NDP 61 . SING C1D H1D no N 61 . 4554 NDP 62 . SING N1N C2N no N 62 . 4554 NDP 63 . SING N1N C6N no N 63 . 4554 NDP 64 . DOUB C2N C3N no N 64 . 4554 NDP 65 . SING C2N H2N no N 65 . 4554 NDP 66 . SING C3N C7N no N 66 . 4554 NDP 67 . SING C3N C4N no N 67 . 4554 NDP 68 . DOUB C7N O7N no N 68 . 4554 NDP 69 . SING C7N N7N no N 69 . 4554 NDP 70 . SING N7N H71N no N 70 . 4554 NDP 71 . SING N7N H72N no N 71 . 4554 NDP 72 . SING C4N C5N no N 72 . 4554 NDP 73 . SING C4N H41N no N 73 . 4554 NDP 74 . SING C4N H42N no N 74 . 4554 NDP 75 . DOUB C5N C6N no N 75 . 4554 NDP 76 . SING C5N H5N no N 76 . 4554 NDP 77 . SING C6N H6N no N 77 . 4554 NDP 78 . DOUB P2B O1X no N 78 . 4554 NDP 79 . SING P2B O2X no N 79 . 4554 NDP 80 . SING P2B O3X no N 80 . 4554 NDP 81 . SING O2X HOP2 no N 81 . 4554 NDP 82 . SING O3X HOP3 no N 82 . 4554 NDP stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4554 _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 'Dihydrofolate reductase' '[U-13C; U-15N]' . . 1 $DHFR . . 1.0 . . mM . . . . 4554 1 2 NADPH . . . . . . . 40.0 . . mM . . . . 4554 1 3 'potassium phosphate' . . . . . . . 70.0 . . mM . . . . 4554 1 4 KCl . . . . . . . 25.0 . . mM . . . . 4554 1 5 D2O '[U-99.99% 2H]' . . . . . . 7 . . % . . . . 4554 1 6 NaN3 . . . . . . . 0.02 . . % . . . . 4554 1 7 DTT . . . . . . . 1 . . mM . . . . 4554 1 8 DSS . . . . . . . 20 . . uM . . . . 4554 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4554 _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 'Dihydrofolate reductase' '[U-13C; U-15N; U-2H]' . . 1 $DHFR . . 1.0 . . mM . . . . 4554 2 2 NADPH . . . . . . . 40.0 . . mM . . . . 4554 2 3 'potassium phosphate' . . . . . . . 40.0 . . mM . . . . 4554 2 4 KCl . . . . . . . 25.0 . . mM . . . . 4554 2 5 D2O . . . . . . . 7 . . % . . . . 4554 2 6 NaN3 . . . . . . . 0.02 . . % . . . . 4554 2 7 DTT . . . . . . . 1.0 . . mM . . . . 4554 2 8 DSS . . . . . . . 20.0 . . uM . . . . 4554 2 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 4554 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.6 0.1 n/a 4554 1 temperature 282 0.1 K 4554 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4554 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectrum processing' 4554 1 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 4554 _Software.ID 2 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectrum analysis and assignment' 4554 2 stop_ save_ save_seq_prob _Software.Sf_category software _Software.Sf_framecode seq_prob _Software.Entry_ID 4554 _Software.ID 3 _Software.Name seq_prob _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'sequence specific assignment' 4554 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 7 $ref_6 4554 3 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 4554 _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 4554 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX-II _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 4554 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_4 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_4 _NMR_spectrometer.Entry_ID 4554 _NMR_spectrometer.ID 4 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4554 _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 . . . 4554 1 2 NMR_spectrometer_2 Bruker AMX-II . 500 . . . 4554 1 3 NMR_spectrometer_3 Bruker AMX . 600 . . . 4554 1 4 NMR_spectrometer_4 Bruker DRX . 600 . . . 4554 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 4554 _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 15N-HSQC . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 2 HNCA . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 3 HNCACB . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 4 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 5 HNCO . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 6 HN(CA)CO . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 7 15N-HSQC-NOESY-HSQC . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 8 ddHNCA . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 9 ddHN(CO)CA . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 10 ddHN(CA)CB . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 11 ddHN(CO)CACB . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 1 12 'dd - deuterium decoupled experiments' . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4554 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 4554 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name 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 4554 _NMR_spec_expt.ID 2 _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_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4554 _NMR_spec_expt.ID 3 _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_ 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 4554 _NMR_spec_expt.ID 4 _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_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4554 _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 4554 _NMR_spec_expt.ID 6 _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_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4554 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name 15N-HSQC-NOESY-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_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4554 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name ddHNCA _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 4554 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name ddHN(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_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 4554 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name ddHN(CA)CB _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_11 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_11 _NMR_spec_expt.Entry_ID 4554 _NMR_spec_expt.ID 11 _NMR_spec_expt.Name ddHN(CO)CACB _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_12 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_12 _NMR_spec_expt.Entry_ID 4554 _NMR_spec_expt.ID 12 _NMR_spec_expt.Name 'dd - deuterium decoupled experiments' _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_set_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_set_1 _Chem_shift_reference.Entry_ID 4554 _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 1.0 . . . . . . . . . 4554 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4554 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4554 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_assigned_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4554 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_set_1 _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 15N-HSQC 1 $sample_1 . 4554 1 2 HNCA 1 $sample_1 . 4554 1 3 HNCACB 1 $sample_1 . 4554 1 4 CBCA(CO)NH 1 $sample_1 . 4554 1 5 HNCO 1 $sample_1 . 4554 1 6 HN(CA)CO 1 $sample_1 . 4554 1 7 15N-HSQC-NOESY-HSQC 1 $sample_1 . 4554 1 8 ddHNCA 1 $sample_1 . 4554 1 9 ddHN(CO)CA 1 $sample_1 . 4554 1 10 ddHN(CA)CB 1 $sample_1 . 4554 1 11 ddHN(CO)CACB 1 $sample_1 . 4554 1 12 'dd - deuterium decoupled experiments' 1 $sample_1 . 4554 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 CA C 13 55.509 . . 1 . . . . . . . . 4554 1 2 . 1 1 1 1 MET CB C 13 32.998 . . 1 . . . . . . . . 4554 1 3 . 1 1 2 2 ILE N N 15 124.139 . . 1 . . . . . . . . 4554 1 4 . 1 1 2 2 ILE H H 1 9.428 . . 1 . . . . . . . . 4554 1 5 . 1 1 2 2 ILE CA C 13 61.227 . . 1 . . . . . . . . 4554 1 6 . 1 1 2 2 ILE CB C 13 39.116 . . 1 . . . . . . . . 4554 1 7 . 1 1 2 2 ILE C C 13 174.439 . . 1 . . . . . . . . 4554 1 8 . 1 1 3 3 SER N N 15 125.727 . . 1 . . . . . . . . 4554 1 9 . 1 1 3 3 SER H H 1 9.414 . . 1 . . . . . . . . 4554 1 10 . 1 1 3 3 SER CA C 13 56.372 . . 1 . . . . . . . . 4554 1 11 . 1 1 3 3 SER CB C 13 65.647 . . 1 . . . . . . . . 4554 1 12 . 1 1 3 3 SER C C 13 173.602 . . 1 . . . . . . . . 4554 1 13 . 1 1 4 4 LEU N N 15 121.477 . . 1 . . . . . . . . 4554 1 14 . 1 1 4 4 LEU H H 1 8.503 . . 1 . . . . . . . . 4554 1 15 . 1 1 4 4 LEU CA C 13 53.446 . . 1 . . . . . . . . 4554 1 16 . 1 1 4 4 LEU CB C 13 43.633 . . 1 . . . . . . . . 4554 1 17 . 1 1 4 4 LEU C C 13 175.507 . . 1 . . . . . . . . 4554 1 18 . 1 1 5 5 ILE N N 15 119.082 . . 1 . . . . . . . . 4554 1 19 . 1 1 5 5 ILE H H 1 8.468 . . 1 . . . . . . . . 4554 1 20 . 1 1 5 5 ILE CA C 13 57.940 . . 1 . . . . . . . . 4554 1 21 . 1 1 5 5 ILE CB C 13 41.612 . . 1 . . . . . . . . 4554 1 22 . 1 1 5 5 ILE C C 13 172.998 . . 1 . . . . . . . . 4554 1 23 . 1 1 6 6 ALA N N 15 128.256 . . 1 . . . . . . . . 4554 1 24 . 1 1 6 6 ALA H H 1 8.672 . . 1 . . . . . . . . 4554 1 25 . 1 1 6 6 ALA CA C 13 52.264 . . 1 . . . . . . . . 4554 1 26 . 1 1 6 6 ALA CB C 13 26.631 . . 1 . . . . . . . . 4554 1 27 . 1 1 6 6 ALA C C 13 174.299 . . 1 . . . . . . . . 4554 1 28 . 1 1 7 7 ALA N N 15 127.606 . . 1 . . . . . . . . 4554 1 29 . 1 1 7 7 ALA H H 1 10.408 . . 1 . . . . . . . . 4554 1 30 . 1 1 7 7 ALA CA C 13 50.950 . . 1 . . . . . . . . 4554 1 31 . 1 1 7 7 ALA CB C 13 20.864 . . 1 . . . . . . . . 4554 1 32 . 1 1 7 7 ALA C C 13 174.717 . . 1 . . . . . . . . 4554 1 33 . 1 1 8 8 LEU N N 15 122.570 . . 1 . . . . . . . . 4554 1 34 . 1 1 8 8 LEU H H 1 9.139 . . 1 . . . . . . . . 4554 1 35 . 1 1 8 8 LEU CA C 13 54.017 . . 1 . . . . . . . . 4554 1 36 . 1 1 8 8 LEU CB C 13 45.871 . . 1 . . . . . . . . 4554 1 37 . 1 1 8 8 LEU C C 13 175.972 . . 1 . . . . . . . . 4554 1 38 . 1 1 9 9 ALA N N 15 126.109 . . 1 . . . . . . . . 4554 1 39 . 1 1 9 9 ALA H H 1 8.644 . . 1 . . . . . . . . 4554 1 40 . 1 1 9 9 ALA CA C 13 49.915 . . 1 . . . . . . . . 4554 1 41 . 1 1 9 9 ALA CB C 13 19.396 . . 1 . . . . . . . . 4554 1 42 . 1 1 9 9 ALA C C 13 176.204 . . 1 . . . . . . . . 4554 1 43 . 1 1 10 10 VAL N N 15 117.960 . . 1 . . . . . . . . 4554 1 44 . 1 1 10 10 VAL H H 1 7.636 . . 1 . . . . . . . . 4554 1 45 . 1 1 10 10 VAL CA C 13 65.081 . . 1 . . . . . . . . 4554 1 46 . 1 1 10 10 VAL CB C 13 31.628 . . 1 . . . . . . . . 4554 1 47 . 1 1 10 10 VAL C C 13 177.970 . . 1 . . . . . . . . 4554 1 48 . 1 1 11 11 ASP N N 15 122.427 . . 1 . . . . . . . . 4554 1 49 . 1 1 11 11 ASP H H 1 9.247 . . 1 . . . . . . . . 4554 1 50 . 1 1 11 11 ASP CA C 13 56.037 . . 1 . . . . . . . . 4554 1 51 . 1 1 11 11 ASP CB C 13 38.734 . . 1 . . . . . . . . 4554 1 52 . 1 1 11 11 ASP C C 13 174.903 . . 1 . . . . . . . . 4554 1 53 . 1 1 12 12 ARG N N 15 107.745 . . 1 . . . . . . . . 4554 1 54 . 1 1 12 12 ARG H H 1 8.530 . . 1 . . . . . . . . 4554 1 55 . 1 1 12 12 ARG CA C 13 57.354 . . 1 . . . . . . . . 4554 1 56 . 1 1 12 12 ARG CB C 13 27.627 . . 1 . . . . . . . . 4554 1 57 . 1 1 12 12 ARG C C 13 175.740 . . 1 . . . . . . . . 4554 1 58 . 1 1 13 13 VAL N N 15 120.461 . . 1 . . . . . . . . 4554 1 59 . 1 1 13 13 VAL H H 1 7.100 . . 1 . . . . . . . . 4554 1 60 . 1 1 13 13 VAL CA C 13 66.022 . . 1 . . . . . . . . 4554 1 61 . 1 1 13 13 VAL CB C 13 33.050 . . 1 . . . . . . . . 4554 1 62 . 1 1 14 14 ILE CA C 13 60.770 . . 1 . . . . . . . . 4554 1 63 . 1 1 14 14 ILE CB C 13 41.092 . . 1 . . . . . . . . 4554 1 64 . 1 1 14 14 ILE C C 13 175.577 . . 1 . . . . . . . . 4554 1 65 . 1 1 15 15 GLY N N 15 105.202 . . 1 . . . . . . . . 4554 1 66 . 1 1 15 15 GLY H H 1 7.318 . . 1 . . . . . . . . 4554 1 67 . 1 1 15 15 GLY CA C 13 45.156 . . 1 . . . . . . . . 4554 1 68 . 1 1 15 15 GLY C C 13 170.884 . . 1 . . . . . . . . 4554 1 69 . 1 1 16 16 MET N N 15 119.421 . . 1 . . . . . . . . 4554 1 70 . 1 1 16 16 MET H H 1 8.763 . . 1 . . . . . . . . 4554 1 71 . 1 1 16 16 MET CA C 13 55.335 . . 1 . . . . . . . . 4554 1 72 . 1 1 16 16 MET CB C 13 34.818 . . 1 . . . . . . . . 4554 1 73 . 1 1 17 17 GLU N N 15 130.383 . . 1 . . . . . . . . 4554 1 74 . 1 1 17 17 GLU H H 1 10.204 . . 1 . . . . . . . . 4554 1 75 . 1 1 17 17 GLU CA C 13 57.611 . . 1 . . . . . . . . 4554 1 76 . 1 1 17 17 GLU CB C 13 27.052 . . 1 . . . . . . . . 4554 1 77 . 1 1 17 17 GLU C C 13 175.577 . . 1 . . . . . . . . 4554 1 78 . 1 1 18 18 ASN N N 15 114.761 . . 1 . . . . . . . . 4554 1 79 . 1 1 18 18 ASN H H 1 9.778 . . 1 . . . . . . . . 4554 1 80 . 1 1 18 18 ASN CA C 13 54.293 . . 1 . . . . . . . . 4554 1 81 . 1 1 18 18 ASN CB C 13 38.749 . . 1 . . . . . . . . 4554 1 82 . 1 1 18 18 ASN C C 13 175.577 . . 1 . . . . . . . . 4554 1 83 . 1 1 19 19 ALA N N 15 119.752 . . 1 . . . . . . . . 4554 1 84 . 1 1 19 19 ALA H H 1 7.572 . . 1 . . . . . . . . 4554 1 85 . 1 1 19 19 ALA CA C 13 50.367 . . 1 . . . . . . . . 4554 1 86 . 1 1 19 19 ALA CB C 13 22.174 . . 1 . . . . . . . . 4554 1 87 . 1 1 19 19 ALA C C 13 176.367 . . 1 . . . . . . . . 4554 1 88 . 1 1 20 20 MET N N 15 120.626 . . 1 . . . . . . . . 4554 1 89 . 1 1 20 20 MET H H 1 8.543 . . 1 . . . . . . . . 4554 1 90 . 1 1 20 20 MET CA C 13 52.916 . . 1 . . . . . . . . 4554 1 91 . 1 1 20 20 MET CB C 13 32.114 . . 1 . . . . . . . . 4554 1 92 . 1 1 21 21 PRO CA C 13 62.534 . . 1 . . . . . . . . 4554 1 93 . 1 1 21 21 PRO CB C 13 28.919 . . 1 . . . . . . . . 4554 1 94 . 1 1 21 21 PRO C C 13 173.881 . . 1 . . . . . . . . 4554 1 95 . 1 1 22 22 TRP N N 15 116.084 . . 1 . . . . . . . . 4554 1 96 . 1 1 22 22 TRP H H 1 7.259 . . 1 . . . . . . . . 4554 1 97 . 1 1 22 22 TRP CA C 13 57.283 . . 1 . . . . . . . . 4554 1 98 . 1 1 22 22 TRP CB C 13 29.010 . . 1 . . . . . . . . 4554 1 99 . 1 1 22 22 TRP C C 13 173.649 . . 1 . . . . . . . . 4554 1 100 . 1 1 23 23 ASN N N 15 116.606 . . 1 . . . . . . . . 4554 1 101 . 1 1 23 23 ASN H H 1 8.943 . . 1 . . . . . . . . 4554 1 102 . 1 1 23 23 ASN CA C 13 53.318 . . 1 . . . . . . . . 4554 1 103 . 1 1 23 23 ASN CB C 13 40.188 . . 1 . . . . . . . . 4554 1 104 . 1 1 23 23 ASN C C 13 173.091 . . 1 . . . . . . . . 4554 1 105 . 1 1 24 24 LEU N N 15 126.273 . . 1 . . . . . . . . 4554 1 106 . 1 1 24 24 LEU H H 1 9.394 . . 1 . . . . . . . . 4554 1 107 . 1 1 24 24 LEU CA C 13 51.668 . . 1 . . . . . . . . 4554 1 108 . 1 1 24 24 LEU CB C 13 43.763 . . 1 . . . . . . . . 4554 1 109 . 1 1 25 25 PRO CA C 13 65.319 . . 1 . . . . . . . . 4554 1 110 . 1 1 25 25 PRO CB C 13 31.490 . . 1 . . . . . . . . 4554 1 111 . 1 1 25 25 PRO C C 13 179.294 . . 1 . . . . . . . . 4554 1 112 . 1 1 26 26 ALA N N 15 120.775 . . 1 . . . . . . . . 4554 1 113 . 1 1 26 26 ALA H H 1 9.436 . . 1 . . . . . . . . 4554 1 114 . 1 1 26 26 ALA CA C 13 55.064 . . 1 . . . . . . . . 4554 1 115 . 1 1 26 26 ALA CB C 13 19.304 . . 1 . . . . . . . . 4554 1 116 . 1 1 26 26 ALA C C 13 181.385 . . 1 . . . . . . . . 4554 1 117 . 1 1 27 27 ASP N N 15 117.260 . . 1 . . . . . . . . 4554 1 118 . 1 1 27 27 ASP H H 1 7.740 . . 1 . . . . . . . . 4554 1 119 . 1 1 27 27 ASP CA C 13 57.083 . . 1 . . . . . . . . 4554 1 120 . 1 1 27 27 ASP CB C 13 43.412 . . 1 . . . . . . . . 4554 1 121 . 1 1 27 27 ASP C C 13 177.598 . . 1 . . . . . . . . 4554 1 122 . 1 1 28 28 LEU N N 15 118.610 . . 1 . . . . . . . . 4554 1 123 . 1 1 28 28 LEU H H 1 7.568 . . 1 . . . . . . . . 4554 1 124 . 1 1 28 28 LEU CA C 13 58.210 . . 1 . . . . . . . . 4554 1 125 . 1 1 28 28 LEU CB C 13 40.330 . . 1 . . . . . . . . 4554 1 126 . 1 1 28 28 LEU C C 13 180.316 . . 1 . . . . . . . . 4554 1 127 . 1 1 29 29 ALA N N 15 120.365 . . 1 . . . . . . . . 4554 1 128 . 1 1 29 29 ALA H H 1 7.734 . . 1 . . . . . . . . 4554 1 129 . 1 1 29 29 ALA CA C 13 55.091 . . 1 . . . . . . . . 4554 1 130 . 1 1 29 29 ALA CB C 13 18.052 . . 1 . . . . . . . . 4554 1 131 . 1 1 29 29 ALA C C 13 178.795 . . 1 . . . . . . . . 4554 1 132 . 1 1 30 30 TRP N N 15 123.417 . . 1 . . . . . . . . 4554 1 133 . 1 1 30 30 TRP H H 1 7.308 . . 1 . . . . . . . . 4554 1 134 . 1 1 30 30 TRP CA C 13 59.982 . . 1 . . . . . . . . 4554 1 135 . 1 1 30 30 TRP CB C 13 29.996 . . 1 . . . . . . . . 4554 1 136 . 1 1 30 30 TRP C C 13 177.738 . . 1 . . . . . . . . 4554 1 137 . 1 1 31 31 PHE N N 15 122.806 . . 1 . . . . . . . . 4554 1 138 . 1 1 31 31 PHE H H 1 9.373 . . 1 . . . . . . . . 4554 1 139 . 1 1 31 31 PHE CA C 13 63.312 . . 1 . . . . . . . . 4554 1 140 . 1 1 31 31 PHE CB C 13 38.873 . . 1 . . . . . . . . 4554 1 141 . 1 1 31 31 PHE C C 13 179.526 . . 1 . . . . . . . . 4554 1 142 . 1 1 32 32 LYS N N 15 121.564 . . 1 . . . . . . . . 4554 1 143 . 1 1 32 32 LYS H H 1 8.556 . . 1 . . . . . . . . 4554 1 144 . 1 1 32 32 LYS CA C 13 60.460 . . 1 . . . . . . . . 4554 1 145 . 1 1 32 32 LYS CB C 13 32.522 . . 1 . . . . . . . . 4554 1 146 . 1 1 32 32 LYS C C 13 178.016 . . 1 . . . . . . . . 4554 1 147 . 1 1 33 33 ARG N N 15 116.397 . . 1 . . . . . . . . 4554 1 148 . 1 1 33 33 ARG H H 1 7.884 . . 1 . . . . . . . . 4554 1 149 . 1 1 33 33 ARG CA C 13 58.692 . . 1 . . . . . . . . 4554 1 150 . 1 1 33 33 ARG CB C 13 29.764 . . 1 . . . . . . . . 4554 1 151 . 1 1 33 33 ARG C C 13 178.435 . . 1 . . . . . . . . 4554 1 152 . 1 1 34 34 ASN N N 15 111.439 . . 1 . . . . . . . . 4554 1 153 . 1 1 34 34 ASN H H 1 7.102 . . 1 . . . . . . . . 4554 1 154 . 1 1 34 34 ASN CA C 13 54.505 . . 1 . . . . . . . . 4554 1 155 . 1 1 34 34 ASN CB C 13 39.262 . . 1 . . . . . . . . 4554 1 156 . 1 1 35 35 THR N N 15 106.642 . . 1 . . . . . . . . 4554 1 157 . 1 1 35 35 THR H H 1 7.142 . . 1 . . . . . . . . 4554 1 158 . 1 1 35 35 THR CA C 13 61.829 . . 1 . . . . . . . . 4554 1 159 . 1 1 35 35 THR CB C 13 70.543 . . 1 . . . . . . . . 4554 1 160 . 1 1 35 35 THR C C 13 174.485 . . 1 . . . . . . . . 4554 1 161 . 1 1 36 36 LEU N N 15 124.315 . . 1 . . . . . . . . 4554 1 162 . 1 1 36 36 LEU H H 1 7.183 . . 1 . . . . . . . . 4554 1 163 . 1 1 36 36 LEU CA C 13 57.060 . . 1 . . . . . . . . 4554 1 164 . 1 1 36 36 LEU CB C 13 41.825 . . 1 . . . . . . . . 4554 1 165 . 1 1 36 36 LEU C C 13 173.997 . . 1 . . . . . . . . 4554 1 166 . 1 1 37 37 ASN N N 15 115.771 . . 1 . . . . . . . . 4554 1 167 . 1 1 37 37 ASN H H 1 8.426 . . 1 . . . . . . . . 4554 1 168 . 1 1 37 37 ASN CA C 13 54.693 . . 1 . . . . . . . . 4554 1 169 . 1 1 37 37 ASN CB C 13 37.520 . . 1 . . . . . . . . 4554 1 170 . 1 1 37 37 ASN C C 13 173.382 . . 1 . . . . . . . . 4554 1 171 . 1 1 38 38 LYS N N 15 119.764 . . 1 . . . . . . . . 4554 1 172 . 1 1 38 38 LYS H H 1 7.689 . . 1 . . . . . . . . 4554 1 173 . 1 1 38 38 LYS CA C 13 54.164 . . 1 . . . . . . . . 4554 1 174 . 1 1 38 38 LYS CB C 13 34.506 . . 1 . . . . . . . . 4554 1 175 . 1 1 39 39 PRO CA C 13 62.500 . . 1 . . . . . . . . 4554 1 176 . 1 1 39 39 PRO CB C 13 32.291 . . 1 . . . . . . . . 4554 1 177 . 1 1 39 39 PRO C C 13 175.600 . . 1 . . . . . . . . 4554 1 178 . 1 1 40 40 VAL N N 15 111.645 . . 1 . . . . . . . . 4554 1 179 . 1 1 40 40 VAL H H 1 8.527 . . 1 . . . . . . . . 4554 1 180 . 1 1 40 40 VAL CA C 13 56.588 . . 1 . . . . . . . . 4554 1 181 . 1 1 40 40 VAL CB C 13 34.228 . . 1 . . . . . . . . 4554 1 182 . 1 1 40 40 VAL C C 13 173.718 . . 1 . . . . . . . . 4554 1 183 . 1 1 41 41 ILE N N 15 121.233 . . 1 . . . . . . . . 4554 1 184 . 1 1 41 41 ILE H H 1 8.481 . . 1 . . . . . . . . 4554 1 185 . 1 1 41 41 ILE CA C 13 59.481 . . 1 . . . . . . . . 4554 1 186 . 1 1 41 41 ILE CB C 13 40.676 . . 1 . . . . . . . . 4554 1 187 . 1 1 41 41 ILE C C 13 174.834 . . 1 . . . . . . . . 4554 1 188 . 1 1 42 42 MET N N 15 123.295 . . 1 . . . . . . . . 4554 1 189 . 1 1 42 42 MET H H 1 9.035 . . 1 . . . . . . . . 4554 1 190 . 1 1 42 42 MET CA C 13 52.199 . . 1 . . . . . . . . 4554 1 191 . 1 1 42 42 MET CB C 13 39.636 . . 1 . . . . . . . . 4554 1 192 . 1 1 42 42 MET C C 13 174.555 . . 1 . . . . . . . . 4554 1 193 . 1 1 43 43 GLY N N 15 105.432 . . 1 . . . . . . . . 4554 1 194 . 1 1 43 43 GLY H H 1 9.048 . . 1 . . . . . . . . 4554 1 195 . 1 1 43 43 GLY CA C 13 44.369 . . 1 . . . . . . . . 4554 1 196 . 1 1 43 43 GLY C C 13 175.136 . . 1 . . . . . . . . 4554 1 197 . 1 1 44 44 ARG N N 15 118.763 . . 1 . . . . . . . . 4554 1 198 . 1 1 44 44 ARG H H 1 7.633 . . 1 . . . . . . . . 4554 1 199 . 1 1 44 44 ARG CA C 13 61.019 . . 1 . . . . . . . . 4554 1 200 . 1 1 44 44 ARG CB C 13 30.068 . . 1 . . . . . . . . 4554 1 201 . 1 1 44 44 ARG C C 13 178.551 . . 1 . . . . . . . . 4554 1 202 . 1 1 45 45 HIS N N 15 113.616 . . 1 . . . . . . . . 4554 1 203 . 1 1 45 45 HIS H H 1 7.429 . . 1 . . . . . . . . 4554 1 204 . 1 1 45 45 HIS CA C 13 57.916 . . 1 . . . . . . . . 4554 1 205 . 1 1 45 45 HIS CB C 13 27.052 . . 1 . . . . . . . . 4554 1 206 . 1 1 45 45 HIS C C 13 178.179 . . 1 . . . . . . . . 4554 1 207 . 1 1 46 46 THR N N 15 121.167 . . 1 . . . . . . . . 4554 1 208 . 1 1 46 46 THR H H 1 8.076 . . 1 . . . . . . . . 4554 1 209 . 1 1 46 46 THR CA C 13 68.772 . . 1 . . . . . . . . 4554 1 210 . 1 1 46 46 THR CB C 13 68.772 . . 1 . . . . . . . . 4554 1 211 . 1 1 46 46 THR C C 13 176.413 . . 1 . . . . . . . . 4554 1 212 . 1 1 47 47 TRP N N 15 123.330 . . 1 . . . . . . . . 4554 1 213 . 1 1 47 47 TRP H H 1 8.331 . . 1 . . . . . . . . 4554 1 214 . 1 1 47 47 TRP CA C 13 59.650 . . 1 . . . . . . . . 4554 1 215 . 1 1 47 47 TRP CB C 13 30.276 . . 1 . . . . . . . . 4554 1 216 . 1 1 47 47 TRP C C 13 177.134 . . 1 . . . . . . . . 4554 1 217 . 1 1 48 48 GLU N N 15 117.821 . . 1 . . . . . . . . 4554 1 218 . 1 1 48 48 GLU H H 1 8.199 . . 1 . . . . . . . . 4554 1 219 . 1 1 48 48 GLU CA C 13 58.884 . . 1 . . . . . . . . 4554 1 220 . 1 1 48 48 GLU CB C 13 28.577 . . 1 . . . . . . . . 4554 1 221 . 1 1 48 48 GLU C C 13 178.597 . . 1 . . . . . . . . 4554 1 222 . 1 1 49 49 SER N N 15 114.305 . . 1 . . . . . . . . 4554 1 223 . 1 1 49 49 SER H H 1 7.873 . . 1 . . . . . . . . 4554 1 224 . 1 1 49 49 SER CA C 13 60.489 . . 1 . . . . . . . . 4554 1 225 . 1 1 49 49 SER CB C 13 63.572 . . 1 . . . . . . . . 4554 1 226 . 1 1 49 49 SER C C 13 175.901 . . 1 . . . . . . . . 4554 1 227 . 1 1 50 50 ILE N N 15 120.112 . . 1 . . . . . . . . 4554 1 228 . 1 1 50 50 ILE H H 1 7.958 . . 1 . . . . . . . . 4554 1 229 . 1 1 50 50 ILE CA C 13 64.625 . . 1 . . . . . . . . 4554 1 230 . 1 1 50 50 ILE CB C 13 39.014 . . 1 . . . . . . . . 4554 1 231 . 1 1 50 50 ILE C C 13 179.248 . . 1 . . . . . . . . 4554 1 232 . 1 1 51 51 GLY N N 15 106.515 . . 1 . . . . . . . . 4554 1 233 . 1 1 51 51 GLY H H 1 7.677 . . 1 . . . . . . . . 4554 1 234 . 1 1 51 51 GLY CA C 13 46.139 . . 1 . . . . . . . . 4554 1 235 . 1 1 51 51 GLY C C 13 172.534 . . 1 . . . . . . . . 4554 1 236 . 1 1 52 52 ARG N N 15 116.964 . . 1 . . . . . . . . 4554 1 237 . 1 1 52 52 ARG H H 1 6.868 . . 1 . . . . . . . . 4554 1 238 . 1 1 52 52 ARG CA C 13 53.644 . . 1 . . . . . . . . 4554 1 239 . 1 1 52 52 ARG CB C 13 29.825 . . 1 . . . . . . . . 4554 1 240 . 1 1 53 53 PRO CA C 13 62.072 . . 1 . . . . . . . . 4554 1 241 . 1 1 53 53 PRO CB C 13 31.805 . . 1 . . . . . . . . 4554 1 242 . 1 1 53 53 PRO C C 13 177.041 . . 1 . . . . . . . . 4554 1 243 . 1 1 54 54 LEU N N 15 126.301 . . 1 . . . . . . . . 4554 1 244 . 1 1 54 54 LEU H H 1 9.885 . . 1 . . . . . . . . 4554 1 245 . 1 1 54 54 LEU CA C 13 53.228 . . 1 . . . . . . . . 4554 1 246 . 1 1 54 54 LEU CB C 13 40.851 . . 1 . . . . . . . . 4554 1 247 . 1 1 55 55 PRO C C 13 179.743 . . 1 . . . . . . . . 4554 1 248 . 1 1 56 56 GLY N N 15 112.525 . . 1 . . . . . . . . 4554 1 249 . 1 1 56 56 GLY H H 1 7.682 . . 1 . . . . . . . . 4554 1 250 . 1 1 56 56 GLY CA C 13 46.769 . . 1 . . . . . . . . 4554 1 251 . 1 1 56 56 GLY C C 13 173.161 . . 1 . . . . . . . . 4554 1 252 . 1 1 57 57 ARG N N 15 116.941 . . 1 . . . . . . . . 4554 1 253 . 1 1 57 57 ARG H H 1 7.211 . . 1 . . . . . . . . 4554 1 254 . 1 1 57 57 ARG CA C 13 53.950 . . 1 . . . . . . . . 4554 1 255 . 1 1 57 57 ARG CB C 13 35.037 . . 1 . . . . . . . . 4554 1 256 . 1 1 57 57 ARG C C 13 174.787 . . 1 . . . . . . . . 4554 1 257 . 1 1 58 58 LYS N N 15 123.554 . . 1 . . . . . . . . 4554 1 258 . 1 1 58 58 LYS H H 1 8.060 . . 1 . . . . . . . . 4554 1 259 . 1 1 58 58 LYS CA C 13 56.652 . . 1 . . . . . . . . 4554 1 260 . 1 1 58 58 LYS CB C 13 32.197 . . 1 . . . . . . . . 4554 1 261 . 1 1 58 58 LYS C C 13 175.066 . . 1 . . . . . . . . 4554 1 262 . 1 1 59 59 ASN N N 15 125.039 . . 1 . . . . . . . . 4554 1 263 . 1 1 59 59 ASN H H 1 9.057 . . 1 . . . . . . . . 4554 1 264 . 1 1 59 59 ASN CA C 13 52.949 . . 1 . . . . . . . . 4554 1 265 . 1 1 59 59 ASN CB C 13 41.145 . . 1 . . . . . . . . 4554 1 266 . 1 1 59 59 ASN C C 13 172.650 . . 1 . . . . . . . . 4554 1 267 . 1 1 60 60 ILE N N 15 126.137 . . 1 . . . . . . . . 4554 1 268 . 1 1 60 60 ILE H H 1 8.878 . . 1 . . . . . . . . 4554 1 269 . 1 1 60 60 ILE CA C 13 59.750 . . 1 . . . . . . . . 4554 1 270 . 1 1 60 60 ILE CB C 13 39.050 . . 1 . . . . . . . . 4554 1 271 . 1 1 60 60 ILE C C 13 172.557 . . 1 . . . . . . . . 4554 1 272 . 1 1 61 61 ILE N N 15 127.122 . . 1 . . . . . . . . 4554 1 273 . 1 1 61 61 ILE H H 1 8.876 . . 1 . . . . . . . . 4554 1 274 . 1 1 61 61 ILE CA C 13 57.669 . . 1 . . . . . . . . 4554 1 275 . 1 1 61 61 ILE CB C 13 37.036 . . 1 . . . . . . . . 4554 1 276 . 1 1 61 61 ILE C C 13 175.879 . . 1 . . . . . . . . 4554 1 277 . 1 1 62 62 LEU N N 15 125.423 . . 1 . . . . . . . . 4554 1 278 . 1 1 62 62 LEU H H 1 8.223 . . 1 . . . . . . . . 4554 1 279 . 1 1 62 62 LEU CA C 13 53.771 . . 1 . . . . . . . . 4554 1 280 . 1 1 62 62 LEU CB C 13 42.895 . . 1 . . . . . . . . 4554 1 281 . 1 1 62 62 LEU C C 13 175.740 . . 1 . . . . . . . . 4554 1 282 . 1 1 63 63 SER N N 15 114.761 . . 1 . . . . . . . . 4554 1 283 . 1 1 63 63 SER H H 1 8.689 . . 1 . . . . . . . . 4554 1 284 . 1 1 63 63 SER CA C 13 58.654 . . 1 . . . . . . . . 4554 1 285 . 1 1 63 63 SER CB C 13 65.012 . . 1 . . . . . . . . 4554 1 286 . 1 1 63 63 SER C C 13 174.346 . . 1 . . . . . . . . 4554 1 287 . 1 1 64 64 SER N N 15 122.762 . . 1 . . . . . . . . 4554 1 288 . 1 1 64 64 SER H H 1 10.221 . . 1 . . . . . . . . 4554 1 289 . 1 1 64 64 SER CA C 13 60.477 . . 1 . . . . . . . . 4554 1 290 . 1 1 64 64 SER CB C 13 64.414 . . 1 . . . . . . . . 4554 1 291 . 1 1 64 64 SER C C 13 175.112 . . 1 . . . . . . . . 4554 1 292 . 1 1 65 65 GLN N N 15 123.017 . . 1 . . . . . . . . 4554 1 293 . 1 1 65 65 GLN H H 1 8.652 . . 1 . . . . . . . . 4554 1 294 . 1 1 65 65 GLN CA C 13 53.124 . . 1 . . . . . . . . 4554 1 295 . 1 1 65 65 GLN CB C 13 29.513 . . 1 . . . . . . . . 4554 1 296 . 1 1 66 66 PRO CA C 13 62.826 . . 1 . . . . . . . . 4554 1 297 . 1 1 66 66 PRO CB C 13 32.010 . . 1 . . . . . . . . 4554 1 298 . 1 1 66 66 PRO C C 13 177.343 . . 1 . . . . . . . . 4554 1 299 . 1 1 67 67 GLY N N 15 109.454 . . 1 . . . . . . . . 4554 1 300 . 1 1 67 67 GLY H H 1 8.134 . . 1 . . . . . . . . 4554 1 301 . 1 1 67 67 GLY CA C 13 42.550 . . 1 . . . . . . . . 4554 1 302 . 1 1 67 67 GLY C C 13 174.508 . . 1 . . . . . . . . 4554 1 303 . 1 1 68 68 THR N N 15 106.177 . . 1 . . . . . . . . 4554 1 304 . 1 1 68 68 THR H H 1 5.752 . . 1 . . . . . . . . 4554 1 305 . 1 1 68 68 THR CA C 13 60.312 . . 1 . . . . . . . . 4554 1 306 . 1 1 68 68 THR CB C 13 69.166 . . 1 . . . . . . . . 4554 1 307 . 1 1 68 68 THR C C 13 174.346 . . 1 . . . . . . . . 4554 1 308 . 1 1 69 69 ASP N N 15 120.330 . . 1 . . . . . . . . 4554 1 309 . 1 1 69 69 ASP H H 1 7.432 . . 1 . . . . . . . . 4554 1 310 . 1 1 69 69 ASP CA C 13 55.282 . . 1 . . . . . . . . 4554 1 311 . 1 1 69 69 ASP CB C 13 41.825 . . 1 . . . . . . . . 4554 1 312 . 1 1 69 69 ASP C C 13 176.390 . . 1 . . . . . . . . 4554 1 313 . 1 1 70 70 ASP N N 15 126.917 . . 1 . . . . . . . . 4554 1 314 . 1 1 70 70 ASP H H 1 9.036 . . 1 . . . . . . . . 4554 1 315 . 1 1 70 70 ASP CA C 13 55.265 . . 1 . . . . . . . . 4554 1 316 . 1 1 70 70 ASP CB C 13 40.276 . . 1 . . . . . . . . 4554 1 317 . 1 1 70 70 ASP C C 13 177.203 . . 1 . . . . . . . . 4554 1 318 . 1 1 71 71 ARG N N 15 118.232 . . 1 . . . . . . . . 4554 1 319 . 1 1 71 71 ARG H H 1 8.986 . . 1 . . . . . . . . 4554 1 320 . 1 1 71 71 ARG CA C 13 57.307 . . 1 . . . . . . . . 4554 1 321 . 1 1 71 71 ARG CB C 13 31.990 . . 1 . . . . . . . . 4554 1 322 . 1 1 71 71 ARG C C 13 176.111 . . 1 . . . . . . . . 4554 1 323 . 1 1 72 72 VAL N N 15 108.493 . . 1 . . . . . . . . 4554 1 324 . 1 1 72 72 VAL H H 1 7.287 . . 1 . . . . . . . . 4554 1 325 . 1 1 72 72 VAL CA C 13 58.159 . . 1 . . . . . . . . 4554 1 326 . 1 1 72 72 VAL CB C 13 33.500 . . 1 . . . . . . . . 4554 1 327 . 1 1 72 72 VAL C C 13 173.068 . . 1 . . . . . . . . 4554 1 328 . 1 1 73 73 THR N N 15 117.244 . . 1 . . . . . . . . 4554 1 329 . 1 1 73 73 THR H H 1 8.088 . . 1 . . . . . . . . 4554 1 330 . 1 1 73 73 THR CA C 13 62.714 . . 1 . . . . . . . . 4554 1 331 . 1 1 73 73 THR CB C 13 70.249 . . 1 . . . . . . . . 4554 1 332 . 1 1 73 73 THR C C 13 172.022 . . 1 . . . . . . . . 4554 1 333 . 1 1 74 74 TRP N N 15 128.837 . . 1 . . . . . . . . 4554 1 334 . 1 1 74 74 TRP H H 1 8.906 . . 1 . . . . . . . . 4554 1 335 . 1 1 74 74 TRP CA C 13 56.035 . . 1 . . . . . . . . 4554 1 336 . 1 1 74 74 TRP CB C 13 28.864 . . 1 . . . . . . . . 4554 1 337 . 1 1 74 74 TRP C C 13 176.832 . . 1 . . . . . . . . 4554 1 338 . 1 1 75 75 VAL N N 15 116.622 . . 1 . . . . . . . . 4554 1 339 . 1 1 75 75 VAL H H 1 9.203 . . 1 . . . . . . . . 4554 1 340 . 1 1 75 75 VAL CA C 13 58.945 . . 1 . . . . . . . . 4554 1 341 . 1 1 75 75 VAL CB C 13 35.914 . . 1 . . . . . . . . 4554 1 342 . 1 1 75 75 VAL C C 13 174.857 . . 1 . . . . . . . . 4554 1 343 . 1 1 76 76 LYS N N 15 115.584 . . 1 . . . . . . . . 4554 1 344 . 1 1 76 76 LYS H H 1 8.277 . . 1 . . . . . . . . 4554 1 345 . 1 1 76 76 LYS CA C 13 55.553 . . 1 . . . . . . . . 4554 1 346 . 1 1 76 76 LYS CB C 13 34.096 . . 1 . . . . . . . . 4554 1 347 . 1 1 76 76 LYS C C 13 175.623 . . 1 . . . . . . . . 4554 1 348 . 1 1 77 77 SER N N 15 108.749 . . 1 . . . . . . . . 4554 1 349 . 1 1 77 77 SER H H 1 7.223 . . 1 . . . . . . . . 4554 1 350 . 1 1 77 77 SER CA C 13 57.195 . . 1 . . . . . . . . 4554 1 351 . 1 1 77 77 SER CB C 13 66.708 . . 1 . . . . . . . . 4554 1 352 . 1 1 77 77 SER C C 13 174.067 . . 1 . . . . . . . . 4554 1 353 . 1 1 78 78 VAL N N 15 122.695 . . 1 . . . . . . . . 4554 1 354 . 1 1 78 78 VAL H H 1 8.968 . . 1 . . . . . . . . 4554 1 355 . 1 1 78 78 VAL CA C 13 67.094 . . 1 . . . . . . . . 4554 1 356 . 1 1 78 78 VAL CB C 13 31.443 . . 1 . . . . . . . . 4554 1 357 . 1 1 78 78 VAL C C 13 177.366 . . 1 . . . . . . . . 4554 1 358 . 1 1 79 79 ASP N N 15 118.071 . . 1 . . . . . . . . 4554 1 359 . 1 1 79 79 ASP H H 1 8.615 . . 1 . . . . . . . . 4554 1 360 . 1 1 79 79 ASP CA C 13 57.585 . . 1 . . . . . . . . 4554 1 361 . 1 1 79 79 ASP CB C 13 39.714 . . 1 . . . . . . . . 4554 1 362 . 1 1 79 79 ASP C C 13 180.084 . . 1 . . . . . . . . 4554 1 363 . 1 1 80 80 GLU N N 15 120.635 . . 1 . . . . . . . . 4554 1 364 . 1 1 80 80 GLU H H 1 8.000 . . 1 . . . . . . . . 4554 1 365 . 1 1 80 80 GLU CA C 13 59.202 . . 1 . . . . . . . . 4554 1 366 . 1 1 80 80 GLU CB C 13 30.731 . . 1 . . . . . . . . 4554 1 367 . 1 1 80 80 GLU C C 13 179.271 . . 1 . . . . . . . . 4554 1 368 . 1 1 81 81 ALA N N 15 122.901 . . 1 . . . . . . . . 4554 1 369 . 1 1 81 81 ALA H H 1 8.264 . . 1 . . . . . . . . 4554 1 370 . 1 1 81 81 ALA CA C 13 55.487 . . 1 . . . . . . . . 4554 1 371 . 1 1 81 81 ALA CB C 13 17.961 . . 1 . . . . . . . . 4554 1 372 . 1 1 81 81 ALA C C 13 177.970 . . 1 . . . . . . . . 4554 1 373 . 1 1 82 82 ILE N N 15 116.075 . . 1 . . . . . . . . 4554 1 374 . 1 1 82 82 ILE H H 1 8.027 . . 1 . . . . . . . . 4554 1 375 . 1 1 82 82 ILE CA C 13 65.674 . . 1 . . . . . . . . 4554 1 376 . 1 1 82 82 ILE CB C 13 38.706 . . 1 . . . . . . . . 4554 1 377 . 1 1 82 82 ILE C C 13 180.456 . . 1 . . . . . . . . 4554 1 378 . 1 1 83 83 ALA N N 15 123.706 . . 1 . . . . . . . . 4554 1 379 . 1 1 83 83 ALA H H 1 8.175 . . 1 . . . . . . . . 4554 1 380 . 1 1 83 83 ALA CA C 13 54.979 . . 1 . . . . . . . . 4554 1 381 . 1 1 83 83 ALA CB C 13 17.970 . . 1 . . . . . . . . 4554 1 382 . 1 1 83 83 ALA C C 13 180.525 . . 1 . . . . . . . . 4554 1 383 . 1 1 84 84 ALA N N 15 119.346 . . 1 . . . . . . . . 4554 1 384 . 1 1 84 84 ALA H H 1 8.075 . . 1 . . . . . . . . 4554 1 385 . 1 1 84 84 ALA CA C 13 53.776 . . 1 . . . . . . . . 4554 1 386 . 1 1 84 84 ALA CB C 13 18.072 . . 1 . . . . . . . . 4554 1 387 . 1 1 84 84 ALA C C 13 177.157 . . 1 . . . . . . . . 4554 1 388 . 1 1 85 85 CYS N N 15 114.394 . . 1 . . . . . . . . 4554 1 389 . 1 1 85 85 CYS H H 1 7.402 . . 1 . . . . . . . . 4554 1 390 . 1 1 85 85 CYS CA C 13 62.015 . . 1 . . . . . . . . 4554 1 391 . 1 1 85 85 CYS CB C 13 27.847 . . 1 . . . . . . . . 4554 1 392 . 1 1 85 85 CYS C C 13 175.391 . . 1 . . . . . . . . 4554 1 393 . 1 1 86 86 GLY N N 15 103.101 . . 1 . . . . . . . . 4554 1 394 . 1 1 86 86 GLY H H 1 7.287 . . 1 . . . . . . . . 4554 1 395 . 1 1 86 86 GLY CA C 13 44.919 . . 1 . . . . . . . . 4554 1 396 . 1 1 86 86 GLY C C 13 173.277 . . 1 . . . . . . . . 4554 1 397 . 1 1 87 87 ASP N N 15 122.162 . . 1 . . . . . . . . 4554 1 398 . 1 1 87 87 ASP H H 1 8.665 . . 1 . . . . . . . . 4554 1 399 . 1 1 87 87 ASP CA C 13 53.206 . . 1 . . . . . . . . 4554 1 400 . 1 1 87 87 ASP CB C 13 39.505 . . 1 . . . . . . . . 4554 1 401 . 1 1 87 87 ASP C C 13 175.414 . . 1 . . . . . . . . 4554 1 402 . 1 1 88 88 VAL N N 15 114.973 . . 1 . . . . . . . . 4554 1 403 . 1 1 88 88 VAL H H 1 7.316 . . 1 . . . . . . . . 4554 1 404 . 1 1 88 88 VAL CA C 13 57.906 . . 1 . . . . . . . . 4554 1 405 . 1 1 88 88 VAL CB C 13 32.322 . . 1 . . . . . . . . 4554 1 406 . 1 1 89 89 PRO CA C 13 64.519 . . 1 . . . . . . . . 4554 1 407 . 1 1 89 89 PRO CB C 13 32.203 . . 1 . . . . . . . . 4554 1 408 . 1 1 89 89 PRO C C 13 177.854 . . 1 . . . . . . . . 4554 1 409 . 1 1 90 90 GLU N N 15 116.615 . . 1 . . . . . . . . 4554 1 410 . 1 1 90 90 GLU H H 1 7.729 . . 1 . . . . . . . . 4554 1 411 . 1 1 90 90 GLU CA C 13 55.820 . . 1 . . . . . . . . 4554 1 412 . 1 1 90 90 GLU CB C 13 32.845 . . 1 . . . . . . . . 4554 1 413 . 1 1 90 90 GLU C C 13 173.370 . . 1 . . . . . . . . 4554 1 414 . 1 1 91 91 ILE N N 15 130.104 . . 1 . . . . . . . . 4554 1 415 . 1 1 91 91 ILE H H 1 8.847 . . 1 . . . . . . . . 4554 1 416 . 1 1 91 91 ILE CA C 13 61.274 . . 1 . . . . . . . . 4554 1 417 . 1 1 91 91 ILE CB C 13 41.393 . . 1 . . . . . . . . 4554 1 418 . 1 1 91 91 ILE C C 13 173.835 . . 1 . . . . . . . . 4554 1 419 . 1 1 92 92 MET N N 15 121.489 . . 1 . . . . . . . . 4554 1 420 . 1 1 92 92 MET H H 1 7.974 . . 1 . . . . . . . . 4554 1 421 . 1 1 92 92 MET CA C 13 51.931 . . 1 . . . . . . . . 4554 1 422 . 1 1 92 92 MET CB C 13 30.106 . . 1 . . . . . . . . 4554 1 423 . 1 1 92 92 MET C C 13 174.090 . . 1 . . . . . . . . 4554 1 424 . 1 1 93 93 VAL N N 15 125.298 . . 1 . . . . . . . . 4554 1 425 . 1 1 93 93 VAL H H 1 9.324 . . 1 . . . . . . . . 4554 1 426 . 1 1 93 93 VAL CA C 13 62.091 . . 1 . . . . . . . . 4554 1 427 . 1 1 93 93 VAL CB C 13 31.443 . . 1 . . . . . . . . 4554 1 428 . 1 1 93 93 VAL C C 13 177.226 . . 1 . . . . . . . . 4554 1 429 . 1 1 94 94 ILE N N 15 118.482 . . 1 . . . . . . . . 4554 1 430 . 1 1 94 94 ILE H H 1 8.554 . . 1 . . . . . . . . 4554 1 431 . 1 1 94 94 ILE CA C 13 60.996 . . 1 . . . . . . . . 4554 1 432 . 1 1 94 94 ILE CB C 13 37.667 . . 1 . . . . . . . . 4554 1 433 . 1 1 94 94 ILE C C 13 173.579 . . 1 . . . . . . . . 4554 1 434 . 1 1 95 95 GLY N N 15 102.691 . . 1 . . . . . . . . 4554 1 435 . 1 1 95 95 GLY H H 1 6.056 . . 1 . . . . . . . . 4554 1 436 . 1 1 95 95 GLY CA C 13 41.349 . . 1 . . . . . . . . 4554 1 437 . 1 1 95 95 GLY C C 13 174.578 . . 1 . . . . . . . . 4554 1 438 . 1 1 96 96 GLY N N 15 112.501 . . 1 . . . . . . . . 4554 1 439 . 1 1 96 96 GLY H H 1 7.700 . . 1 . . . . . . . . 4554 1 440 . 1 1 96 96 GLY CA C 13 46.522 . . 1 . . . . . . . . 4554 1 441 . 1 1 96 96 GLY C C 13 173.927 . . 1 . . . . . . . . 4554 1 442 . 1 1 97 97 GLY N N 15 108.472 . . 1 . . . . . . . . 4554 1 443 . 1 1 97 97 GLY H H 1 7.425 . . 1 . . . . . . . . 4554 1 444 . 1 1 97 97 GLY CA C 13 49.396 . . 1 . . . . . . . . 4554 1 445 . 1 1 97 97 GLY C C 13 175.414 . . 1 . . . . . . . . 4554 1 446 . 1 1 98 98 ARG N N 15 123.629 . . 1 . . . . . . . . 4554 1 447 . 1 1 98 98 ARG H H 1 9.877 . . 1 . . . . . . . . 4554 1 448 . 1 1 98 98 ARG CA C 13 58.360 . . 1 . . . . . . . . 4554 1 449 . 1 1 98 98 ARG CB C 13 29.664 . . 1 . . . . . . . . 4554 1 450 . 1 1 98 98 ARG C C 13 180.944 . . 1 . . . . . . . . 4554 1 451 . 1 1 99 99 VAL N N 15 122.974 . . 1 . . . . . . . . 4554 1 452 . 1 1 99 99 VAL H H 1 7.497 . . 1 . . . . . . . . 4554 1 453 . 1 1 99 99 VAL CA C 13 68.544 . . 1 . . . . . . . . 4554 1 454 . 1 1 99 99 VAL CB C 13 31.531 . . 1 . . . . . . . . 4554 1 455 . 1 1 99 99 VAL C C 13 178.899 . . 1 . . . . . . . . 4554 1 456 . 1 1 100 100 TYR N N 15 120.179 . . 1 . . . . . . . . 4554 1 457 . 1 1 100 100 TYR H H 1 9.621 . . 1 . . . . . . . . 4554 1 458 . 1 1 100 100 TYR CA C 13 60.157 . . 1 . . . . . . . . 4554 1 459 . 1 1 100 100 TYR CB C 13 37.954 . . 1 . . . . . . . . 4554 1 460 . 1 1 100 100 TYR C C 13 178.365 . . 1 . . . . . . . . 4554 1 461 . 1 1 101 101 GLU N N 15 115.906 . . 1 . . . . . . . . 4554 1 462 . 1 1 101 101 GLU H H 1 8.182 . . 1 . . . . . . . . 4554 1 463 . 1 1 101 101 GLU CA C 13 59.932 . . 1 . . . . . . . . 4554 1 464 . 1 1 101 101 GLU CB C 13 29.680 . . 1 . . . . . . . . 4554 1 465 . 1 1 101 101 GLU C C 13 178.620 . . 1 . . . . . . . . 4554 1 466 . 1 1 102 102 GLN N N 15 114.072 . . 1 . . . . . . . . 4554 1 467 . 1 1 102 102 GLN H H 1 7.301 . . 1 . . . . . . . . 4554 1 468 . 1 1 102 102 GLN CA C 13 57.887 . . 1 . . . . . . . . 4554 1 469 . 1 1 102 102 GLN CB C 13 32.714 . . 1 . . . . . . . . 4554 1 470 . 1 1 102 102 GLN C C 13 177.459 . . 1 . . . . . . . . 4554 1 471 . 1 1 103 103 PHE N N 15 113.616 . . 1 . . . . . . . . 4554 1 472 . 1 1 103 103 PHE H H 1 8.190 . . 1 . . . . . . . . 4554 1 473 . 1 1 103 103 PHE CA C 13 60.481 . . 1 . . . . . . . . 4554 1 474 . 1 1 103 103 PHE CB C 13 41.531 . . 1 . . . . . . . . 4554 1 475 . 1 1 103 103 PHE C C 13 177.180 . . 1 . . . . . . . . 4554 1 476 . 1 1 104 104 LEU N N 15 123.339 . . 1 . . . . . . . . 4554 1 477 . 1 1 104 104 LEU H H 1 8.538 . . 1 . . . . . . . . 4554 1 478 . 1 1 104 104 LEU CA C 13 60.925 . . 1 . . . . . . . . 4554 1 479 . 1 1 104 104 LEU CB C 13 38.250 . . 1 . . . . . . . . 4554 1 480 . 1 1 105 105 PRO CA C 13 65.342 . . 1 . . . . . . . . 4554 1 481 . 1 1 105 105 PRO CB C 13 31.212 . . 1 . . . . . . . . 4554 1 482 . 1 1 105 105 PRO C C 13 177.482 . . 1 . . . . . . . . 4554 1 483 . 1 1 106 106 LYS N N 15 112.927 . . 1 . . . . . . . . 4554 1 484 . 1 1 106 106 LYS H H 1 7.439 . . 1 . . . . . . . . 4554 1 485 . 1 1 106 106 LYS CA C 13 55.572 . . 1 . . . . . . . . 4554 1 486 . 1 1 106 106 LYS CB C 13 34.595 . . 1 . . . . . . . . 4554 1 487 . 1 1 106 106 LYS C C 13 176.065 . . 1 . . . . . . . . 4554 1 488 . 1 1 107 107 ALA N N 15 122.651 . . 1 . . . . . . . . 4554 1 489 . 1 1 107 107 ALA H H 1 8.008 . . 1 . . . . . . . . 4554 1 490 . 1 1 107 107 ALA CA C 13 52.493 . . 1 . . . . . . . . 4554 1 491 . 1 1 107 107 ALA CB C 13 20.935 . . 1 . . . . . . . . 4554 1 492 . 1 1 108 108 GLN N N 15 118.294 . . 1 . . . . . . . . 4554 1 493 . 1 1 108 108 GLN H H 1 9.323 . . 1 . . . . . . . . 4554 1 494 . 1 1 108 108 GLN CA C 13 55.580 . . 1 . . . . . . . . 4554 1 495 . 1 1 108 108 GLN CB C 13 31.524 . . 1 . . . . . . . . 4554 1 496 . 1 1 108 108 GLN C C 13 175.484 . . 1 . . . . . . . . 4554 1 497 . 1 1 109 109 LYS N N 15 120.843 . . 1 . . . . . . . . 4554 1 498 . 1 1 109 109 LYS H H 1 7.822 . . 1 . . . . . . . . 4554 1 499 . 1 1 109 109 LYS CA C 13 56.015 . . 1 . . . . . . . . 4554 1 500 . 1 1 109 109 LYS CB C 13 36.898 . . 1 . . . . . . . . 4554 1 501 . 1 1 109 109 LYS C C 13 174.137 . . 1 . . . . . . . . 4554 1 502 . 1 1 110 110 LEU N N 15 121.616 . . 1 . . . . . . . . 4554 1 503 . 1 1 110 110 LEU H H 1 9.015 . . 1 . . . . . . . . 4554 1 504 . 1 1 110 110 LEU CA C 13 52.973 . . 1 . . . . . . . . 4554 1 505 . 1 1 110 110 LEU CB C 13 44.462 . . 1 . . . . . . . . 4554 1 506 . 1 1 110 110 LEU C C 13 174.764 . . 1 . . . . . . . . 4554 1 507 . 1 1 111 111 TYR N N 15 122.037 . . 1 . . . . . . . . 4554 1 508 . 1 1 111 111 TYR H H 1 9.408 . . 1 . . . . . . . . 4554 1 509 . 1 1 111 111 TYR CA C 13 56.299 . . 1 . . . . . . . . 4554 1 510 . 1 1 111 111 TYR CB C 13 38.435 . . 1 . . . . . . . . 4554 1 511 . 1 1 111 111 TYR C C 13 174.206 . . 1 . . . . . . . . 4554 1 512 . 1 1 112 112 LEU N N 15 122.458 . . 1 . . . . . . . . 4554 1 513 . 1 1 112 112 LEU H H 1 9.734 . . 1 . . . . . . . . 4554 1 514 . 1 1 112 112 LEU CA C 13 52.718 . . 1 . . . . . . . . 4554 1 515 . 1 1 112 112 LEU CB C 13 45.119 . . 1 . . . . . . . . 4554 1 516 . 1 1 112 112 LEU C C 13 175.670 . . 1 . . . . . . . . 4554 1 517 . 1 1 113 113 THR N N 15 117.736 . . 1 . . . . . . . . 4554 1 518 . 1 1 113 113 THR H H 1 8.083 . . 1 . . . . . . . . 4554 1 519 . 1 1 113 113 THR CA C 13 60.162 . . 1 . . . . . . . . 4554 1 520 . 1 1 113 113 THR CB C 13 68.818 . . 1 . . . . . . . . 4554 1 521 . 1 1 113 113 THR C C 13 173.416 . . 1 . . . . . . . . 4554 1 522 . 1 1 114 114 HIS N N 15 126.104 . . 1 . . . . . . . . 4554 1 523 . 1 1 114 114 HIS H H 1 9.292 . . 1 . . . . . . . . 4554 1 524 . 1 1 114 114 HIS CA C 13 55.089 . . 1 . . . . . . . . 4554 1 525 . 1 1 114 114 HIS CB C 13 30.900 . . 1 . . . . . . . . 4554 1 526 . 1 1 114 114 HIS C C 13 175.833 . . 1 . . . . . . . . 4554 1 527 . 1 1 115 115 ILE N N 15 127.126 . . 1 . . . . . . . . 4554 1 528 . 1 1 115 115 ILE H H 1 9.135 . . 1 . . . . . . . . 4554 1 529 . 1 1 115 115 ILE CA C 13 60.741 . . 1 . . . . . . . . 4554 1 530 . 1 1 115 115 ILE CB C 13 39.220 . . 1 . . . . . . . . 4554 1 531 . 1 1 115 115 ILE C C 13 176.832 . . 1 . . . . . . . . 4554 1 532 . 1 1 116 116 ASP N N 15 129.899 . . 1 . . . . . . . . 4554 1 533 . 1 1 116 116 ASP H H 1 8.415 . . 1 . . . . . . . . 4554 1 534 . 1 1 116 116 ASP CA C 13 53.509 . . 1 . . . . . . . . 4554 1 535 . 1 1 116 116 ASP CB C 13 38.500 . . 1 . . . . . . . . 4554 1 536 . 1 1 116 116 ASP C C 13 173.927 . . 1 . . . . . . . . 4554 1 537 . 1 1 117 117 ALA N N 15 124.188 . . 1 . . . . . . . . 4554 1 538 . 1 1 117 117 ALA H H 1 7.801 . . 1 . . . . . . . . 4554 1 539 . 1 1 117 117 ALA CA C 13 51.049 . . 1 . . . . . . . . 4554 1 540 . 1 1 117 117 ALA CB C 13 20.298 . . 1 . . . . . . . . 4554 1 541 . 1 1 117 117 ALA C C 13 174.578 . . 1 . . . . . . . . 4554 1 542 . 1 1 118 118 GLU N N 15 123.420 . . 1 . . . . . . . . 4554 1 543 . 1 1 118 118 GLU H H 1 8.629 . . 1 . . . . . . . . 4554 1 544 . 1 1 118 118 GLU CA C 13 55.278 . . 1 . . . . . . . . 4554 1 545 . 1 1 118 118 GLU CB C 13 29.178 . . 1 . . . . . . . . 4554 1 546 . 1 1 118 118 GLU C C 13 175.321 . . 1 . . . . . . . . 4554 1 547 . 1 1 119 119 VAL N N 15 119.754 . . 1 . . . . . . . . 4554 1 548 . 1 1 119 119 VAL H H 1 8.278 . . 1 . . . . . . . . 4554 1 549 . 1 1 119 119 VAL CA C 13 58.730 . . 1 . . . . . . . . 4554 1 550 . 1 1 119 119 VAL CB C 13 35.321 . . 1 . . . . . . . . 4554 1 551 . 1 1 119 119 VAL C C 13 174.787 . . 1 . . . . . . . . 4554 1 552 . 1 1 120 120 GLU N N 15 124.162 . . 1 . . . . . . . . 4554 1 553 . 1 1 120 120 GLU H H 1 8.474 . . 1 . . . . . . . . 4554 1 554 . 1 1 120 120 GLU CA C 13 56.408 . . 1 . . . . . . . . 4554 1 555 . 1 1 120 120 GLU CB C 13 30.245 . . 1 . . . . . . . . 4554 1 556 . 1 1 120 120 GLU C C 13 175.995 . . 1 . . . . . . . . 4554 1 557 . 1 1 121 121 GLY N N 15 107.202 . . 1 . . . . . . . . 4554 1 558 . 1 1 121 121 GLY H H 1 8.594 . . 1 . . . . . . . . 4554 1 559 . 1 1 121 121 GLY CA C 13 45.973 . . 1 . . . . . . . . 4554 1 560 . 1 1 121 121 GLY C C 13 172.882 . . 1 . . . . . . . . 4554 1 561 . 1 1 122 122 ASP N N 15 116.551 . . 1 . . . . . . . . 4554 1 562 . 1 1 122 122 ASP H H 1 8.885 . . 1 . . . . . . . . 4554 1 563 . 1 1 122 122 ASP CA C 13 52.187 . . 1 . . . . . . . . 4554 1 564 . 1 1 122 122 ASP CB C 13 42.339 . . 1 . . . . . . . . 4554 1 565 . 1 1 122 122 ASP C C 13 176.320 . . 1 . . . . . . . . 4554 1 566 . 1 1 123 123 THR N N 15 115.610 . . 1 . . . . . . . . 4554 1 567 . 1 1 123 123 THR H H 1 7.541 . . 1 . . . . . . . . 4554 1 568 . 1 1 123 123 THR CA C 13 62.798 . . 1 . . . . . . . . 4554 1 569 . 1 1 123 123 THR CB C 13 72.991 . . 1 . . . . . . . . 4554 1 570 . 1 1 123 123 THR C C 13 172.859 . . 1 . . . . . . . . 4554 1 571 . 1 1 124 124 HIS N N 15 126.951 . . 1 . . . . . . . . 4554 1 572 . 1 1 124 124 HIS H H 1 9.615 . . 1 . . . . . . . . 4554 1 573 . 1 1 124 124 HIS CA C 13 56.550 . . 1 . . . . . . . . 4554 1 574 . 1 1 124 124 HIS CB C 13 33.613 . . 1 . . . . . . . . 4554 1 575 . 1 1 124 124 HIS C C 13 174.044 . . 1 . . . . . . . . 4554 1 576 . 1 1 125 125 PHE N N 15 124.958 . . 1 . . . . . . . . 4554 1 577 . 1 1 125 125 PHE H H 1 9.357 . . 1 . . . . . . . . 4554 1 578 . 1 1 125 125 PHE CA C 13 57.077 . . 1 . . . . . . . . 4554 1 579 . 1 1 125 125 PHE CB C 13 41.787 . . 1 . . . . . . . . 4554 1 580 . 1 1 126 126 PRO CA C 13 62.511 . . 1 . . . . . . . . 4554 1 581 . 1 1 126 126 PRO CB C 13 31.988 . . 1 . . . . . . . . 4554 1 582 . 1 1 126 126 PRO C C 13 173.951 . . 1 . . . . . . . . 4554 1 583 . 1 1 127 127 ASP N N 15 117.656 . . 1 . . . . . . . . 4554 1 584 . 1 1 127 127 ASP H H 1 8.230 . . 1 . . . . . . . . 4554 1 585 . 1 1 127 127 ASP CA C 13 54.293 . . 1 . . . . . . . . 4554 1 586 . 1 1 127 127 ASP CB C 13 40.603 . . 1 . . . . . . . . 4554 1 587 . 1 1 127 127 ASP C C 13 173.463 . . 1 . . . . . . . . 4554 1 588 . 1 1 128 128 TYR N N 15 119.752 . . 1 . . . . . . . . 4554 1 589 . 1 1 128 128 TYR H H 1 7.564 . . 1 . . . . . . . . 4554 1 590 . 1 1 128 128 TYR CA C 13 55.365 . . 1 . . . . . . . . 4554 1 591 . 1 1 128 128 TYR CB C 13 39.202 . . 1 . . . . . . . . 4554 1 592 . 1 1 128 128 TYR C C 13 173.602 . . 1 . . . . . . . . 4554 1 593 . 1 1 129 129 GLU N N 15 123.652 . . 1 . . . . . . . . 4554 1 594 . 1 1 129 129 GLU H H 1 8.913 . . 1 . . . . . . . . 4554 1 595 . 1 1 129 129 GLU CA C 13 53.124 . . 1 . . . . . . . . 4554 1 596 . 1 1 129 129 GLU CB C 13 29.721 . . 1 . . . . . . . . 4554 1 597 . 1 1 130 130 PRO CA C 13 65.984 . . 1 . . . . . . . . 4554 1 598 . 1 1 130 130 PRO CB C 13 32.205 . . 1 . . . . . . . . 4554 1 599 . 1 1 130 130 PRO C C 13 178.504 . . 1 . . . . . . . . 4554 1 600 . 1 1 131 131 ASP N N 15 114.886 . . 1 . . . . . . . . 4554 1 601 . 1 1 131 131 ASP H H 1 9.228 . . 1 . . . . . . . . 4554 1 602 . 1 1 131 131 ASP CA C 13 56.561 . . 1 . . . . . . . . 4554 1 603 . 1 1 131 131 ASP CB C 13 39.958 . . 1 . . . . . . . . 4554 1 604 . 1 1 131 131 ASP C C 13 176.111 . . 1 . . . . . . . . 4554 1 605 . 1 1 132 132 ASP N N 15 117.958 . . 1 . . . . . . . . 4554 1 606 . 1 1 132 132 ASP H H 1 8.256 . . 1 . . . . . . . . 4554 1 607 . 1 1 132 132 ASP CA C 13 55.010 . . 1 . . . . . . . . 4554 1 608 . 1 1 132 132 ASP CB C 13 41.316 . . 1 . . . . . . . . 4554 1 609 . 1 1 132 132 ASP C C 13 175.159 . . 1 . . . . . . . . 4554 1 610 . 1 1 133 133 TRP N N 15 119.886 . . 1 . . . . . . . . 4554 1 611 . 1 1 133 133 TRP H H 1 7.841 . . 1 . . . . . . . . 4554 1 612 . 1 1 133 133 TRP CA C 13 56.052 . . 1 . . . . . . . . 4554 1 613 . 1 1 133 133 TRP CB C 13 34.125 . . 1 . . . . . . . . 4554 1 614 . 1 1 133 133 TRP C C 13 173.951 . . 1 . . . . . . . . 4554 1 615 . 1 1 134 134 GLU N N 15 122.976 . . 1 . . . . . . . . 4554 1 616 . 1 1 134 134 GLU H H 1 9.636 . . 1 . . . . . . . . 4554 1 617 . 1 1 134 134 GLU CA C 13 54.295 . . 1 . . . . . . . . 4554 1 618 . 1 1 134 134 GLU CB C 13 32.498 . . 1 . . . . . . . . 4554 1 619 . 1 1 134 134 GLU C C 13 175.809 . . 1 . . . . . . . . 4554 1 620 . 1 1 135 135 SER N N 15 121.612 . . 1 . . . . . . . . 4554 1 621 . 1 1 135 135 SER H H 1 9.164 . . 1 . . . . . . . . 4554 1 622 . 1 1 135 135 SER CA C 13 58.652 . . 1 . . . . . . . . 4554 1 623 . 1 1 135 135 SER CB C 13 62.312 . . 1 . . . . . . . . 4554 1 624 . 1 1 135 135 SER C C 13 176.274 . . 1 . . . . . . . . 4554 1 625 . 1 1 136 136 VAL N N 15 122.018 . . 1 . . . . . . . . 4554 1 626 . 1 1 136 136 VAL H H 1 9.083 . . 1 . . . . . . . . 4554 1 627 . 1 1 136 136 VAL CA C 13 60.947 . . 1 . . . . . . . . 4554 1 628 . 1 1 136 136 VAL CB C 13 32.472 . . 1 . . . . . . . . 4554 1 629 . 1 1 136 136 VAL C C 13 175.902 . . 1 . . . . . . . . 4554 1 630 . 1 1 137 137 PHE N N 15 123.857 . . 1 . . . . . . . . 4554 1 631 . 1 1 137 137 PHE H H 1 7.942 . . 1 . . . . . . . . 4554 1 632 . 1 1 137 137 PHE CA C 13 58.406 . . 1 . . . . . . . . 4554 1 633 . 1 1 137 137 PHE CB C 13 42.875 . . 1 . . . . . . . . 4554 1 634 . 1 1 137 137 PHE C C 13 173.706 . . 1 . . . . . . . . 4554 1 635 . 1 1 138 138 SER N N 15 119.592 . . 1 . . . . . . . . 4554 1 636 . 1 1 138 138 SER H H 1 7.680 . . 1 . . . . . . . . 4554 1 637 . 1 1 138 138 SER CA C 13 57.104 . . 1 . . . . . . . . 4554 1 638 . 1 1 138 138 SER CB C 13 64.241 . . 1 . . . . . . . . 4554 1 639 . 1 1 138 138 SER C C 13 173.254 . . 1 . . . . . . . . 4554 1 640 . 1 1 139 139 GLU N N 15 126.127 . . 1 . . . . . . . . 4554 1 641 . 1 1 139 139 GLU H H 1 8.778 . . 1 . . . . . . . . 4554 1 642 . 1 1 139 139 GLU CA C 13 56.060 . . 1 . . . . . . . . 4554 1 643 . 1 1 139 139 GLU CB C 13 34.866 . . 1 . . . . . . . . 4554 1 644 . 1 1 139 139 GLU C C 13 173.927 . . 1 . . . . . . . . 4554 1 645 . 1 1 140 140 PHE N N 15 128.944 . . 1 . . . . . . . . 4554 1 646 . 1 1 140 140 PHE H H 1 8.776 . . 1 . . . . . . . . 4554 1 647 . 1 1 140 140 PHE CA C 13 58.690 . . 1 . . . . . . . . 4554 1 648 . 1 1 140 140 PHE CB C 13 40.361 . . 1 . . . . . . . . 4554 1 649 . 1 1 140 140 PHE C C 13 174.555 . . 1 . . . . . . . . 4554 1 650 . 1 1 141 141 HIS N N 15 123.125 . . 1 . . . . . . . . 4554 1 651 . 1 1 141 141 HIS H H 1 8.203 . . 1 . . . . . . . . 4554 1 652 . 1 1 141 141 HIS CA C 13 54.280 . . 1 . . . . . . . . 4554 1 653 . 1 1 141 141 HIS CB C 13 31.790 . . 1 . . . . . . . . 4554 1 654 . 1 1 141 141 HIS C C 13 172.301 . . 1 . . . . . . . . 4554 1 655 . 1 1 142 142 ASP N N 15 120.304 . . 1 . . . . . . . . 4554 1 656 . 1 1 142 142 ASP H H 1 8.168 . . 1 . . . . . . . . 4554 1 657 . 1 1 142 142 ASP CA C 13 53.300 . . 1 . . . . . . . . 4554 1 658 . 1 1 142 142 ASP CB C 13 42.445 . . 1 . . . . . . . . 4554 1 659 . 1 1 142 142 ASP C C 13 175.786 . . 1 . . . . . . . . 4554 1 660 . 1 1 143 143 ALA N N 15 122.135 . . 1 . . . . . . . . 4554 1 661 . 1 1 143 143 ALA H H 1 8.221 . . 1 . . . . . . . . 4554 1 662 . 1 1 143 143 ALA CA C 13 53.023 . . 1 . . . . . . . . 4554 1 663 . 1 1 143 143 ALA CB C 13 19.125 . . 1 . . . . . . . . 4554 1 664 . 1 1 143 143 ALA C C 13 177.203 . . 1 . . . . . . . . 4554 1 665 . 1 1 144 144 ASP N N 15 121.209 . . 1 . . . . . . . . 4554 1 666 . 1 1 144 144 ASP H H 1 9.149 . . 1 . . . . . . . . 4554 1 667 . 1 1 144 144 ASP CA C 13 53.013 . . 1 . . . . . . . . 4554 1 668 . 1 1 144 144 ASP CB C 13 41.862 . . 1 . . . . . . . . 4554 1 669 . 1 1 144 144 ASP C C 13 177.250 . . 1 . . . . . . . . 4554 1 670 . 1 1 145 145 ALA N N 15 117.949 . . 1 . . . . . . . . 4554 1 671 . 1 1 145 145 ALA H H 1 8.285 . . 1 . . . . . . . . 4554 1 672 . 1 1 145 145 ALA CA C 13 55.011 . . 1 . . . . . . . . 4554 1 673 . 1 1 145 145 ALA CB C 13 18.189 . . 1 . . . . . . . . 4554 1 674 . 1 1 145 145 ALA C C 13 178.829 . . 1 . . . . . . . . 4554 1 675 . 1 1 146 146 GLN N N 15 113.097 . . 1 . . . . . . . . 4554 1 676 . 1 1 146 146 GLN H H 1 7.969 . . 1 . . . . . . . . 4554 1 677 . 1 1 146 146 GLN CA C 13 56.569 . . 1 . . . . . . . . 4554 1 678 . 1 1 146 146 GLN CB C 13 30.929 . . 1 . . . . . . . . 4554 1 679 . 1 1 146 146 GLN C C 13 175.112 . . 1 . . . . . . . . 4554 1 680 . 1 1 147 147 ASN N N 15 119.624 . . 1 . . . . . . . . 4554 1 681 . 1 1 147 147 ASN H H 1 8.257 . . 1 . . . . . . . . 4554 1 682 . 1 1 147 147 ASN CA C 13 52.376 . . 1 . . . . . . . . 4554 1 683 . 1 1 147 147 ASN CB C 13 41.089 . . 1 . . . . . . . . 4554 1 684 . 1 1 147 147 ASN C C 13 173.625 . . 1 . . . . . . . . 4554 1 685 . 1 1 148 148 SER N N 15 117.007 . . 1 . . . . . . . . 4554 1 686 . 1 1 148 148 SER H H 1 9.016 . . 1 . . . . . . . . 4554 1 687 . 1 1 148 148 SER CA C 13 60.746 . . 1 . . . . . . . . 4554 1 688 . 1 1 148 148 SER CB C 13 63.312 . . 1 . . . . . . . . 4554 1 689 . 1 1 148 148 SER C C 13 172.534 . . 1 . . . . . . . . 4554 1 690 . 1 1 149 149 HIS N N 15 117.355 . . 1 . . . . . . . . 4554 1 691 . 1 1 149 149 HIS H H 1 6.926 . . 1 . . . . . . . . 4554 1 692 . 1 1 149 149 HIS CA C 13 53.735 . . 1 . . . . . . . . 4554 1 693 . 1 1 149 149 HIS CB C 13 33.815 . . 1 . . . . . . . . 4554 1 694 . 1 1 149 149 HIS C C 13 173.858 . . 1 . . . . . . . . 4554 1 695 . 1 1 150 150 SER N N 15 113.840 . . 1 . . . . . . . . 4554 1 696 . 1 1 150 150 SER H H 1 8.728 . . 1 . . . . . . . . 4554 1 697 . 1 1 150 150 SER CA C 13 58.416 . . 1 . . . . . . . . 4554 1 698 . 1 1 150 150 SER CB C 13 64.348 . . 1 . . . . . . . . 4554 1 699 . 1 1 150 150 SER C C 13 173.161 . . 1 . . . . . . . . 4554 1 700 . 1 1 151 151 TYR N N 15 114.698 . . 1 . . . . . . . . 4554 1 701 . 1 1 151 151 TYR H H 1 7.650 . . 1 . . . . . . . . 4554 1 702 . 1 1 151 151 TYR CA C 13 54.796 . . 1 . . . . . . . . 4554 1 703 . 1 1 151 151 TYR CB C 13 39.211 . . 1 . . . . . . . . 4554 1 704 . 1 1 151 151 TYR C C 13 172.232 . . 1 . . . . . . . . 4554 1 705 . 1 1 152 152 CYS N N 15 118.531 . . 1 . . . . . . . . 4554 1 706 . 1 1 152 152 CYS H H 1 8.318 . . 1 . . . . . . . . 4554 1 707 . 1 1 152 152 CYS CA C 13 55.246 . . 1 . . . . . . . . 4554 1 708 . 1 1 152 152 CYS CB C 13 30.113 . . 1 . . . . . . . . 4554 1 709 . 1 1 152 152 CYS C C 13 174.113 . . 1 . . . . . . . . 4554 1 710 . 1 1 153 153 PHE N N 15 128.452 . . 1 . . . . . . . . 4554 1 711 . 1 1 153 153 PHE H H 1 8.390 . . 1 . . . . . . . . 4554 1 712 . 1 1 153 153 PHE CA C 13 55.579 . . 1 . . . . . . . . 4554 1 713 . 1 1 153 153 PHE CB C 13 40.112 . . 1 . . . . . . . . 4554 1 714 . 1 1 153 153 PHE C C 13 175.066 . . 1 . . . . . . . . 4554 1 715 . 1 1 154 154 GLU N N 15 124.254 . . 1 . . . . . . . . 4554 1 716 . 1 1 154 154 GLU H H 1 9.866 . . 1 . . . . . . . . 4554 1 717 . 1 1 154 154 GLU CA C 13 54.515 . . 1 . . . . . . . . 4554 1 718 . 1 1 154 154 GLU CB C 13 35.075 . . 1 . . . . . . . . 4554 1 719 . 1 1 154 154 GLU C C 13 174.601 . . 1 . . . . . . . . 4554 1 720 . 1 1 155 155 ILE N N 15 123.751 . . 1 . . . . . . . . 4554 1 721 . 1 1 155 155 ILE H H 1 8.700 . . 1 . . . . . . . . 4554 1 722 . 1 1 155 155 ILE CA C 13 60.162 . . 1 . . . . . . . . 4554 1 723 . 1 1 155 155 ILE CB C 13 40.260 . . 1 . . . . . . . . 4554 1 724 . 1 1 155 155 ILE C C 13 175.159 . . 1 . . . . . . . . 4554 1 725 . 1 1 156 156 LEU N N 15 125.884 . . 1 . . . . . . . . 4554 1 726 . 1 1 156 156 LEU H H 1 9.325 . . 1 . . . . . . . . 4554 1 727 . 1 1 156 156 LEU CA C 13 53.291 . . 1 . . . . . . . . 4554 1 728 . 1 1 156 156 LEU CB C 13 45.662 . . 1 . . . . . . . . 4554 1 729 . 1 1 156 156 LEU C C 13 175.902 . . 1 . . . . . . . . 4554 1 730 . 1 1 157 157 GLU N N 15 119.589 . . 1 . . . . . . . . 4554 1 731 . 1 1 157 157 GLU H H 1 9.380 . . 1 . . . . . . . . 4554 1 732 . 1 1 157 157 GLU CA C 13 54.483 . . 1 . . . . . . . . 4554 1 733 . 1 1 157 157 GLU CB C 13 33.570 . . 1 . . . . . . . . 4554 1 734 . 1 1 157 157 GLU C C 13 176.251 . . 1 . . . . . . . . 4554 1 735 . 1 1 158 158 ARG N N 15 127.120 . . 1 . . . . . . . . 4554 1 736 . 1 1 158 158 ARG H H 1 8.323 . . 1 . . . . . . . . 4554 1 737 . 1 1 158 158 ARG CA C 13 57.378 . . 1 . . . . . . . . 4554 1 738 . 1 1 158 158 ARG CB C 13 30.711 . . 1 . . . . . . . . 4554 1 739 . 1 1 158 158 ARG C C 13 176.460 . . 1 . . . . . . . . 4554 1 740 . 1 1 159 159 ARG N N 15 131.571 . . 1 . . . . . . . . 4554 1 741 . 1 1 159 159 ARG H H 1 8.040 . . 1 . . . . . . . . 4554 1 742 . 1 1 159 159 ARG CA C 13 58.741 . . 1 . . . . . . . . 4554 1 743 . 1 1 159 159 ARG CB C 13 30.970 . . 1 . . . . . . . . 4554 1 stop_ save_