data_4886 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4886 _Entry.Title ; Backbone 1H and 15N and 1HB chemical shift assignments for Azotobacter vinelandii C69A apoflavodoxin ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-10-26 _Entry.Accession_date 2000-10-26 _Entry.Last_release_date 2000-12-04 _Entry.Original_release_date 2000-12-04 _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 Elles Steensma . . . 4886 2 Carlo 'van Mierlo' . P.M. . 4886 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4886 coupling_constants 1 4886 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 524 4886 '15N chemical shifts' 146 4886 'coupling constants' 76 4886 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 . . 2000-12-04 2000-10-26 original author . 4886 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 376 . 4886 BMRB 1379 . 4886 BMRB 4881 . 4886 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4886 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98411455 _Citation.DOI . _Citation.PubMed_ID 9737928 _Citation.Full_citation . _Citation.Title ; Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of Molecular Biology' _Citation.Journal_volume 282 _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 653 _Citation.Page_last 666 _Citation.Year 1998 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Elles Steensma . . . 4886 1 2 Carlo 'van Mierlo' . P.M. . 4886 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID apoflavodoxin 4886 1 'hydrogen/deuterium exchange' 4886 1 'protein stability' 4886 1 'protein folding' 4886 1 'NMR spectroscopy' 4886 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4886 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9737928 _Citation.Full_citation ; Steensma E, van Mierlo CP. Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology. ; _Citation.Title 'Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 282 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 653 _Citation.Page_last 666 _Citation.Year 1998 _Citation.Details ; The structural characteristics of Azotobacter vinelandii apoflavodoxin II have been determined using multidimensional NMR spectroscopy. Apoflavodoxin has a stable, well-ordered core but its flavin binding region is flexible. The local stability of apoflavodoxin was probed using hydrogen/deuterium exchange measurements. The existence of an apoflavodoxin equilibrium folding intermediate is inferred from the non-coincidence of CD and fluorescence unfolding curves obtained for the guanidinium hydrochloride induced unfolding of apoflavodoxin. We suggest that the structured part of the putative intermediate is composed of the elements of secondary structure which have the slowest exchanging amide protons in the native protein. These elements are strands beta1, beta3, beta4 and beta5a and helices alpha4 and alpha5. We propose that it is a general feature of flavodoxins that the stable nucleus resides in the C-terminal part of these proteins. The results on flavodoxin are compared with those on two sequentially unrelated proteins sharing the flavodoxin-like fold: Che Y and cutinase. It is shown that the stable nucleus is found in different parts of the flavodoxin-like topology. ; 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 E. Steensma E. . . 4886 2 2 'C. P.' 'van Mierlo' C. P. . 4886 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4886 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9521106 _Citation.Full_citation ; Steensma E, Nijman MJ, Bollen YJ, de Jager PA, van den Berg WA, van Dongen WM, van Mierlo CP. Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding. ; _Citation.Title 'Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 7 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 306 _Citation.Page_last 317 _Citation.Year 1998 _Citation.Details ; As a first step to determine the folding pathway of a protein with an alpha/beta doubly wound topology, the 1H, 13C, and 15N backbone chemical shifts of Azotobacter vinelandii holoflavodoxin II (179 residues) have been determined using multidimensional NMR spectroscopy. Its secondary structure is shown to contain a five-stranded parallel beta-sheet (beta2-beta1-beta3-beta4-beta5) and five alpha-helices. Exchange rates for the individual amide protons of holoflavodoxin were determined using the hydrogen exchange method. The amide protons of 65 residues distributed throughout the structure of holoflavodoxin exchange slowly at pH* 6.2 [kex < 10(-5) s(-1)] and can be used as probes in future folding studies. Measured exchange rates relate to apparent local free energies for transient opening. We propose that the amide protons in the core of holoflavodoxin only exchange by global unfolding of the apo state of the protein. The results obtained are discussed with respect to their implications for flavodoxin folding and for modulation of the flavin redox potential by the apoprotein. We do not find any evidence that A. vinelandii holoflavodoxin II is divided into two subdomains based on its amide proton exchange rates, as opposed to what is found for the structurally but not sequentially homologous alpha/beta doubly wound protein Che Y. ; 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 E. Steensma E. . . 4886 3 2 'M. J.' Nijman M. J. . 4886 3 3 'Y. J.' Bollen Y. J. . 4886 3 4 'P. A.' 'de Jager' P. A. . 4886 3 5 'W. A.' 'van den Berg' W. A. . 4886 3 6 'W. M.' 'van Dongen' W. M. . 4886 3 7 'C. P.' 'van Mierlo' C. P. . 4886 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4886 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9827999 _Citation.Full_citation ; van Mierlo CP, van Dongen WM, Vergeldt F, van Berkel WJ, Steensma E. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate. ; _Citation.Title 'The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 7 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 2331 _Citation.Page_last 2344 _Citation.Year 1998 _Citation.Details ; A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of alpha/beta doubly wound proteins. The guanidinium hydrochloride induced unfolding of apoflavodoxin is demonstrated to be reversible. Apoflavodoxin thus can fold in the absence of the FMN cofactor. The unfolding curves obtained for wild-type, C69A and C69S apoflavodoxin as monitored by circular dichroism and fluorescence spectroscopy do not coincide. Apoflavodoxin unfolding occurs therefore not via a simple two-state mechanism. The experimental data can be described by a three-state mechanism of apoflavodoxin equilibrium unfolding in which a relatively stable intermediate is involved. The intermediate species lacks the characteristic tertiary structure of native apoflavodoxin as deduced from fluorescence spectroscopy, but has significant secondary structure as inferred from circular dichroism spectroscopy. Both spectroscopic techniques show that thermally-induced unfolding of apoflavodoxin also proceeds through formation of a similar molten globule-like species. Thermal unfolding of apoflavodoxin is accompanied by anomalous circular dichroism characteristics: the negative ellipticity at 222 nM increases in the transition zone of unfolding. This effect is most likely attributable to changes in tertiary interactions of aromatic side chains upon protein unfolding. From the presented results and hydrogen/deuterium exchange data, a model for the equilibrium unfolding of apoflavodoxin is presented. ; 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. P.' 'van Mierlo' C. P. . 4886 4 2 'W. M.' 'van Dongen' W. M. . 4886 4 3 F. Vergeldt F. . . 4886 4 4 'W. J.' 'van Berkel' W. J. . 4886 4 5 E. Steensma E. . . 4886 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4886 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8631324 _Citation.Full_citation ; Steensma E, Heering HA, Hagen WR, Van Mierlo CP. Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,. ; _Citation.Title 'Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 235 _Citation.Journal_issue 1-2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 167 _Citation.Page_last 172 _Citation.Year 1996 _Citation.Details ; This study deals with the detailed electrochemistry and complete EPR-monitored titrations of flavodoxin II of Azotobacter vinelandii (ATCC 478). Since wild-type flavodoxin dimerises via intermolecular disulphide bond formation between Cys69 residues, Cys69 has been replaced by both an alanine and a serine residue. Redox properties of the C69A and C69S flavodoxin mutants were compared to those of wild-type flavodoxin. In the presence of the promotor neomycin, C69A and C69S flavodoxin showed a reversible response of the semiquinone/hydroquinone couple at the glassy carbon electrode. However, the addition of dithiothreitol proved to be necessary for the stabilisation of the wild-type flavodoxin response. EPR-monitored redox titrations of wild-type and C69A flavodoxin at high and low pH confirmed the redox potentials measured using cyclic voltammetry. The pH dependence of the semiquinone/hydroquinone redox potentials cannot be described using a model assuming one redox-linked pK. Instead, the presence of at least two redox-linked protonation sites is suggested: pKred.1 = 5.39 +/- 0.08, pKox = 7.29 +/- 0.14, and pKred.2 = 7.84 +/- 0.14 with Em.7 = -459 +/- 4 mV, and a constant redox potential at high pH of -485 +/- 4 mV. The dependence of the semiquinone/hydroquinone redox potential on temperature is -0.5 +/- 0.1 mV . K(-1), yielding delta H degrees = 28.6 +/- 1.5 kJ . mol(1) and delta S degrees = -50.0 +/- 6.2 J . mol(-1) . K(-1). No significant differences in redox properties of wild-type, C69A, and C69S flavodoxin were observed. The electrochemical data suggest that replacement of Cys69 in the vicinity of the FMN by either an alanine or a serine residue does not alter the dielectric properties and structure of A. vinelandii flavodoxin II. ; 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 E. Steensma E. . . 4886 5 2 'H. A.' Heering H. A. . 4886 5 3 'W. R.' Hagen W. R. . 4886 5 4 'C. P.' 'Van Mierlo' C. P. . 4886 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4886 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; van Mierlo, C.P.M. and Steensma, E.; Journal of Molecular Catalysis B: Enzymatic 7 (1999) 147-156. Stabilisation centres differ between structurally homologous proteins as shown by NMR spectroscopy ; _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 4886 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10867188 _Citation.Full_citation ; van Mierlo CP, Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. ; _Citation.Title 'Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biotechnol.' _Citation.Journal_name_full 'Journal of biotechnology' _Citation.Journal_volume 79 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0168-1656 _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 281 _Citation.Page_last 298 _Citation.Year 2000 _Citation.Details ; In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing so, three main spectroscopic techniques used to investigate protein folding and stability are briefly introduced. These techniques are: circular dichroism (CD) spectroscopy, fluorescence emission spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy in combination with the hydrogen exchange methodology. Results on the denaturant-induced and thermal equilibrium unfolding of apoflavodoxin from A. vinelandii, i.e. flavodoxin in the absence of the riboflavin-5'-monophosphate (FMN) cofactor, are discussed. A scheme for the equilibrium unfolding of apoflavodoxin is presented which involves a relatively stable molten globule-like intermediate. Denaturant-induced apoflavodoxin (un)folding as followed at the residue-level by NMR shows that the transition of native A. vinelandii apoflavodoxin to its molten globule state is highly co-operative. However, the unfolding of the molten globule to the unfolded state of the protein is non-co-operative. A comparison of the folding of A. vinelandii flavodoxin with the folding of flavodoxin from Anaboena PCC 7119 is made. The local stabilities of apo- and holoflavodoxin from A. vinelandii as measured by NMR spectroscopy are compared. Both Che Y and cutinase, which have no sequence homology with apoflavodoxin but which share the flavodoxin-like topology, have stabilisation centres different from that of apoflavodoxin from A. vinelandii. The stable centres of structurally similar proteins can thus reside in different parts of the same protein topology. Insight in the variations in (local) unfolding processes of structurally similar proteins can be used to stabilise proteins with a flavodoxin-like fold. Finally, the importance of some recent experimental and theoretical developments for the study of flavodoxin folding is briefly discussed. ; 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. P.' 'van Mierlo' C. P. . 4886 7 2 E. Steensma E. . . 4886 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 4886 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10739257 _Citation.Full_citation ; van Mierlo CP, van den Oever JM, Steensma E. Apoflavodoxin (un)folding followed at the residue level by NMR. ; _Citation.Title 'Apoflavodoxin (un)folding followed at the residue level by NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 9 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 145 _Citation.Page_last 157 _Citation.Year 2000 _Citation.Details ; The denaturant-induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR spectroscopy. NH groups of 21 residues of the protein could be followed in a series of 1H-15N heteronuclear single-quantum coherence spectra recorded at increasing concentrations of guanidinium hydrochloride despite the formation of protein aggregate. These NH groups are distributed throughout the whole apoflavodoxin structure. The midpoints of unfolding determined by NMR coincide with the one obtained by fluorescence emission spectroscopy. Both techniques give rise to unfolding curves with transition zones at significantly lower denaturant concentrations than the one obtained by circular dichroism spectroscopy. The NMR (un)folding data support a mechanism for apoflavodoxin folding in which a relatively stable intermediate is involved. Native apoflavodoxin is shown to cooperatively unfold to a molten globule-like state with extremely broadened NMR resonances. This initial unfolding step is slow on the NMR chemical shift timescale. The subsequent unfolding of the molten globule is faster on the NMR chemical shift timescale and the limited appearance of 1H-15N HSQC cross peaks of unfolded apoflavodoxin in the denaturant range studied indicates that it is noncooperative. ; 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. P.' 'van Mierlo' C. P. . 4886 8 2 'J. M.' 'van den Oever' J. M. . 4886 8 3 E. Steensma E. . . 4886 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 4886 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 889809 _Citation.Full_citation ; Tanaka M, Haniu M, Yasunobu KT, Yoch DC. Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii. ; _Citation.Title 'Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 16 _Citation.Journal_issue 16 _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 3525 _Citation.Page_last 3537 _Citation.Year 1977 _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 M. Tanaka M. . . 4886 9 2 M. Haniu M. . . 4886 9 3 'K. T.' Yasunobu K. T. . 4886 9 4 'D. C.' Yoch D. C. . 4886 9 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_apoflavodoxin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_apoflavodoxin _Assembly.Entry_ID 4886 _Assembly.ID 1 _Assembly.Name 'Azotobacter vinelandii C69A apoflavodoxin II' _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 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4886 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 'C69A apoflavodoxin' 1 $apoflavodoxin . . . native . . . . . 4886 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Azotobacter vinelandii C69A apoflavodoxin II' system 4886 1 apoflavodoxin abbreviation 4886 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'holoflavodoxin is an electron transfer protein' 4886 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_apoflavodoxin _Entity.Sf_category entity _Entity.Sf_framecode apoflavodoxin _Entity.Entry_ID 4886 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Azotobacter vinelandii apoflavodoxin II' _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 ; AKIGLFFGSNTGKTRKVAKS IKKRFDDETMSDALNVNRVS AEDFAQYQFLILGTPTLGEG ELPGLSSDAENESWEEFLPK IEGLDFSGKTVALFGLGDQV GYPENYLDALGELYSFFKDR GAKIVGSWSTDGYEFESSEA VVDGKFVGLALDLDNQSGKT DERVAAWLAQIAPEFGLSL ; _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 179 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 20000 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 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 15474 . Apoflavodoxin . . . . . 100.00 179 100.00 100.00 6.44e-123 . . . . 4886 1 2 no BMRB 17465 . aII . . . . . 100.00 179 100.00 100.00 6.44e-123 . . . . 4886 1 3 no BMRB 4881 . holoflavodoxin . . . . . 100.00 179 100.00 100.00 6.44e-123 . . . . 4886 1 4 no PDB 1YOB . "C69a Flavodoxin Ii From Azotobacter Vinelandii" . . . . . 100.00 179 100.00 100.00 6.44e-123 . . . . 4886 1 5 no GB AAA22154 . "flavodoxin [Azotobacter vinelandii]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 6 no GB AAA64735 . "flavodoxin (nifF) [Azotobacter vinelandii]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 7 no GB ACO76434 . "Flavodoxin, nifF [Azotobacter vinelandii DJ]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 8 no GB AGK13779 . "Flavodoxin, nifF [Azotobacter vinelandii CA]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 9 no GB AGK18380 . "Flavodoxin, nifF [Azotobacter vinelandii CA6]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 10 no PRF 752055A . flavodoxin . . . . . 100.00 179 98.88 99.44 9.59e-122 . . . . 4886 1 11 no REF WP_012698862 . "flavodoxin [Azotobacter vinelandii]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 12 no REF YP_002797409 . "Flavodoxin, nifF [Azotobacter vinelandii DJ]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 13 no REF YP_007891221 . "Flavodoxin, nifF [Azotobacter vinelandii CA]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 14 no REF YP_007896269 . "Flavodoxin, nifF [Azotobacter vinelandii CA6]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 15 no SP P00324 . "RecName: Full=Flavodoxin-2 [Azotobacter vinelandii]" . . . . . 100.00 180 99.44 99.44 1.67e-122 . . . . 4886 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Azotobacter vinelandii apoflavodoxin II' common 4886 1 C69A variant 4886 1 apoflavodoxin abbreviation 4886 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 . ALA . 4886 1 2 . LYS . 4886 1 3 . ILE . 4886 1 4 . GLY . 4886 1 5 . LEU . 4886 1 6 . PHE . 4886 1 7 . PHE . 4886 1 8 . GLY . 4886 1 9 . SER . 4886 1 10 . ASN . 4886 1 11 . THR . 4886 1 12 . GLY . 4886 1 13 . LYS . 4886 1 14 . THR . 4886 1 15 . ARG . 4886 1 16 . LYS . 4886 1 17 . VAL . 4886 1 18 . ALA . 4886 1 19 . LYS . 4886 1 20 . SER . 4886 1 21 . ILE . 4886 1 22 . LYS . 4886 1 23 . LYS . 4886 1 24 . ARG . 4886 1 25 . PHE . 4886 1 26 . ASP . 4886 1 27 . ASP . 4886 1 28 . GLU . 4886 1 29 . THR . 4886 1 30 . MET . 4886 1 31 . SER . 4886 1 32 . ASP . 4886 1 33 . ALA . 4886 1 34 . LEU . 4886 1 35 . ASN . 4886 1 36 . VAL . 4886 1 37 . ASN . 4886 1 38 . ARG . 4886 1 39 . VAL . 4886 1 40 . SER . 4886 1 41 . ALA . 4886 1 42 . GLU . 4886 1 43 . ASP . 4886 1 44 . PHE . 4886 1 45 . ALA . 4886 1 46 . GLN . 4886 1 47 . TYR . 4886 1 48 . GLN . 4886 1 49 . PHE . 4886 1 50 . LEU . 4886 1 51 . ILE . 4886 1 52 . LEU . 4886 1 53 . GLY . 4886 1 54 . THR . 4886 1 55 . PRO . 4886 1 56 . THR . 4886 1 57 . LEU . 4886 1 58 . GLY . 4886 1 59 . GLU . 4886 1 60 . GLY . 4886 1 61 . GLU . 4886 1 62 . LEU . 4886 1 63 . PRO . 4886 1 64 . GLY . 4886 1 65 . LEU . 4886 1 66 . SER . 4886 1 67 . SER . 4886 1 68 . ASP . 4886 1 69 . ALA . 4886 1 70 . GLU . 4886 1 71 . ASN . 4886 1 72 . GLU . 4886 1 73 . SER . 4886 1 74 . TRP . 4886 1 75 . GLU . 4886 1 76 . GLU . 4886 1 77 . PHE . 4886 1 78 . LEU . 4886 1 79 . PRO . 4886 1 80 . LYS . 4886 1 81 . ILE . 4886 1 82 . GLU . 4886 1 83 . GLY . 4886 1 84 . LEU . 4886 1 85 . ASP . 4886 1 86 . PHE . 4886 1 87 . SER . 4886 1 88 . GLY . 4886 1 89 . LYS . 4886 1 90 . THR . 4886 1 91 . VAL . 4886 1 92 . ALA . 4886 1 93 . LEU . 4886 1 94 . PHE . 4886 1 95 . GLY . 4886 1 96 . LEU . 4886 1 97 . GLY . 4886 1 98 . ASP . 4886 1 99 . GLN . 4886 1 100 . VAL . 4886 1 101 . GLY . 4886 1 102 . TYR . 4886 1 103 . PRO . 4886 1 104 . GLU . 4886 1 105 . ASN . 4886 1 106 . TYR . 4886 1 107 . LEU . 4886 1 108 . ASP . 4886 1 109 . ALA . 4886 1 110 . LEU . 4886 1 111 . GLY . 4886 1 112 . GLU . 4886 1 113 . LEU . 4886 1 114 . TYR . 4886 1 115 . SER . 4886 1 116 . PHE . 4886 1 117 . PHE . 4886 1 118 . LYS . 4886 1 119 . ASP . 4886 1 120 . ARG . 4886 1 121 . GLY . 4886 1 122 . ALA . 4886 1 123 . LYS . 4886 1 124 . ILE . 4886 1 125 . VAL . 4886 1 126 . GLY . 4886 1 127 . SER . 4886 1 128 . TRP . 4886 1 129 . SER . 4886 1 130 . THR . 4886 1 131 . ASP . 4886 1 132 . GLY . 4886 1 133 . TYR . 4886 1 134 . GLU . 4886 1 135 . PHE . 4886 1 136 . GLU . 4886 1 137 . SER . 4886 1 138 . SER . 4886 1 139 . GLU . 4886 1 140 . ALA . 4886 1 141 . VAL . 4886 1 142 . VAL . 4886 1 143 . ASP . 4886 1 144 . GLY . 4886 1 145 . LYS . 4886 1 146 . PHE . 4886 1 147 . VAL . 4886 1 148 . GLY . 4886 1 149 . LEU . 4886 1 150 . ALA . 4886 1 151 . LEU . 4886 1 152 . ASP . 4886 1 153 . LEU . 4886 1 154 . ASP . 4886 1 155 . ASN . 4886 1 156 . GLN . 4886 1 157 . SER . 4886 1 158 . GLY . 4886 1 159 . LYS . 4886 1 160 . THR . 4886 1 161 . ASP . 4886 1 162 . GLU . 4886 1 163 . ARG . 4886 1 164 . VAL . 4886 1 165 . ALA . 4886 1 166 . ALA . 4886 1 167 . TRP . 4886 1 168 . LEU . 4886 1 169 . ALA . 4886 1 170 . GLN . 4886 1 171 . ILE . 4886 1 172 . ALA . 4886 1 173 . PRO . 4886 1 174 . GLU . 4886 1 175 . PHE . 4886 1 176 . GLY . 4886 1 177 . LEU . 4886 1 178 . SER . 4886 1 179 . LEU . 4886 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 . ALA 1 1 4886 1 . LYS 2 2 4886 1 . ILE 3 3 4886 1 . GLY 4 4 4886 1 . LEU 5 5 4886 1 . PHE 6 6 4886 1 . PHE 7 7 4886 1 . GLY 8 8 4886 1 . SER 9 9 4886 1 . ASN 10 10 4886 1 . THR 11 11 4886 1 . GLY 12 12 4886 1 . LYS 13 13 4886 1 . THR 14 14 4886 1 . ARG 15 15 4886 1 . LYS 16 16 4886 1 . VAL 17 17 4886 1 . ALA 18 18 4886 1 . LYS 19 19 4886 1 . SER 20 20 4886 1 . ILE 21 21 4886 1 . LYS 22 22 4886 1 . LYS 23 23 4886 1 . ARG 24 24 4886 1 . PHE 25 25 4886 1 . ASP 26 26 4886 1 . ASP 27 27 4886 1 . GLU 28 28 4886 1 . THR 29 29 4886 1 . MET 30 30 4886 1 . SER 31 31 4886 1 . ASP 32 32 4886 1 . ALA 33 33 4886 1 . LEU 34 34 4886 1 . ASN 35 35 4886 1 . VAL 36 36 4886 1 . ASN 37 37 4886 1 . ARG 38 38 4886 1 . VAL 39 39 4886 1 . SER 40 40 4886 1 . ALA 41 41 4886 1 . GLU 42 42 4886 1 . ASP 43 43 4886 1 . PHE 44 44 4886 1 . ALA 45 45 4886 1 . GLN 46 46 4886 1 . TYR 47 47 4886 1 . GLN 48 48 4886 1 . PHE 49 49 4886 1 . LEU 50 50 4886 1 . ILE 51 51 4886 1 . LEU 52 52 4886 1 . GLY 53 53 4886 1 . THR 54 54 4886 1 . PRO 55 55 4886 1 . THR 56 56 4886 1 . LEU 57 57 4886 1 . GLY 58 58 4886 1 . GLU 59 59 4886 1 . GLY 60 60 4886 1 . GLU 61 61 4886 1 . LEU 62 62 4886 1 . PRO 63 63 4886 1 . GLY 64 64 4886 1 . LEU 65 65 4886 1 . SER 66 66 4886 1 . SER 67 67 4886 1 . ASP 68 68 4886 1 . ALA 69 69 4886 1 . GLU 70 70 4886 1 . ASN 71 71 4886 1 . GLU 72 72 4886 1 . SER 73 73 4886 1 . TRP 74 74 4886 1 . GLU 75 75 4886 1 . GLU 76 76 4886 1 . PHE 77 77 4886 1 . LEU 78 78 4886 1 . PRO 79 79 4886 1 . LYS 80 80 4886 1 . ILE 81 81 4886 1 . GLU 82 82 4886 1 . GLY 83 83 4886 1 . LEU 84 84 4886 1 . ASP 85 85 4886 1 . PHE 86 86 4886 1 . SER 87 87 4886 1 . GLY 88 88 4886 1 . LYS 89 89 4886 1 . THR 90 90 4886 1 . VAL 91 91 4886 1 . ALA 92 92 4886 1 . LEU 93 93 4886 1 . PHE 94 94 4886 1 . GLY 95 95 4886 1 . LEU 96 96 4886 1 . GLY 97 97 4886 1 . ASP 98 98 4886 1 . GLN 99 99 4886 1 . VAL 100 100 4886 1 . GLY 101 101 4886 1 . TYR 102 102 4886 1 . PRO 103 103 4886 1 . GLU 104 104 4886 1 . ASN 105 105 4886 1 . TYR 106 106 4886 1 . LEU 107 107 4886 1 . ASP 108 108 4886 1 . ALA 109 109 4886 1 . LEU 110 110 4886 1 . GLY 111 111 4886 1 . GLU 112 112 4886 1 . LEU 113 113 4886 1 . TYR 114 114 4886 1 . SER 115 115 4886 1 . PHE 116 116 4886 1 . PHE 117 117 4886 1 . LYS 118 118 4886 1 . ASP 119 119 4886 1 . ARG 120 120 4886 1 . GLY 121 121 4886 1 . ALA 122 122 4886 1 . LYS 123 123 4886 1 . ILE 124 124 4886 1 . VAL 125 125 4886 1 . GLY 126 126 4886 1 . SER 127 127 4886 1 . TRP 128 128 4886 1 . SER 129 129 4886 1 . THR 130 130 4886 1 . ASP 131 131 4886 1 . GLY 132 132 4886 1 . TYR 133 133 4886 1 . GLU 134 134 4886 1 . PHE 135 135 4886 1 . GLU 136 136 4886 1 . SER 137 137 4886 1 . SER 138 138 4886 1 . GLU 139 139 4886 1 . ALA 140 140 4886 1 . VAL 141 141 4886 1 . VAL 142 142 4886 1 . ASP 143 143 4886 1 . GLY 144 144 4886 1 . LYS 145 145 4886 1 . PHE 146 146 4886 1 . VAL 147 147 4886 1 . GLY 148 148 4886 1 . LEU 149 149 4886 1 . ALA 150 150 4886 1 . LEU 151 151 4886 1 . ASP 152 152 4886 1 . LEU 153 153 4886 1 . ASP 154 154 4886 1 . ASN 155 155 4886 1 . GLN 156 156 4886 1 . SER 157 157 4886 1 . GLY 158 158 4886 1 . LYS 159 159 4886 1 . THR 160 160 4886 1 . ASP 161 161 4886 1 . GLU 162 162 4886 1 . ARG 163 163 4886 1 . VAL 164 164 4886 1 . ALA 165 165 4886 1 . ALA 166 166 4886 1 . TRP 167 167 4886 1 . LEU 168 168 4886 1 . ALA 169 169 4886 1 . GLN 170 170 4886 1 . ILE 171 171 4886 1 . ALA 172 172 4886 1 . PRO 173 173 4886 1 . GLU 174 174 4886 1 . PHE 175 175 4886 1 . GLY 176 176 4886 1 . LEU 177 177 4886 1 . SER 178 178 4886 1 . LEU 179 179 4886 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4886 _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 $apoflavodoxin . 354 organism . 'Azotobacter vinelandii' . . . Eubacteria . Azotobacter vinelandii . . . . . . . . 478 . . . . . . . . . . . . 4886 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 4886 _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 $apoflavodoxin . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli TG2 . . . . . . . . . . . . . . . . . . . . . . 4886 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4886 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; A hydrogen/deuterium exchange experiment was carried out in 150 mM potassium pyrophosphate and 100% D2O ; _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 'Azotobacter vinelandii apoflavodoxin II' [U-15N] . . 1 $apoflavodoxin . . 2 . . mM . . . . 4886 1 2 'potassium pyrophosphate' . . . . . . . 150 . . mM . . . . 4886 1 3 H2O . . . . . . . 90 . . % . . . . 4886 1 4 D2O . . . . . . . 10 . . % . . . . 4886 1 stop_ save_ ####################### # Sample conditions # ####################### save_Conditions_sample_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Conditions_sample_1 _Sample_condition_list.Entry_ID 4886 _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* 6.0 0.1 n/a 4886 1 temperature 303 0.5 K 4886 1 'ionic strength' 0.3 0.03 M 4886 1 stop_ save_ ############################ # Computer software used # ############################ save_Felix _Software.Sf_category software _Software.Sf_framecode Felix _Software.Entry_ID 4886 _Software.ID 1 _Software.Name Felix _Software.Version 2.3 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'processing of data' 4886 1 stop_ save_ save_Xeasy _Software.Sf_category software _Software.Sf_framecode Xeasy _Software.Entry_ID 4886 _Software.ID 2 _Software.Name Xeasy _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectral analysis' 4886 2 'peak assignment' 4886 2 'measurement peak heights' 4886 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4886 _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_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4886 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker AMX . 500 . . . 4886 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 4886 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '1H-15N HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 2 ct-HNHA . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 3 ct-HNHB . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 4 TOCSY-HMQC . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 5 HMQC-NOESY-HSQC . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 6 NOESY-HSQC . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 7 'triple-resonance 5 mm inverse probe with a self-shielded z-gradient' . . . . . . . . . . . 1 $sample_1 . . . 1 $Conditions_sample_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4886 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4886 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details ; 1H chemical shifts were referenced using internal TSP as a standard and pH-corrected values are reported here in ppm relative to DSS TSP is the internal chemical shift reference since this compound was present in the sample. However, the values reported are in ppm relative to DSS. The referencing for entry 4886 is similar to that for entry 4881. ; 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 1.000000000 . . . . . . . . . 4886 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4886 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_shifts_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shifts_set_1 _Assigned_chem_shift_list.Entry_ID 4886 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Conditions_sample_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4886 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 ALA HA H 1 4.26 0.02 . 9 . . . . . . . . 4886 1 2 . 1 1 1 1 ALA HB1 H 1 1.46 0.02 . 9 . . . . . . . . 4886 1 3 . 1 1 1 1 ALA HB2 H 1 1.46 0.02 . 9 . . . . . . . . 4886 1 4 . 1 1 1 1 ALA HB3 H 1 1.46 0.02 . 9 . . . . . . . . 4886 1 5 . 1 1 2 2 LYS N N 15 120.9 0.1 . 1 . . . . . . . . 4886 1 6 . 1 1 2 2 LYS H H 1 7.68 0.02 . 1 . . . . . . . . 4886 1 7 . 1 1 2 2 LYS HA H 1 4.38 0.02 . 1 . . . . . . . . 4886 1 8 . 1 1 2 2 LYS HB2 H 1 2.25 0.02 . 2 . . . . . . . . 4886 1 9 . 1 1 2 2 LYS HB3 H 1 1.59 0.02 . 2 . . . . . . . . 4886 1 10 . 1 1 3 3 ILE N N 15 117.5 0.1 . 1 . . . . . . . . 4886 1 11 . 1 1 3 3 ILE H H 1 8.18 0.02 . 1 . . . . . . . . 4886 1 12 . 1 1 3 3 ILE HA H 1 4.81 0.02 . 1 . . . . . . . . 4886 1 13 . 1 1 3 3 ILE HB H 1 1.76 0.02 . 1 . . . . . . . . 4886 1 14 . 1 1 4 4 GLY N N 15 117.6 0.1 . 1 . . . . . . . . 4886 1 15 . 1 1 4 4 GLY H H 1 8.67 0.02 . 1 . . . . . . . . 4886 1 16 . 1 1 4 4 GLY HA2 H 1 3.37 0.02 . 2 . . . . . . . . 4886 1 17 . 1 1 4 4 GLY HA3 H 1 2.06 0.02 . 2 . . . . . . . . 4886 1 18 . 1 1 5 5 LEU N N 15 130.5 0.1 . 1 . . . . . . . . 4886 1 19 . 1 1 5 5 LEU H H 1 7.30 0.02 . 1 . . . . . . . . 4886 1 20 . 1 1 5 5 LEU HA H 1 5.40 0.02 . 1 . . . . . . . . 4886 1 21 . 1 1 5 5 LEU HB2 H 1 1.70 0.02 . 2 . . . . . . . . 4886 1 22 . 1 1 5 5 LEU HB3 H 1 1.02 0.02 . 2 . . . . . . . . 4886 1 23 . 1 1 6 6 PHE N N 15 121.1 0.1 . 1 . . . . . . . . 4886 1 24 . 1 1 6 6 PHE H H 1 8.64 0.02 . 1 . . . . . . . . 4886 1 25 . 1 1 6 6 PHE HA H 1 6.08 0.02 . 1 . . . . . . . . 4886 1 26 . 1 1 6 6 PHE HB2 H 1 2.95 0.02 . 2 . . . . . . . . 4886 1 27 . 1 1 7 7 PHE HA H 1 5.97 0.02 . 1 . . . . . . . . 4886 1 28 . 1 1 7 7 PHE HB2 H 1 3.11 0.02 . 2 . . . . . . . . 4886 1 29 . 1 1 8 8 GLY N N 15 105.9 0.1 . 1 . . . . . . . . 4886 1 30 . 1 1 8 8 GLY H H 1 7.37 0.02 . 1 . . . . . . . . 4886 1 31 . 1 1 8 8 GLY HA2 H 1 4.21 0.02 . 2 . . . . . . . . 4886 1 32 . 1 1 8 8 GLY HA3 H 1 3.32 0.02 . 2 . . . . . . . . 4886 1 33 . 1 1 13 13 LYS HA H 1 4.13 0.02 . 1 . . . . . . . . 4886 1 34 . 1 1 14 14 THR HA H 1 3.68 0.02 . 1 . . . . . . . . 4886 1 35 . 1 1 15 15 ARG HA H 1 2.58 0.02 . 1 . . . . . . . . 4886 1 36 . 1 1 16 16 LYS N N 15 118.9 0.1 . 1 . . . . . . . . 4886 1 37 . 1 1 16 16 LYS H H 1 7.42 0.02 . 1 . . . . . . . . 4886 1 38 . 1 1 16 16 LYS HA H 1 3.87 0.02 . 1 . . . . . . . . 4886 1 39 . 1 1 16 16 LYS HB2 H 1 1.99 0.02 . 2 . . . . . . . . 4886 1 40 . 1 1 17 17 VAL N N 15 119.7 0.1 . 1 . . . . . . . . 4886 1 41 . 1 1 17 17 VAL H H 1 7.61 0.02 . 1 . . . . . . . . 4886 1 42 . 1 1 17 17 VAL HA H 1 3.49 0.02 . 1 . . . . . . . . 4886 1 43 . 1 1 17 17 VAL HB H 1 2.00 0.02 . 1 . . . . . . . . 4886 1 44 . 1 1 18 18 ALA N N 15 122.5 0.1 . 1 . . . . . . . . 4886 1 45 . 1 1 18 18 ALA H H 1 8.37 0.02 . 1 . . . . . . . . 4886 1 46 . 1 1 18 18 ALA HA H 1 3.88 0.02 . 1 . . . . . . . . 4886 1 47 . 1 1 18 18 ALA HB1 H 1 1.38 0.02 . 1 . . . . . . . . 4886 1 48 . 1 1 18 18 ALA HB2 H 1 1.38 0.02 . 1 . . . . . . . . 4886 1 49 . 1 1 18 18 ALA HB3 H 1 1.38 0.02 . 1 . . . . . . . . 4886 1 50 . 1 1 19 19 LYS N N 15 116.8 0.1 . 1 . . . . . . . . 4886 1 51 . 1 1 19 19 LYS H H 1 8.63 0.02 . 1 . . . . . . . . 4886 1 52 . 1 1 19 19 LYS HA H 1 3.87 0.02 . 1 . . . . . . . . 4886 1 53 . 1 1 19 19 LYS HB2 H 1 1.89 0.02 . 2 . . . . . . . . 4886 1 54 . 1 1 20 20 SER N N 15 116.6 0.1 . 1 . . . . . . . . 4886 1 55 . 1 1 20 20 SER H H 1 7.73 0.02 . 1 . . . . . . . . 4886 1 56 . 1 1 20 20 SER HA H 1 4.22 0.02 . 1 . . . . . . . . 4886 1 57 . 1 1 20 20 SER HB2 H 1 4.03 0.02 . 2 . . . . . . . . 4886 1 58 . 1 1 21 21 ILE N N 15 124.1 0.1 . 1 . . . . . . . . 4886 1 59 . 1 1 21 21 ILE H H 1 7.56 0.02 . 1 . . . . . . . . 4886 1 60 . 1 1 21 21 ILE HA H 1 3.61 0.02 . 1 . . . . . . . . 4886 1 61 . 1 1 21 21 ILE HB H 1 2.15 0.02 . 1 . . . . . . . . 4886 1 62 . 1 1 22 22 LYS N N 15 117.8 0.1 . 1 . . . . . . . . 4886 1 63 . 1 1 22 22 LYS H H 1 7.43 0.02 . 1 . . . . . . . . 4886 1 64 . 1 1 22 22 LYS HA H 1 4.58 0.02 . 1 . . . . . . . . 4886 1 65 . 1 1 22 22 LYS HB2 H 1 1.95 0.02 . 2 . . . . . . . . 4886 1 66 . 1 1 23 23 LYS N N 15 116.6 0.1 . 1 . . . . . . . . 4886 1 67 . 1 1 23 23 LYS H H 1 7.66 0.02 . 1 . . . . . . . . 4886 1 68 . 1 1 23 23 LYS HA H 1 4.08 0.02 . 1 . . . . . . . . 4886 1 69 . 1 1 23 23 LYS HB2 H 1 1.95 0.02 . 2 . . . . . . . . 4886 1 70 . 1 1 23 23 LYS HB3 H 1 1.85 0.02 . 2 . . . . . . . . 4886 1 71 . 1 1 24 24 ARG N N 15 114.6 0.1 . 1 . . . . . . . . 4886 1 72 . 1 1 24 24 ARG H H 1 7.10 0.02 . 1 . . . . . . . . 4886 1 73 . 1 1 24 24 ARG HA H 1 3.97 0.02 . 1 . . . . . . . . 4886 1 74 . 1 1 24 24 ARG HB2 H 1 1.12 0.02 . 2 . . . . . . . . 4886 1 75 . 1 1 25 25 PHE N N 15 117.0 0.1 . 1 . . . . . . . . 4886 1 76 . 1 1 25 25 PHE H H 1 8.15 0.02 . 1 . . . . . . . . 4886 1 77 . 1 1 25 25 PHE HA H 1 5.21 0.02 . 1 . . . . . . . . 4886 1 78 . 1 1 25 25 PHE HB2 H 1 3.21 0.02 . 2 . . . . . . . . 4886 1 79 . 1 1 25 25 PHE HB3 H 1 2.81 0.02 . 2 . . . . . . . . 4886 1 80 . 1 1 26 26 ASP N N 15 122.1 0.1 . 1 . . . . . . . . 4886 1 81 . 1 1 26 26 ASP H H 1 8.80 0.02 . 1 . . . . . . . . 4886 1 82 . 1 1 26 26 ASP HA H 1 4.74 0.02 . 1 . . . . . . . . 4886 1 83 . 1 1 26 26 ASP HB2 H 1 3.41 0.02 . 2 . . . . . . . . 4886 1 84 . 1 1 26 26 ASP HB3 H 1 2.87 0.02 . 2 . . . . . . . . 4886 1 85 . 1 1 27 27 ASP N N 15 117.7 0.1 . 1 . . . . . . . . 4886 1 86 . 1 1 27 27 ASP H H 1 8.55 0.02 . 1 . . . . . . . . 4886 1 87 . 1 1 27 27 ASP HA H 1 4.58 0.02 . 1 . . . . . . . . 4886 1 88 . 1 1 27 27 ASP HB2 H 1 2.90 0.02 . 2 . . . . . . . . 4886 1 89 . 1 1 27 27 ASP HB3 H 1 2.75 0.02 . 2 . . . . . . . . 4886 1 90 . 1 1 28 28 GLU N N 15 119.2 0.1 . 1 . . . . . . . . 4886 1 91 . 1 1 28 28 GLU H H 1 8.04 0.02 . 1 . . . . . . . . 4886 1 92 . 1 1 28 28 GLU HA H 1 4.34 0.02 . 1 . . . . . . . . 4886 1 93 . 1 1 28 28 GLU HB2 H 1 2.15 0.02 . 2 . . . . . . . . 4886 1 94 . 1 1 29 29 THR N N 15 118.4 0.1 . 1 . . . . . . . . 4886 1 95 . 1 1 29 29 THR H H 1 8.16 0.02 . 1 . . . . . . . . 4886 1 96 . 1 1 29 29 THR HA H 1 3.95 0.02 . 1 . . . . . . . . 4886 1 97 . 1 1 29 29 THR HB H 1 4.27 0.02 . 1 . . . . . . . . 4886 1 98 . 1 1 30 30 MET N N 15 121.4 0.1 . 1 . . . . . . . . 4886 1 99 . 1 1 30 30 MET H H 1 8.30 0.02 . 1 . . . . . . . . 4886 1 100 . 1 1 30 30 MET HA H 1 5.33 0.02 . 1 . . . . . . . . 4886 1 101 . 1 1 30 30 MET HB2 H 1 1.68 0.02 . 2 . . . . . . . . 4886 1 102 . 1 1 31 31 SER N N 15 124.8 0.1 . 1 . . . . . . . . 4886 1 103 . 1 1 31 31 SER H H 1 8.72 0.02 . 1 . . . . . . . . 4886 1 104 . 1 1 31 31 SER HA H 1 4.41 0.02 . 1 . . . . . . . . 4886 1 105 . 1 1 31 31 SER HB2 H 1 4.29 0.02 . 2 . . . . . . . . 4886 1 106 . 1 1 31 31 SER HB3 H 1 3.90 0.02 . 2 . . . . . . . . 4886 1 107 . 1 1 32 32 ASP N N 15 114.8 0.1 . 1 . . . . . . . . 4886 1 108 . 1 1 32 32 ASP H H 1 7.91 0.02 . 1 . . . . . . . . 4886 1 109 . 1 1 32 32 ASP HA H 1 4.48 0.02 . 1 . . . . . . . . 4886 1 110 . 1 1 32 32 ASP HB2 H 1 2.56 0.02 . 2 . . . . . . . . 4886 1 111 . 1 1 33 33 ALA N N 15 122.9 0.1 . 1 . . . . . . . . 4886 1 112 . 1 1 33 33 ALA H H 1 8.26 0.02 . 1 . . . . . . . . 4886 1 113 . 1 1 33 33 ALA HA H 1 4.13 0.02 . 1 . . . . . . . . 4886 1 114 . 1 1 33 33 ALA HB1 H 1 1.27 0.02 . 1 . . . . . . . . 4886 1 115 . 1 1 33 33 ALA HB2 H 1 1.27 0.02 . 1 . . . . . . . . 4886 1 116 . 1 1 33 33 ALA HB3 H 1 1.27 0.02 . 1 . . . . . . . . 4886 1 117 . 1 1 35 35 ASN ND2 N 15 113.4 0.1 . 1 . . . . . . . . 4886 1 118 . 1 1 35 35 ASN HD21 H 1 6.95 0.02 . 2 . . . . . . . . 4886 1 119 . 1 1 35 35 ASN HD22 H 1 7.72 0.02 . 2 . . . . . . . . 4886 1 120 . 1 1 37 37 ASN ND2 N 15 111.1 0.1 . 9 . . . . . . . . 4886 1 121 . 1 1 37 37 ASN HD21 H 1 6.51 0.02 . 9 . . . . . . . . 4886 1 122 . 1 1 37 37 ASN HD22 H 1 7.10 0.02 . 9 . . . . . . . . 4886 1 123 . 1 1 40 40 SER HB2 H 1 4.50 0.02 . 2 . . . . . . . . 4886 1 124 . 1 1 40 40 SER HB3 H 1 4.16 0.02 . 2 . . . . . . . . 4886 1 125 . 1 1 41 41 ALA N N 15 124.4 0.1 . 1 . . . . . . . . 4886 1 126 . 1 1 41 41 ALA H H 1 9.17 0.02 . 1 . . . . . . . . 4886 1 127 . 1 1 41 41 ALA HA H 1 4.03 0.02 . 1 . . . . . . . . 4886 1 128 . 1 1 41 41 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . 4886 1 129 . 1 1 41 41 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . 4886 1 130 . 1 1 41 41 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . 4886 1 131 . 1 1 42 42 GLU N N 15 115.5 0.1 . 1 . . . . . . . . 4886 1 132 . 1 1 42 42 GLU H H 1 8.56 0.02 . 1 . . . . . . . . 4886 1 133 . 1 1 42 42 GLU HA H 1 4.07 0.02 . 1 . . . . . . . . 4886 1 134 . 1 1 42 42 GLU HB2 H 1 2.14 0.02 . 2 . . . . . . . . 4886 1 135 . 1 1 42 42 GLU HB3 H 1 2.05 0.02 . 2 . . . . . . . . 4886 1 136 . 1 1 43 43 ASP N N 15 120.6 0.1 . 1 . . . . . . . . 4886 1 137 . 1 1 43 43 ASP H H 1 7.93 0.02 . 1 . . . . . . . . 4886 1 138 . 1 1 43 43 ASP HA H 1 4.55 0.02 . 1 . . . . . . . . 4886 1 139 . 1 1 43 43 ASP HB2 H 1 3.17 0.02 . 2 . . . . . . . . 4886 1 140 . 1 1 43 43 ASP HB3 H 1 2.93 0.02 . 2 . . . . . . . . 4886 1 141 . 1 1 44 44 PHE N N 15 121.0 0.1 . 1 . . . . . . . . 4886 1 142 . 1 1 44 44 PHE H H 1 8.31 0.02 . 1 . . . . . . . . 4886 1 143 . 1 1 44 44 PHE HA H 1 4.30 0.02 . 1 . . . . . . . . 4886 1 144 . 1 1 44 44 PHE HB2 H 1 3.47 0.02 . 2 . . . . . . . . 4886 1 145 . 1 1 44 44 PHE HB3 H 1 3.12 0.02 . 2 . . . . . . . . 4886 1 146 . 1 1 45 45 ALA N N 15 116.5 0.1 . 1 . . . . . . . . 4886 1 147 . 1 1 45 45 ALA H H 1 8.36 0.02 . 1 . . . . . . . . 4886 1 148 . 1 1 45 45 ALA HA H 1 4.25 0.02 . 1 . . . . . . . . 4886 1 149 . 1 1 45 45 ALA HB1 H 1 1.66 0.02 . 1 . . . . . . . . 4886 1 150 . 1 1 45 45 ALA HB2 H 1 1.66 0.02 . 1 . . . . . . . . 4886 1 151 . 1 1 45 45 ALA HB3 H 1 1.66 0.02 . 1 . . . . . . . . 4886 1 152 . 1 1 46 46 GLN N N 15 114.4 0.1 . 1 . . . . . . . . 4886 1 153 . 1 1 46 46 GLN H H 1 7.29 0.02 . 1 . . . . . . . . 4886 1 154 . 1 1 46 46 GLN HA H 1 4.21 0.02 . 1 . . . . . . . . 4886 1 155 . 1 1 46 46 GLN HB2 H 1 2.02 0.02 . 2 . . . . . . . . 4886 1 156 . 1 1 46 46 GLN NE2 N 15 113.0 0.1 . 1 . . . . . . . . 4886 1 157 . 1 1 46 46 GLN HE21 H 1 6.85 0.02 . 2 . . . . . . . . 4886 1 158 . 1 1 46 46 GLN HE22 H 1 7.54 0.02 . 2 . . . . . . . . 4886 1 159 . 1 1 47 47 TYR N N 15 116.5 0.1 . 1 . . . . . . . . 4886 1 160 . 1 1 47 47 TYR H H 1 6.87 0.02 . 1 . . . . . . . . 4886 1 161 . 1 1 47 47 TYR HA H 1 4.54 0.02 . 1 . . . . . . . . 4886 1 162 . 1 1 47 47 TYR HB2 H 1 3.47 0.02 . 2 . . . . . . . . 4886 1 163 . 1 1 47 47 TYR HB3 H 1 2.78 0.02 . 2 . . . . . . . . 4886 1 164 . 1 1 48 48 GLN N N 15 121.6 0.1 . 1 . . . . . . . . 4886 1 165 . 1 1 48 48 GLN H H 1 10.00 0.02 . 1 . . . . . . . . 4886 1 166 . 1 1 48 48 GLN HA H 1 4.26 0.02 . 1 . . . . . . . . 4886 1 167 . 1 1 48 48 GLN HB2 H 1 2.11 0.02 . 2 . . . . . . . . 4886 1 168 . 1 1 48 48 GLN NE2 N 15 112.0 0.1 . 1 . . . . . . . . 4886 1 169 . 1 1 48 48 GLN HE21 H 1 6.91 0.02 . 2 . . . . . . . . 4886 1 170 . 1 1 48 48 GLN HE22 H 1 7.22 0.02 . 2 . . . . . . . . 4886 1 171 . 1 1 49 49 PHE N N 15 115.4 0.1 . 1 . . . . . . . . 4886 1 172 . 1 1 49 49 PHE H H 1 7.28 0.02 . 1 . . . . . . . . 4886 1 173 . 1 1 49 49 PHE HA H 1 5.54 0.02 . 1 . . . . . . . . 4886 1 174 . 1 1 49 49 PHE HB2 H 1 3.13 0.02 . 2 . . . . . . . . 4886 1 175 . 1 1 50 50 LEU N N 15 124.9 0.1 . 1 . . . . . . . . 4886 1 176 . 1 1 50 50 LEU H H 1 9.20 0.02 . 1 . . . . . . . . 4886 1 177 . 1 1 50 50 LEU HA H 1 5.56 0.02 . 1 . . . . . . . . 4886 1 178 . 1 1 50 50 LEU HB2 H 1 1.78 0.02 . 2 . . . . . . . . 4886 1 179 . 1 1 50 50 LEU HB3 H 1 1.42 0.02 . 2 . . . . . . . . 4886 1 180 . 1 1 51 51 ILE N N 15 121.9 0.1 . 1 . . . . . . . . 4886 1 181 . 1 1 51 51 ILE H H 1 9.02 0.02 . 1 . . . . . . . . 4886 1 182 . 1 1 51 51 ILE HA H 1 5.28 0.02 . 1 . . . . . . . . 4886 1 183 . 1 1 51 51 ILE HB H 1 1.68 0.02 . 1 . . . . . . . . 4886 1 184 . 1 1 52 52 LEU N N 15 124.5 0.1 . 1 . . . . . . . . 4886 1 185 . 1 1 52 52 LEU H H 1 8.88 0.02 . 1 . . . . . . . . 4886 1 186 . 1 1 52 52 LEU HA H 1 5.94 0.02 . 1 . . . . . . . . 4886 1 187 . 1 1 52 52 LEU HB2 H 1 1.81 0.02 . 2 . . . . . . . . 4886 1 188 . 1 1 52 52 LEU HB3 H 1 1.41 0.02 . 2 . . . . . . . . 4886 1 189 . 1 1 53 53 GLY N N 15 106.0 0.1 . 1 . . . . . . . . 4886 1 190 . 1 1 53 53 GLY H H 1 8.80 0.02 . 1 . . . . . . . . 4886 1 191 . 1 1 53 53 GLY HA2 H 1 4.34 0.02 . 2 . . . . . . . . 4886 1 192 . 1 1 53 53 GLY HA3 H 1 1.93 0.02 . 2 . . . . . . . . 4886 1 193 . 1 1 54 54 THR HA H 1 5.48 0.02 . 1 . . . . . . . . 4886 1 194 . 1 1 54 54 THR HB H 1 3.87 0.02 . 1 . . . . . . . . 4886 1 195 . 1 1 68 68 ASP N N 15 121.8 0.1 . 1 . . . . . . . . 4886 1 196 . 1 1 68 68 ASP H H 1 8.30 0.02 . 1 . . . . . . . . 4886 1 197 . 1 1 68 68 ASP HA H 1 4.69 0.02 . 1 . . . . . . . . 4886 1 198 . 1 1 68 68 ASP HB2 H 1 2.77 0.02 . 2 . . . . . . . . 4886 1 199 . 1 1 69 69 ALA N N 15 123.4 0.1 . 1 . . . . . . . . 4886 1 200 . 1 1 69 69 ALA H H 1 8.06 0.02 . 1 . . . . . . . . 4886 1 201 . 1 1 69 69 ALA HA H 1 4.36 0.02 . 1 . . . . . . . . 4886 1 202 . 1 1 69 69 ALA HB1 H 1 1.46 0.02 . 1 . . . . . . . . 4886 1 203 . 1 1 69 69 ALA HB2 H 1 1.46 0.02 . 1 . . . . . . . . 4886 1 204 . 1 1 69 69 ALA HB3 H 1 1.46 0.02 . 1 . . . . . . . . 4886 1 205 . 1 1 70 70 GLU N N 15 118.7 0.1 . 1 . . . . . . . . 4886 1 206 . 1 1 70 70 GLU H H 1 8.30 0.02 . 1 . . . . . . . . 4886 1 207 . 1 1 70 70 GLU HA H 1 4.34 0.02 . 1 . . . . . . . . 4886 1 208 . 1 1 70 70 GLU HB2 H 1 2.15 0.02 . 2 . . . . . . . . 4886 1 209 . 1 1 70 70 GLU HB3 H 1 2.02 0.02 . 2 . . . . . . . . 4886 1 210 . 1 1 71 71 ASN ND2 N 15 114.0 0.1 . 1 . . . . . . . . 4886 1 211 . 1 1 71 71 ASN HD21 H 1 7.17 0.02 . 2 . . . . . . . . 4886 1 212 . 1 1 71 71 ASN HD22 H 1 7.81 0.02 . 9 . . . . . . . . 4886 1 213 . 1 1 74 74 TRP N N 15 123.0 0.1 . 9 . . . . . . . . 4886 1 214 . 1 1 74 74 TRP H H 1 8.10 0.02 . 9 . . . . . . . . 4886 1 215 . 1 1 74 74 TRP HA H 1 3.51 0.02 . 1 . . . . . . . . 4886 1 216 . 1 1 74 74 TRP HB2 H 1 2.49 0.02 . 2 . . . . . . . . 4886 1 217 . 1 1 74 74 TRP HB3 H 1 2.33 0.02 . 2 . . . . . . . . 4886 1 218 . 1 1 74 74 TRP NE1 N 15 127.1 0.1 . 1 . . . . . . . . 4886 1 219 . 1 1 74 74 TRP HE1 H 1 10.07 0.02 . 1 . . . . . . . . 4886 1 220 . 1 1 78 78 LEU HA H 1 3.69 0.02 . 1 . . . . . . . . 4886 1 221 . 1 1 79 79 PRO HA H 1 4.36 0.02 . 1 . . . . . . . . 4886 1 222 . 1 1 80 80 LYS N N 15 113.1 0.1 . 1 . . . . . . . . 4886 1 223 . 1 1 80 80 LYS H H 1 7.86 0.02 . 1 . . . . . . . . 4886 1 224 . 1 1 80 80 LYS HA H 1 4.07 0.02 . 1 . . . . . . . . 4886 1 225 . 1 1 80 80 LYS HB2 H 1 1.67 0.02 . 2 . . . . . . . . 4886 1 226 . 1 1 80 80 LYS HB3 H 1 1.54 0.02 . 2 . . . . . . . . 4886 1 227 . 1 1 81 81 ILE N N 15 107.9 0.1 . 1 . . . . . . . . 4886 1 228 . 1 1 81 81 ILE H H 1 7.32 0.02 . 1 . . . . . . . . 4886 1 229 . 1 1 81 81 ILE HA H 1 4.64 0.02 . 1 . . . . . . . . 4886 1 230 . 1 1 81 81 ILE HB H 1 2.62 0.02 . 1 . . . . . . . . 4886 1 231 . 1 1 82 82 GLU N N 15 121.0 0.1 . 1 . . . . . . . . 4886 1 232 . 1 1 82 82 GLU H H 1 7.19 0.02 . 1 . . . . . . . . 4886 1 233 . 1 1 82 82 GLU HA H 1 4.20 0.02 . 1 . . . . . . . . 4886 1 234 . 1 1 82 82 GLU HB2 H 1 2.24 0.02 . 2 . . . . . . . . 4886 1 235 . 1 1 83 83 GLY N N 15 107.1 0.1 . 1 . . . . . . . . 4886 1 236 . 1 1 83 83 GLY H H 1 8.64 0.02 . 1 . . . . . . . . 4886 1 237 . 1 1 83 83 GLY HA2 H 1 4.32 0.02 . 2 . . . . . . . . 4886 1 238 . 1 1 83 83 GLY HA3 H 1 3.65 0.02 . 2 . . . . . . . . 4886 1 239 . 1 1 84 84 LEU N N 15 121.0 0.1 . 1 . . . . . . . . 4886 1 240 . 1 1 84 84 LEU H H 1 7.49 0.02 . 1 . . . . . . . . 4886 1 241 . 1 1 84 84 LEU HA H 1 4.32 0.02 . 1 . . . . . . . . 4886 1 242 . 1 1 84 84 LEU HB2 H 1 2.02 0.02 . 2 . . . . . . . . 4886 1 243 . 1 1 84 84 LEU HB3 H 1 1.07 0.02 . 2 . . . . . . . . 4886 1 244 . 1 1 85 85 ASP N N 15 119.5 0.1 . 1 . . . . . . . . 4886 1 245 . 1 1 85 85 ASP H H 1 8.13 0.02 . 1 . . . . . . . . 4886 1 246 . 1 1 85 85 ASP HA H 1 4.82 0.02 . 1 . . . . . . . . 4886 1 247 . 1 1 85 85 ASP HB2 H 1 2.83 0.02 . 2 . . . . . . . . 4886 1 248 . 1 1 85 85 ASP HB3 H 1 2.69 0.02 . 2 . . . . . . . . 4886 1 249 . 1 1 86 86 PHE N N 15 124.9 0.1 . 1 . . . . . . . . 4886 1 250 . 1 1 86 86 PHE H H 1 9.09 0.02 . 1 . . . . . . . . 4886 1 251 . 1 1 86 86 PHE HA H 1 4.49 0.02 . 1 . . . . . . . . 4886 1 252 . 1 1 86 86 PHE HB2 H 1 3.56 0.02 . 2 . . . . . . . . 4886 1 253 . 1 1 86 86 PHE HB3 H 1 2.70 0.02 . 2 . . . . . . . . 4886 1 254 . 1 1 87 87 SER N N 15 117.7 0.1 . 1 . . . . . . . . 4886 1 255 . 1 1 87 87 SER H H 1 8.53 0.02 . 1 . . . . . . . . 4886 1 256 . 1 1 87 87 SER HA H 1 4.42 0.02 . 1 . . . . . . . . 4886 1 257 . 1 1 87 87 SER HB2 H 1 3.94 0.02 . 2 . . . . . . . . 4886 1 258 . 1 1 88 88 GLY N N 15 113.7 0.1 . 1 . . . . . . . . 4886 1 259 . 1 1 88 88 GLY H H 1 8.88 0.02 . 1 . . . . . . . . 4886 1 260 . 1 1 88 88 GLY HA2 H 1 4.25 0.02 . 2 . . . . . . . . 4886 1 261 . 1 1 88 88 GLY HA3 H 1 3.79 0.02 . 2 . . . . . . . . 4886 1 262 . 1 1 89 89 LYS N N 15 121.2 0.1 . 1 . . . . . . . . 4886 1 263 . 1 1 89 89 LYS H H 1 8.05 0.02 . 1 . . . . . . . . 4886 1 264 . 1 1 89 89 LYS HA H 1 4.77 0.02 . 1 . . . . . . . . 4886 1 265 . 1 1 89 89 LYS HB2 H 1 2.27 0.02 . 2 . . . . . . . . 4886 1 266 . 1 1 89 89 LYS HB3 H 1 1.57 0.02 . 2 . . . . . . . . 4886 1 267 . 1 1 90 90 THR N N 15 120.2 0.1 . 1 . . . . . . . . 4886 1 268 . 1 1 90 90 THR H H 1 7.95 0.02 . 1 . . . . . . . . 4886 1 269 . 1 1 90 90 THR HA H 1 5.18 0.02 . 1 . . . . . . . . 4886 1 270 . 1 1 90 90 THR HB H 1 3.73 0.02 . 1 . . . . . . . . 4886 1 271 . 1 1 91 91 VAL N N 15 127.5 0.1 . 1 . . . . . . . . 4886 1 272 . 1 1 91 91 VAL H H 1 9.19 0.02 . 1 . . . . . . . . 4886 1 273 . 1 1 91 91 VAL HA H 1 5.33 0.02 . 1 . . . . . . . . 4886 1 274 . 1 1 91 91 VAL HB H 1 1.73 0.02 . 1 . . . . . . . . 4886 1 275 . 1 1 92 92 ALA N N 15 128.4 0.1 . 1 . . . . . . . . 4886 1 276 . 1 1 92 92 ALA H H 1 8.95 0.02 . 1 . . . . . . . . 4886 1 277 . 1 1 92 92 ALA HA H 1 5.55 0.02 . 1 . . . . . . . . 4886 1 278 . 1 1 92 92 ALA HB1 H 1 1.58 0.02 . 1 . . . . . . . . 4886 1 279 . 1 1 92 92 ALA HB2 H 1 1.58 0.02 . 1 . . . . . . . . 4886 1 280 . 1 1 92 92 ALA HB3 H 1 1.58 0.02 . 1 . . . . . . . . 4886 1 281 . 1 1 93 93 LEU N N 15 122.1 0.1 . 1 . . . . . . . . 4886 1 282 . 1 1 93 93 LEU H H 1 10.23 0.02 . 1 . . . . . . . . 4886 1 283 . 1 1 93 93 LEU HA H 1 5.81 0.02 . 1 . . . . . . . . 4886 1 284 . 1 1 93 93 LEU HB2 H 1 1.71 0.02 . 2 . . . . . . . . 4886 1 285 . 1 1 93 93 LEU HB3 H 1 1.30 0.02 . 2 . . . . . . . . 4886 1 286 . 1 1 94 94 PHE N N 15 114.7 0.1 . 1 . . . . . . . . 4886 1 287 . 1 1 94 94 PHE H H 1 8.92 0.02 . 1 . . . . . . . . 4886 1 288 . 1 1 94 94 PHE HA H 1 5.13 0.02 . 1 . . . . . . . . 4886 1 289 . 1 1 94 94 PHE HB2 H 1 2.21 0.02 . 2 . . . . . . . . 4886 1 290 . 1 1 95 95 GLY N N 15 106.9 0.1 . 1 . . . . . . . . 4886 1 291 . 1 1 95 95 GLY H H 1 8.78 0.02 . 1 . . . . . . . . 4886 1 292 . 1 1 95 95 GLY HA2 H 1 5.33 0.02 . 2 . . . . . . . . 4886 1 293 . 1 1 95 95 GLY HA3 H 1 3.09 0.02 . 2 . . . . . . . . 4886 1 294 . 1 1 96 96 LEU N N 15 122.0 0.1 . 1 . . . . . . . . 4886 1 295 . 1 1 96 96 LEU H H 1 7.64 0.02 . 1 . . . . . . . . 4886 1 296 . 1 1 96 96 LEU HA H 1 5.06 0.02 . 1 . . . . . . . . 4886 1 297 . 1 1 96 96 LEU HB2 H 1 1.96 0.02 . 2 . . . . . . . . 4886 1 298 . 1 1 96 96 LEU HB3 H 1 1.45 0.02 . 2 . . . . . . . . 4886 1 299 . 1 1 97 97 GLY N N 15 107.9 0.1 . 1 . . . . . . . . 4886 1 300 . 1 1 97 97 GLY H H 1 8.12 0.02 . 1 . . . . . . . . 4886 1 301 . 1 1 97 97 GLY HA2 H 1 4.54 0.02 . 2 . . . . . . . . 4886 1 302 . 1 1 97 97 GLY HA3 H 1 3.90 0.02 . 2 . . . . . . . . 4886 1 303 . 1 1 98 98 ASP HA H 1 5.20 0.02 . 9 . . . . . . . . 4886 1 304 . 1 1 99 99 GLN N N 15 123.9 0.1 . 9 . . . . . . . . 4886 1 305 . 1 1 99 99 GLN H H 1 8.72 0.02 . 9 . . . . . . . . 4886 1 306 . 1 1 99 99 GLN HA H 1 3.86 0.02 . 1 . . . . . . . . 4886 1 307 . 1 1 99 99 GLN HB2 H 1 2.33 0.02 . 2 . . . . . . . . 4886 1 308 . 1 1 99 99 GLN HB3 H 1 1.08 0.02 . 2 . . . . . . . . 4886 1 309 . 1 1 100 100 VAL N N 15 119.4 0.1 . 1 . . . . . . . . 4886 1 310 . 1 1 100 100 VAL H H 1 7.34 0.02 . 1 . . . . . . . . 4886 1 311 . 1 1 100 100 VAL HA H 1 3.85 0.02 . 1 . . . . . . . . 4886 1 312 . 1 1 100 100 VAL HB H 1 2.04 0.02 . 1 . . . . . . . . 4886 1 313 . 1 1 101 101 GLY N N 15 108.7 0.1 . 1 . . . . . . . . 4886 1 314 . 1 1 101 101 GLY H H 1 8.92 0.02 . 1 . . . . . . . . 4886 1 315 . 1 1 101 101 GLY HA2 H 1 3.80 0.02 . 2 . . . . . . . . 4886 1 316 . 1 1 101 101 GLY HA3 H 1 3.58 0.02 . 2 . . . . . . . . 4886 1 317 . 1 1 102 102 TYR N N 15 116.4 0.1 . 1 . . . . . . . . 4886 1 318 . 1 1 102 102 TYR H H 1 7.47 0.02 . 1 . . . . . . . . 4886 1 319 . 1 1 102 102 TYR HA H 1 5.13 0.02 . 1 . . . . . . . . 4886 1 320 . 1 1 102 102 TYR HB2 H 1 3.14 0.02 . 2 . . . . . . . . 4886 1 321 . 1 1 103 103 PRO HA H 1 4.58 0.02 . 1 . . . . . . . . 4886 1 322 . 1 1 104 104 GLU N N 15 117.7 0.1 . 1 . . . . . . . . 4886 1 323 . 1 1 104 104 GLU H H 1 8.80 0.02 . 1 . . . . . . . . 4886 1 324 . 1 1 104 104 GLU HA H 1 4.66 0.02 . 1 . . . . . . . . 4886 1 325 . 1 1 104 104 GLU HB2 H 1 2.28 0.02 . 2 . . . . . . . . 4886 1 326 . 1 1 104 104 GLU HB3 H 1 2.10 0.02 . 2 . . . . . . . . 4886 1 327 . 1 1 105 105 ASN N N 15 119.0 0.1 . 1 . . . . . . . . 4886 1 328 . 1 1 105 105 ASN H H 1 7.90 0.02 . 1 . . . . . . . . 4886 1 329 . 1 1 105 105 ASN HA H 1 5.13 0.02 . 1 . . . . . . . . 4886 1 330 . 1 1 105 105 ASN HB2 H 1 3.27 0.02 . 2 . . . . . . . . 4886 1 331 . 1 1 105 105 ASN HB3 H 1 3.12 0.02 . 2 . . . . . . . . 4886 1 332 . 1 1 105 105 ASN ND2 N 15 112.3 0.1 . 1 . . . . . . . . 4886 1 333 . 1 1 105 105 ASN HD21 H 1 6.84 0.02 . 2 . . . . . . . . 4886 1 334 . 1 1 105 105 ASN HD22 H 1 8.17 0.02 . 2 . . . . . . . . 4886 1 335 . 1 1 106 106 TYR N N 15 122.1 0.1 . 1 . . . . . . . . 4886 1 336 . 1 1 106 106 TYR H H 1 7.70 0.02 . 1 . . . . . . . . 4886 1 337 . 1 1 106 106 TYR HB2 H 1 3.43 0.02 . 2 . . . . . . . . 4886 1 338 . 1 1 106 106 TYR HB3 H 1 2.65 0.02 . 2 . . . . . . . . 4886 1 339 . 1 1 109 109 ALA HA H 1 4.16 0.02 . 1 . . . . . . . . 4886 1 340 . 1 1 110 110 LEU N N 15 118.6 0.1 . 1 . . . . . . . . 4886 1 341 . 1 1 110 110 LEU H H 1 7.32 0.02 . 1 . . . . . . . . 4886 1 342 . 1 1 110 110 LEU HA H 1 3.85 0.02 . 1 . . . . . . . . 4886 1 343 . 1 1 110 110 LEU HB2 H 1 1.88 0.02 . 2 . . . . . . . . 4886 1 344 . 1 1 110 110 LEU HB3 H 1 1.11 0.02 . 2 . . . . . . . . 4886 1 345 . 1 1 111 111 GLY N N 15 104.9 0.1 . 1 . . . . . . . . 4886 1 346 . 1 1 111 111 GLY H H 1 7.49 0.02 . 1 . . . . . . . . 4886 1 347 . 1 1 111 111 GLY HA2 H 1 3.71 0.02 . 1 . . . . . . . . 4886 1 348 . 1 1 111 111 GLY HA3 H 1 3.71 0.02 . 1 . . . . . . . . 4886 1 349 . 1 1 112 112 GLU N N 15 122.0 0.1 . 1 . . . . . . . . 4886 1 350 . 1 1 112 112 GLU H H 1 7.60 0.02 . 1 . . . . . . . . 4886 1 351 . 1 1 112 112 GLU HA H 1 4.20 0.02 . 1 . . . . . . . . 4886 1 352 . 1 1 112 112 GLU HB2 H 1 2.14 0.02 . 2 . . . . . . . . 4886 1 353 . 1 1 113 113 LEU N N 15 120.9 0.1 . 1 . . . . . . . . 4886 1 354 . 1 1 113 113 LEU H H 1 7.59 0.02 . 1 . . . . . . . . 4886 1 355 . 1 1 113 113 LEU HA H 1 3.93 0.02 . 1 . . . . . . . . 4886 1 356 . 1 1 113 113 LEU HB2 H 1 1.55 0.02 . 2 . . . . . . . . 4886 1 357 . 1 1 113 113 LEU HB3 H 1 1.38 0.02 . 2 . . . . . . . . 4886 1 358 . 1 1 114 114 TYR N N 15 118.7 0.1 . 1 . . . . . . . . 4886 1 359 . 1 1 114 114 TYR H H 1 8.14 0.02 . 1 . . . . . . . . 4886 1 360 . 1 1 114 114 TYR HA H 1 4.02 0.02 . 1 . . . . . . . . 4886 1 361 . 1 1 114 114 TYR HB2 H 1 3.36 0.02 . 2 . . . . . . . . 4886 1 362 . 1 1 114 114 TYR HB3 H 1 3.00 0.02 . 2 . . . . . . . . 4886 1 363 . 1 1 115 115 SER N N 15 114.6 0.1 . 1 . . . . . . . . 4886 1 364 . 1 1 115 115 SER H H 1 8.16 0.02 . 1 . . . . . . . . 4886 1 365 . 1 1 115 115 SER HA H 1 3.87 0.02 . 1 . . . . . . . . 4886 1 366 . 1 1 115 115 SER HB2 H 1 4.02 0.02 . 2 . . . . . . . . 4886 1 367 . 1 1 116 116 PHE N N 15 120.5 0.1 . 1 . . . . . . . . 4886 1 368 . 1 1 116 116 PHE H H 1 7.68 0.02 . 1 . . . . . . . . 4886 1 369 . 1 1 116 116 PHE HA H 1 3.87 0.02 . 1 . . . . . . . . 4886 1 370 . 1 1 116 116 PHE HB2 H 1 2.97 0.02 . 2 . . . . . . . . 4886 1 371 . 1 1 117 117 PHE N N 15 114.5 0.1 . 1 . . . . . . . . 4886 1 372 . 1 1 117 117 PHE H H 1 7.72 0.02 . 1 . . . . . . . . 4886 1 373 . 1 1 117 117 PHE HA H 1 3.87 0.02 . 1 . . . . . . . . 4886 1 374 . 1 1 117 117 PHE HB2 H 1 2.68 0.02 . 2 . . . . . . . . 4886 1 375 . 1 1 118 118 LYS N N 15 124.7 0.1 . 1 . . . . . . . . 4886 1 376 . 1 1 118 118 LYS H H 1 9.07 0.02 . 1 . . . . . . . . 4886 1 377 . 1 1 118 118 LYS HA H 1 3.98 0.02 . 1 . . . . . . . . 4886 1 378 . 1 1 118 118 LYS HB2 H 1 1.64 0.02 . 2 . . . . . . . . 4886 1 379 . 1 1 118 118 LYS HB3 H 1 1.23 0.02 . 2 . . . . . . . . 4886 1 380 . 1 1 119 119 ASP N N 15 119.4 0.1 . 1 . . . . . . . . 4886 1 381 . 1 1 119 119 ASP H H 1 8.41 0.02 . 1 . . . . . . . . 4886 1 382 . 1 1 119 119 ASP HA H 1 4.48 0.02 . 1 . . . . . . . . 4886 1 383 . 1 1 119 119 ASP HB2 H 1 2.66 0.02 . 2 . . . . . . . . 4886 1 384 . 1 1 120 120 ARG N N 15 116.7 0.1 . 1 . . . . . . . . 4886 1 385 . 1 1 120 120 ARG H H 1 6.78 0.02 . 1 . . . . . . . . 4886 1 386 . 1 1 120 120 ARG HA H 1 4.61 0.02 . 1 . . . . . . . . 4886 1 387 . 1 1 120 120 ARG HB2 H 1 2.72 0.02 . 2 . . . . . . . . 4886 1 388 . 1 1 120 120 ARG HB3 H 1 1.37 0.02 . 2 . . . . . . . . 4886 1 389 . 1 1 121 121 GLY N N 15 105.4 0.1 . 1 . . . . . . . . 4886 1 390 . 1 1 121 121 GLY H H 1 7.51 0.02 . 1 . . . . . . . . 4886 1 391 . 1 1 121 121 GLY HA2 H 1 4.39 0.02 . 2 . . . . . . . . 4886 1 392 . 1 1 121 121 GLY HA3 H 1 3.86 0.02 . 2 . . . . . . . . 4886 1 393 . 1 1 122 122 ALA N N 15 121.0 0.1 . 1 . . . . . . . . 4886 1 394 . 1 1 122 122 ALA H H 1 7.69 0.02 . 1 . . . . . . . . 4886 1 395 . 1 1 122 122 ALA HA H 1 4.51 0.02 . 1 . . . . . . . . 4886 1 396 . 1 1 122 122 ALA HB1 H 1 1.23 0.02 . 1 . . . . . . . . 4886 1 397 . 1 1 122 122 ALA HB2 H 1 1.23 0.02 . 1 . . . . . . . . 4886 1 398 . 1 1 122 122 ALA HB3 H 1 1.23 0.02 . 1 . . . . . . . . 4886 1 399 . 1 1 123 123 LYS N N 15 123.6 0.1 . 1 . . . . . . . . 4886 1 400 . 1 1 123 123 LYS H H 1 8.58 0.02 . 1 . . . . . . . . 4886 1 401 . 1 1 123 123 LYS HA H 1 4.55 0.02 . 1 . . . . . . . . 4886 1 402 . 1 1 123 123 LYS HB2 H 1 2.06 0.02 . 2 . . . . . . . . 4886 1 403 . 1 1 123 123 LYS HB3 H 1 1.85 0.02 . 2 . . . . . . . . 4886 1 404 . 1 1 124 124 ILE N N 15 128.1 0.1 . 1 . . . . . . . . 4886 1 405 . 1 1 124 124 ILE H H 1 8.48 0.02 . 1 . . . . . . . . 4886 1 406 . 1 1 124 124 ILE HA H 1 5.53 0.02 . 1 . . . . . . . . 4886 1 407 . 1 1 124 124 ILE HB H 1 2.05 0.02 . 1 . . . . . . . . 4886 1 408 . 1 1 125 125 VAL N N 15 122.9 0.1 . 1 . . . . . . . . 4886 1 409 . 1 1 125 125 VAL H H 1 9.00 0.02 . 1 . . . . . . . . 4886 1 410 . 1 1 125 125 VAL HA H 1 5.07 0.02 . 1 . . . . . . . . 4886 1 411 . 1 1 125 125 VAL HB H 1 2.46 0.02 . 1 . . . . . . . . 4886 1 412 . 1 1 126 126 GLY N N 15 107.7 0.1 . 1 . . . . . . . . 4886 1 413 . 1 1 126 126 GLY H H 1 8.92 0.02 . 1 . . . . . . . . 4886 1 414 . 1 1 126 126 GLY HA2 H 1 4.72 0.02 . 2 . . . . . . . . 4886 1 415 . 1 1 126 126 GLY HA3 H 1 3.86 0.02 . 2 . . . . . . . . 4886 1 416 . 1 1 127 127 SER N N 15 114.3 0.1 . 1 . . . . . . . . 4886 1 417 . 1 1 127 127 SER H H 1 7.89 0.02 . 1 . . . . . . . . 4886 1 418 . 1 1 127 127 SER HA H 1 4.53 0.02 . 1 . . . . . . . . 4886 1 419 . 1 1 127 127 SER HB2 H 1 4.20 0.02 . 2 . . . . . . . . 4886 1 420 . 1 1 127 127 SER HB3 H 1 4.07 0.02 . 2 . . . . . . . . 4886 1 421 . 1 1 128 128 TRP N N 15 123.0 0.1 . 1 . . . . . . . . 4886 1 422 . 1 1 128 128 TRP H H 1 8.76 0.02 . 1 . . . . . . . . 4886 1 423 . 1 1 128 128 TRP HA H 1 5.53 0.02 . 1 . . . . . . . . 4886 1 424 . 1 1 128 128 TRP HB2 H 1 3.51 0.02 . 2 . . . . . . . . 4886 1 425 . 1 1 128 128 TRP HB3 H 1 3.12 0.02 . 2 . . . . . . . . 4886 1 426 . 1 1 128 128 TRP NE1 N 15 129.0 0.1 . 1 . . . . . . . . 4886 1 427 . 1 1 128 128 TRP HE1 H 1 10.35 0.02 . 1 . . . . . . . . 4886 1 428 . 1 1 129 129 SER N N 15 120.3 0.1 . 1 . . . . . . . . 4886 1 429 . 1 1 129 129 SER H H 1 7.54 0.02 . 1 . . . . . . . . 4886 1 430 . 1 1 129 129 SER HA H 1 4.49 0.02 . 1 . . . . . . . . 4886 1 431 . 1 1 129 129 SER HB2 H 1 3.93 0.02 . 2 . . . . . . . . 4886 1 432 . 1 1 129 129 SER HB3 H 1 3.62 0.02 . 2 . . . . . . . . 4886 1 433 . 1 1 130 130 THR N N 15 113.2 0.1 . 1 . . . . . . . . 4886 1 434 . 1 1 130 130 THR H H 1 8.47 0.02 . 1 . . . . . . . . 4886 1 435 . 1 1 130 130 THR HA H 1 4.48 0.02 . 1 . . . . . . . . 4886 1 436 . 1 1 130 130 THR HB H 1 4.58 0.02 . 1 . . . . . . . . 4886 1 437 . 1 1 131 131 ASP N N 15 125.0 0.1 . 1 . . . . . . . . 4886 1 438 . 1 1 131 131 ASP H H 1 8.42 0.02 . 1 . . . . . . . . 4886 1 439 . 1 1 131 131 ASP HA H 1 4.60 0.02 . 1 . . . . . . . . 4886 1 440 . 1 1 131 131 ASP HB2 H 1 2.67 0.02 . 2 . . . . . . . . 4886 1 441 . 1 1 132 132 GLY N N 15 112.2 0.1 . 1 . . . . . . . . 4886 1 442 . 1 1 132 132 GLY H H 1 9.09 0.02 . 1 . . . . . . . . 4886 1 443 . 1 1 132 132 GLY HA2 H 1 4.24 0.02 . 2 . . . . . . . . 4886 1 444 . 1 1 132 132 GLY HA3 H 1 3.76 0.02 . 2 . . . . . . . . 4886 1 445 . 1 1 133 133 TYR N N 15 118.7 0.1 . 1 . . . . . . . . 4886 1 446 . 1 1 133 133 TYR H H 1 7.86 0.02 . 1 . . . . . . . . 4886 1 447 . 1 1 133 133 TYR HA H 1 5.08 0.02 . 1 . . . . . . . . 4886 1 448 . 1 1 133 133 TYR HB2 H 1 3.43 0.02 . 2 . . . . . . . . 4886 1 449 . 1 1 133 133 TYR HB3 H 1 3.07 0.02 . 2 . . . . . . . . 4886 1 450 . 1 1 134 134 GLU N N 15 123.7 0.1 . 1 . . . . . . . . 4886 1 451 . 1 1 134 134 GLU H H 1 9.30 0.02 . 1 . . . . . . . . 4886 1 452 . 1 1 134 134 GLU HA H 1 4.74 0.02 . 1 . . . . . . . . 4886 1 453 . 1 1 134 134 GLU HB2 H 1 2.00 0.02 . 2 . . . . . . . . 4886 1 454 . 1 1 135 135 PHE N N 15 118.2 0.1 . 1 . . . . . . . . 4886 1 455 . 1 1 135 135 PHE H H 1 7.59 0.02 . 1 . . . . . . . . 4886 1 456 . 1 1 135 135 PHE HA H 1 4.90 0.02 . 1 . . . . . . . . 4886 1 457 . 1 1 135 135 PHE HB2 H 1 3.42 0.02 . 2 . . . . . . . . 4886 1 458 . 1 1 135 135 PHE HB3 H 1 3.20 0.02 . 2 . . . . . . . . 4886 1 459 . 1 1 136 136 GLU N N 15 120.3 0.1 . 1 . . . . . . . . 4886 1 460 . 1 1 136 136 GLU H H 1 9.02 0.02 . 1 . . . . . . . . 4886 1 461 . 1 1 136 136 GLU HA H 1 4.46 0.02 . 1 . . . . . . . . 4886 1 462 . 1 1 136 136 GLU HB2 H 1 2.12 0.02 . 2 . . . . . . . . 4886 1 463 . 1 1 136 136 GLU HB3 H 1 1.87 0.02 . 2 . . . . . . . . 4886 1 464 . 1 1 137 137 SER N N 15 112.8 0.1 . 1 . . . . . . . . 4886 1 465 . 1 1 137 137 SER H H 1 8.48 0.02 . 1 . . . . . . . . 4886 1 466 . 1 1 137 137 SER HA H 1 4.88 0.02 . 1 . . . . . . . . 4886 1 467 . 1 1 137 137 SER HB2 H 1 4.01 0.02 . 2 . . . . . . . . 4886 1 468 . 1 1 138 138 SER N N 15 113.8 0.1 . 1 . . . . . . . . 4886 1 469 . 1 1 138 138 SER H H 1 8.39 0.02 . 1 . . . . . . . . 4886 1 470 . 1 1 138 138 SER HA H 1 4.77 0.02 . 1 . . . . . . . . 4886 1 471 . 1 1 138 138 SER HB2 H 1 4.06 0.02 . 2 . . . . . . . . 4886 1 472 . 1 1 138 138 SER HB3 H 1 3.43 0.02 . 2 . . . . . . . . 4886 1 473 . 1 1 139 139 GLU N N 15 128.3 0.1 . 1 . . . . . . . . 4886 1 474 . 1 1 139 139 GLU H H 1 9.40 0.02 . 1 . . . . . . . . 4886 1 475 . 1 1 139 139 GLU HA H 1 4.50 0.02 . 1 . . . . . . . . 4886 1 476 . 1 1 139 139 GLU HB2 H 1 2.40 0.02 . 2 . . . . . . . . 4886 1 477 . 1 1 139 139 GLU HB3 H 1 1.94 0.02 . 2 . . . . . . . . 4886 1 478 . 1 1 140 140 ALA N N 15 119.3 0.1 . 1 . . . . . . . . 4886 1 479 . 1 1 140 140 ALA H H 1 8.69 0.02 . 1 . . . . . . . . 4886 1 480 . 1 1 140 140 ALA HA H 1 4.16 0.02 . 1 . . . . . . . . 4886 1 481 . 1 1 140 140 ALA HB1 H 1 1.44 0.02 . 1 . . . . . . . . 4886 1 482 . 1 1 140 140 ALA HB2 H 1 1.44 0.02 . 1 . . . . . . . . 4886 1 483 . 1 1 140 140 ALA HB3 H 1 1.44 0.02 . 1 . . . . . . . . 4886 1 484 . 1 1 141 141 VAL N N 15 118.5 0.1 . 1 . . . . . . . . 4886 1 485 . 1 1 141 141 VAL H H 1 6.81 0.02 . 1 . . . . . . . . 4886 1 486 . 1 1 141 141 VAL HA H 1 4.49 0.02 . 1 . . . . . . . . 4886 1 487 . 1 1 141 141 VAL HB H 1 1.94 0.02 . 1 . . . . . . . . 4886 1 488 . 1 1 142 142 VAL N N 15 128.7 0.1 . 1 . . . . . . . . 4886 1 489 . 1 1 142 142 VAL H H 1 8.69 0.02 . 1 . . . . . . . . 4886 1 490 . 1 1 142 142 VAL HA H 1 4.14 0.02 . 1 . . . . . . . . 4886 1 491 . 1 1 142 142 VAL HB H 1 1.62 0.02 . 1 . . . . . . . . 4886 1 492 . 1 1 143 143 ASP N N 15 127.6 0.1 . 1 . . . . . . . . 4886 1 493 . 1 1 143 143 ASP H H 1 9.35 0.02 . 1 . . . . . . . . 4886 1 494 . 1 1 143 143 ASP HA H 1 4.33 0.02 . 1 . . . . . . . . 4886 1 495 . 1 1 143 143 ASP HB2 H 1 3.03 0.02 . 2 . . . . . . . . 4886 1 496 . 1 1 143 143 ASP HB3 H 1 2.69 0.02 . 2 . . . . . . . . 4886 1 497 . 1 1 144 144 GLY N N 15 101.9 0.1 . 1 . . . . . . . . 4886 1 498 . 1 1 144 144 GLY H H 1 8.34 0.02 . 1 . . . . . . . . 4886 1 499 . 1 1 144 144 GLY HA2 H 1 4.11 0.02 . 2 . . . . . . . . 4886 1 500 . 1 1 144 144 GLY HA3 H 1 3.53 0.02 . 2 . . . . . . . . 4886 1 501 . 1 1 145 145 LYS N N 15 119.2 0.1 . 1 . . . . . . . . 4886 1 502 . 1 1 145 145 LYS H H 1 7.57 0.02 . 1 . . . . . . . . 4886 1 503 . 1 1 145 145 LYS HA H 1 4.68 0.02 . 1 . . . . . . . . 4886 1 504 . 1 1 145 145 LYS HB2 H 1 1.97 0.02 . 2 . . . . . . . . 4886 1 505 . 1 1 145 145 LYS HB3 H 1 1.69 0.02 . 2 . . . . . . . . 4886 1 506 . 1 1 146 146 PHE N N 15 119.7 0.1 . 1 . . . . . . . . 4886 1 507 . 1 1 146 146 PHE H H 1 9.15 0.02 . 1 . . . . . . . . 4886 1 508 . 1 1 146 146 PHE HA H 1 5.27 0.02 . 1 . . . . . . . . 4886 1 509 . 1 1 146 146 PHE HB2 H 1 3.50 0.02 . 2 . . . . . . . . 4886 1 510 . 1 1 146 146 PHE HB3 H 1 3.30 0.02 . 2 . . . . . . . . 4886 1 511 . 1 1 147 147 VAL N N 15 112.3 0.1 . 1 . . . . . . . . 4886 1 512 . 1 1 147 147 VAL H H 1 8.50 0.02 . 1 . . . . . . . . 4886 1 513 . 1 1 147 147 VAL HA H 1 3.98 0.02 . 1 . . . . . . . . 4886 1 514 . 1 1 147 147 VAL HB H 1 2.04 0.02 . 1 . . . . . . . . 4886 1 515 . 1 1 148 148 GLY N N 15 106.1 0.1 . 1 . . . . . . . . 4886 1 516 . 1 1 148 148 GLY H H 1 7.07 0.02 . 1 . . . . . . . . 4886 1 517 . 1 1 148 148 GLY HA2 H 1 4.81 0.02 . 2 . . . . . . . . 4886 1 518 . 1 1 148 148 GLY HA3 H 1 3.91 0.02 . 2 . . . . . . . . 4886 1 519 . 1 1 149 149 LEU N N 15 117.0 0.1 . 1 . . . . . . . . 4886 1 520 . 1 1 149 149 LEU H H 1 7.44 0.02 . 1 . . . . . . . . 4886 1 521 . 1 1 149 149 LEU HA H 1 2.86 0.02 . 1 . . . . . . . . 4886 1 522 . 1 1 150 150 ALA N N 15 127.7 0.1 . 1 . . . . . . . . 4886 1 523 . 1 1 150 150 ALA H H 1 5.24 0.02 . 1 . . . . . . . . 4886 1 524 . 1 1 150 150 ALA HA H 1 4.22 0.02 . 1 . . . . . . . . 4886 1 525 . 1 1 150 150 ALA HB1 H 1 0.20 0.02 . 1 . . . . . . . . 4886 1 526 . 1 1 150 150 ALA HB2 H 1 0.20 0.02 . 1 . . . . . . . . 4886 1 527 . 1 1 150 150 ALA HB3 H 1 0.20 0.02 . 1 . . . . . . . . 4886 1 528 . 1 1 151 151 LEU N N 15 123.5 0.1 . 1 . . . . . . . . 4886 1 529 . 1 1 151 151 LEU H H 1 8.65 0.02 . 1 . . . . . . . . 4886 1 530 . 1 1 151 151 LEU HA H 1 4.89 0.02 . 1 . . . . . . . . 4886 1 531 . 1 1 151 151 LEU HB2 H 1 1.95 0.02 . 2 . . . . . . . . 4886 1 532 . 1 1 151 151 LEU HB3 H 1 1.27 0.02 . 2 . . . . . . . . 4886 1 533 . 1 1 152 152 ASP N N 15 120.2 0.1 . 1 . . . . . . . . 4886 1 534 . 1 1 152 152 ASP H H 1 8.09 0.02 . 1 . . . . . . . . 4886 1 535 . 1 1 152 152 ASP HA H 1 5.38 0.02 . 1 . . . . . . . . 4886 1 536 . 1 1 153 153 LEU N N 15 128.0 0.1 . 1 . . . . . . . . 4886 1 537 . 1 1 153 153 LEU H H 1 9.14 0.02 . 1 . . . . . . . . 4886 1 538 . 1 1 153 153 LEU HA H 1 4.03 0.02 . 1 . . . . . . . . 4886 1 539 . 1 1 153 153 LEU HB2 H 1 1.93 0.02 . 2 . . . . . . . . 4886 1 540 . 1 1 153 153 LEU HB3 H 1 1.46 0.02 . 2 . . . . . . . . 4886 1 541 . 1 1 154 154 ASP N N 15 120.5 0.1 . 1 . . . . . . . . 4886 1 542 . 1 1 154 154 ASP H H 1 8.54 0.02 . 1 . . . . . . . . 4886 1 543 . 1 1 154 154 ASP HA H 1 4.72 0.02 . 1 . . . . . . . . 4886 1 544 . 1 1 154 154 ASP HB2 H 1 2.84 0.02 . 2 . . . . . . . . 4886 1 545 . 1 1 154 154 ASP HB3 H 1 2.72 0.02 . 2 . . . . . . . . 4886 1 546 . 1 1 155 155 ASN N N 15 114.9 0.1 . 1 . . . . . . . . 4886 1 547 . 1 1 155 155 ASN H H 1 9.01 0.02 . 1 . . . . . . . . 4886 1 548 . 1 1 155 155 ASN HA H 1 4.98 0.02 . 1 . . . . . . . . 4886 1 549 . 1 1 155 155 ASN HB2 H 1 2.98 0.02 . 2 . . . . . . . . 4886 1 550 . 1 1 155 155 ASN HB3 H 1 2.58 0.02 . 2 . . . . . . . . 4886 1 551 . 1 1 155 155 ASN ND2 N 15 109.4 0.1 . 1 . . . . . . . . 4886 1 552 . 1 1 155 155 ASN HD21 H 1 6.11 0.02 . 2 . . . . . . . . 4886 1 553 . 1 1 155 155 ASN HD22 H 1 8.73 0.02 . 2 . . . . . . . . 4886 1 554 . 1 1 156 156 GLN N N 15 117.0 0.1 . 9 . . . . . . . . 4886 1 555 . 1 1 156 156 GLN H H 1 7.44 0.02 . 9 . . . . . . . . 4886 1 556 . 1 1 156 156 GLN HA H 1 5.02 0.02 . 9 . . . . . . . . 4886 1 557 . 1 1 156 156 GLN HB2 H 1 2.26 0.02 . 2 . . . . . . . . 4886 1 558 . 1 1 156 156 GLN HB3 H 1 2.11 0.02 . 2 . . . . . . . . 4886 1 559 . 1 1 156 156 GLN NE2 N 15 114.4 0.1 . 1 . . . . . . . . 4886 1 560 . 1 1 156 156 GLN HE21 H 1 6.89 0.02 . 2 . . . . . . . . 4886 1 561 . 1 1 156 156 GLN HE22 H 1 7.81 0.02 . 9 . . . . . . . . 4886 1 562 . 1 1 157 157 SER N N 15 118.4 0.1 . 9 . . . . . . . . 4886 1 563 . 1 1 157 157 SER H H 1 8.77 0.02 . 9 . . . . . . . . 4886 1 564 . 1 1 157 157 SER HA H 1 4.08 0.02 . 1 . . . . . . . . 4886 1 565 . 1 1 157 157 SER HB2 H 1 4.19 0.02 . 2 . . . . . . . . 4886 1 566 . 1 1 158 158 GLY HA2 H 1 4.02 0.02 . 1 . . . . . . . . 4886 1 567 . 1 1 158 158 GLY HA3 H 1 4.02 0.02 . 1 . . . . . . . . 4886 1 568 . 1 1 159 159 LYS N N 15 117.3 0.1 . 1 . . . . . . . . 4886 1 569 . 1 1 159 159 LYS H H 1 7.46 0.02 . 1 . . . . . . . . 4886 1 570 . 1 1 159 159 LYS HA H 1 4.64 0.02 . 1 . . . . . . . . 4886 1 571 . 1 1 159 159 LYS HB2 H 1 2.11 0.02 . 2 . . . . . . . . 4886 1 572 . 1 1 159 159 LYS HB3 H 1 1.75 0.02 . 2 . . . . . . . . 4886 1 573 . 1 1 160 160 THR N N 15 117.2 0.1 . 1 . . . . . . . . 4886 1 574 . 1 1 160 160 THR H H 1 7.68 0.02 . 1 . . . . . . . . 4886 1 575 . 1 1 160 160 THR HA H 1 3.65 0.02 . 1 . . . . . . . . 4886 1 576 . 1 1 160 160 THR HB H 1 4.32 0.02 . 1 . . . . . . . . 4886 1 577 . 1 1 161 161 ASP N N 15 120.8 0.1 . 1 . . . . . . . . 4886 1 578 . 1 1 161 161 ASP H H 1 8.73 0.02 . 1 . . . . . . . . 4886 1 579 . 1 1 161 161 ASP HA H 1 4.33 0.02 . 1 . . . . . . . . 4886 1 580 . 1 1 161 161 ASP HB2 H 1 2.70 0.02 . 2 . . . . . . . . 4886 1 581 . 1 1 162 162 GLU N N 15 120.3 0.1 . 1 . . . . . . . . 4886 1 582 . 1 1 162 162 GLU H H 1 8.65 0.02 . 1 . . . . . . . . 4886 1 583 . 1 1 162 162 GLU HA H 1 4.25 0.02 . 1 . . . . . . . . 4886 1 584 . 1 1 162 162 GLU HB2 H 1 2.26 0.02 . 2 . . . . . . . . 4886 1 585 . 1 1 162 162 GLU HB3 H 1 2.19 0.02 . 2 . . . . . . . . 4886 1 586 . 1 1 163 163 ARG N N 15 121.4 0.1 . 1 . . . . . . . . 4886 1 587 . 1 1 163 163 ARG H H 1 8.09 0.02 . 1 . . . . . . . . 4886 1 588 . 1 1 163 163 ARG HA H 1 4.39 0.02 . 1 . . . . . . . . 4886 1 589 . 1 1 163 163 ARG HB2 H 1 1.98 0.02 . 2 . . . . . . . . 4886 1 590 . 1 1 163 163 ARG HB3 H 1 1.72 0.02 . 2 . . . . . . . . 4886 1 591 . 1 1 164 164 VAL N N 15 118.1 0.1 . 1 . . . . . . . . 4886 1 592 . 1 1 164 164 VAL H H 1 8.64 0.02 . 1 . . . . . . . . 4886 1 593 . 1 1 164 164 VAL HA H 1 3.39 0.02 . 1 . . . . . . . . 4886 1 594 . 1 1 164 164 VAL HB H 1 2.12 0.02 . 1 . . . . . . . . 4886 1 595 . 1 1 165 165 ALA N N 15 119.3 0.1 . 1 . . . . . . . . 4886 1 596 . 1 1 165 165 ALA H H 1 8.06 0.02 . 1 . . . . . . . . 4886 1 597 . 1 1 165 165 ALA HA H 1 3.99 0.02 . 1 . . . . . . . . 4886 1 598 . 1 1 165 165 ALA HB1 H 1 1.59 0.02 . 1 . . . . . . . . 4886 1 599 . 1 1 165 165 ALA HB2 H 1 1.59 0.02 . 1 . . . . . . . . 4886 1 600 . 1 1 165 165 ALA HB3 H 1 1.59 0.02 . 1 . . . . . . . . 4886 1 601 . 1 1 166 166 ALA N N 15 120.8 0.1 . 1 . . . . . . . . 4886 1 602 . 1 1 166 166 ALA H H 1 8.08 0.02 . 1 . . . . . . . . 4886 1 603 . 1 1 166 166 ALA HA H 1 4.45 0.02 . 1 . . . . . . . . 4886 1 604 . 1 1 166 166 ALA HB1 H 1 2.03 0.02 . 1 . . . . . . . . 4886 1 605 . 1 1 166 166 ALA HB2 H 1 2.03 0.02 . 1 . . . . . . . . 4886 1 606 . 1 1 166 166 ALA HB3 H 1 2.03 0.02 . 1 . . . . . . . . 4886 1 607 . 1 1 167 167 TRP N N 15 123.8 0.1 . 1 . . . . . . . . 4886 1 608 . 1 1 167 167 TRP H H 1 9.02 0.02 . 1 . . . . . . . . 4886 1 609 . 1 1 167 167 TRP HA H 1 4.45 0.02 . 1 . . . . . . . . 4886 1 610 . 1 1 167 167 TRP HB2 H 1 3.15 0.02 . 2 . . . . . . . . 4886 1 611 . 1 1 167 167 TRP HB3 H 1 2.72 0.02 . 2 . . . . . . . . 4886 1 612 . 1 1 167 167 TRP NE1 N 15 132.6 0.1 . 1 . . . . . . . . 4886 1 613 . 1 1 167 167 TRP HE1 H 1 11.18 0.02 . 1 . . . . . . . . 4886 1 614 . 1 1 168 168 LEU N N 15 117.2 0.1 . 1 . . . . . . . . 4886 1 615 . 1 1 168 168 LEU H H 1 8.87 0.02 . 1 . . . . . . . . 4886 1 616 . 1 1 168 168 LEU HA H 1 3.82 0.02 . 1 . . . . . . . . 4886 1 617 . 1 1 168 168 LEU HB2 H 1 2.08 0.02 . 2 . . . . . . . . 4886 1 618 . 1 1 168 168 LEU HB3 H 1 1.24 0.02 . 2 . . . . . . . . 4886 1 619 . 1 1 169 169 ALA N N 15 118.4 0.1 . 1 . . . . . . . . 4886 1 620 . 1 1 169 169 ALA H H 1 7.57 0.02 . 1 . . . . . . . . 4886 1 621 . 1 1 169 169 ALA HA H 1 4.13 0.02 . 1 . . . . . . . . 4886 1 622 . 1 1 169 169 ALA HB1 H 1 1.63 0.02 . 1 . . . . . . . . 4886 1 623 . 1 1 169 169 ALA HB2 H 1 1.63 0.02 . 1 . . . . . . . . 4886 1 624 . 1 1 169 169 ALA HB3 H 1 1.63 0.02 . 1 . . . . . . . . 4886 1 625 . 1 1 170 170 GLN N N 15 118.7 0.1 . 1 . . . . . . . . 4886 1 626 . 1 1 170 170 GLN H H 1 7.93 0.02 . 1 . . . . . . . . 4886 1 627 . 1 1 170 170 GLN HA H 1 4.24 0.02 . 1 . . . . . . . . 4886 1 628 . 1 1 170 170 GLN HB2 H 1 2.59 0.02 . 2 . . . . . . . . 4886 1 629 . 1 1 170 170 GLN NE2 N 15 110.5 0.1 . 1 . . . . . . . . 4886 1 630 . 1 1 170 170 GLN HE21 H 1 7.66 0.02 . 2 . . . . . . . . 4886 1 631 . 1 1 170 170 GLN HE22 H 1 7.87 0.02 . 2 . . . . . . . . 4886 1 632 . 1 1 171 171 ILE N N 15 110.4 0.1 . 1 . . . . . . . . 4886 1 633 . 1 1 171 171 ILE H H 1 7.99 0.02 . 1 . . . . . . . . 4886 1 634 . 1 1 171 171 ILE HA H 1 4.45 0.02 . 1 . . . . . . . . 4886 1 635 . 1 1 171 171 ILE HB H 1 1.91 0.02 . 1 . . . . . . . . 4886 1 636 . 1 1 172 172 ALA N N 15 125.4 0.1 . 1 . . . . . . . . 4886 1 637 . 1 1 172 172 ALA H H 1 7.85 0.02 . 1 . . . . . . . . 4886 1 638 . 1 1 172 172 ALA HA H 1 3.98 0.02 . 1 . . . . . . . . 4886 1 639 . 1 1 172 172 ALA HB1 H 1 1.68 0.02 . 1 . . . . . . . . 4886 1 640 . 1 1 172 172 ALA HB2 H 1 1.68 0.02 . 1 . . . . . . . . 4886 1 641 . 1 1 172 172 ALA HB3 H 1 1.68 0.02 . 1 . . . . . . . . 4886 1 642 . 1 1 173 173 PRO HA H 1 4.57 0.02 . 1 . . . . . . . . 4886 1 643 . 1 1 174 174 GLU N N 15 115.7 0.1 . 1 . . . . . . . . 4886 1 644 . 1 1 174 174 GLU H H 1 7.74 0.02 . 1 . . . . . . . . 4886 1 645 . 1 1 174 174 GLU HA H 1 4.38 0.02 . 1 . . . . . . . . 4886 1 646 . 1 1 174 174 GLU HB2 H 1 2.19 0.02 . 2 . . . . . . . . 4886 1 647 . 1 1 174 174 GLU HB3 H 1 2.14 0.02 . 2 . . . . . . . . 4886 1 648 . 1 1 175 175 PHE N N 15 116.6 0.1 . 1 . . . . . . . . 4886 1 649 . 1 1 175 175 PHE H H 1 7.70 0.02 . 1 . . . . . . . . 4886 1 650 . 1 1 175 175 PHE HA H 1 4.13 0.02 . 1 . . . . . . . . 4886 1 651 . 1 1 175 175 PHE HB2 H 1 2.90 0.02 . 2 . . . . . . . . 4886 1 652 . 1 1 175 175 PHE HB3 H 1 2.54 0.02 . 2 . . . . . . . . 4886 1 653 . 1 1 176 176 GLY N N 15 108.8 0.1 . 1 . . . . . . . . 4886 1 654 . 1 1 176 176 GLY H H 1 7.78 0.02 . 1 . . . . . . . . 4886 1 655 . 1 1 176 176 GLY HA2 H 1 3.92 0.02 . 2 . . . . . . . . 4886 1 656 . 1 1 176 176 GLY HA3 H 1 3.76 0.02 . 2 . . . . . . . . 4886 1 657 . 1 1 177 177 LEU N N 15 118.1 0.1 . 1 . . . . . . . . 4886 1 658 . 1 1 177 177 LEU H H 1 7.74 0.02 . 1 . . . . . . . . 4886 1 659 . 1 1 177 177 LEU HA H 1 4.46 0.02 . 1 . . . . . . . . 4886 1 660 . 1 1 177 177 LEU HB2 H 1 1.58 0.02 . 2 . . . . . . . . 4886 1 661 . 1 1 177 177 LEU HB3 H 1 1.36 0.02 . 2 . . . . . . . . 4886 1 662 . 1 1 178 178 SER N N 15 118.2 0.1 . 1 . . . . . . . . 4886 1 663 . 1 1 178 178 SER H H 1 8.66 0.02 . 1 . . . . . . . . 4886 1 664 . 1 1 178 178 SER HA H 1 4.64 0.02 . 1 . . . . . . . . 4886 1 665 . 1 1 178 178 SER HB2 H 1 3.97 0.02 . 2 . . . . . . . . 4886 1 666 . 1 1 178 178 SER HB3 H 1 3.85 0.02 . 2 . . . . . . . . 4886 1 667 . 1 1 179 179 LEU N N 15 131.5 0.1 . 1 . . . . . . . . 4886 1 668 . 1 1 179 179 LEU H H 1 8.04 0.02 . 1 . . . . . . . . 4886 1 669 . 1 1 179 179 LEU HA H 1 4.34 0.02 . 1 . . . . . . . . 4886 1 670 . 1 1 179 179 LEU HB2 H 1 1.64 0.02 . 2 . . . . . . . . 4886 1 stop_ save_ ######################## # Coupling constants # ######################## save_J-values_set_1 _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode J-values_set_1 _Coupling_constant_list.Entry_ID 4886 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $Conditions_sample_1 _Coupling_constant_list.Spectrometer_frequency_1H 500 _Coupling_constant_list.Details . _Coupling_constant_list.Text_data_format . _Coupling_constant_list.Text_data . loop_ _Coupling_constant_experiment.Experiment_ID _Coupling_constant_experiment.Experiment_name _Coupling_constant_experiment.Sample_ID _Coupling_constant_experiment.Sample_label _Coupling_constant_experiment.Sample_state _Coupling_constant_experiment.Entry_ID _Coupling_constant_experiment.Coupling_constant_list_ID . . 1 $sample_1 . 4886 1 stop_ loop_ _Coupling_constant.ID _Coupling_constant.Code _Coupling_constant.Assembly_atom_ID_1 _Coupling_constant.Entity_assembly_ID_1 _Coupling_constant.Entity_ID_1 _Coupling_constant.Comp_index_ID_1 _Coupling_constant.Seq_ID_1 _Coupling_constant.Comp_ID_1 _Coupling_constant.Atom_ID_1 _Coupling_constant.Atom_type_1 _Coupling_constant.Atom_isotope_number_1 _Coupling_constant.Ambiguity_code_1 _Coupling_constant.Assembly_atom_ID_2 _Coupling_constant.Entity_assembly_ID_2 _Coupling_constant.Entity_ID_2 _Coupling_constant.Comp_index_ID_2 _Coupling_constant.Seq_ID_2 _Coupling_constant.Comp_ID_2 _Coupling_constant.Atom_ID_2 _Coupling_constant.Atom_type_2 _Coupling_constant.Atom_isotope_number_2 _Coupling_constant.Ambiguity_code_2 _Coupling_constant.Val _Coupling_constant.Val_min _Coupling_constant.Val_max _Coupling_constant.Val_err _Coupling_constant.Resonance_ID_1 _Coupling_constant.Resonance_ID_2 _Coupling_constant.Auth_entity_assembly_ID_1 _Coupling_constant.Auth_seq_ID_1 _Coupling_constant.Auth_comp_ID_1 _Coupling_constant.Auth_atom_ID_1 _Coupling_constant.Auth_entity_assembly_ID_2 _Coupling_constant.Auth_seq_ID_2 _Coupling_constant.Auth_comp_ID_2 _Coupling_constant.Auth_atom_ID_2 _Coupling_constant.Details _Coupling_constant.Entry_ID _Coupling_constant.Coupling_constant_list_ID 1 3JHNHA . 1 1 5 5 LEU H . . . . 1 1 5 5 LEU HA . . . 9.7 . . 0.5 . . . . . . . . . . . 4886 1 2 3JHNHA . 1 1 6 6 PHE H . . . . 1 1 6 6 PHE HA . . . 11.7 . . 0.5 . . . . . . . . . . . 4886 1 3 3JHNHA . 1 1 17 17 VAL H . . . . 1 1 17 17 VAL HA . . . 5.4 . . 0.5 . . . . . . . . . . . 4886 1 4 3JHNHA . 1 1 18 18 ALA H . . . . 1 1 18 18 ALA HA . . . 2.2 . . 0.5 . . . . . . . . . . . 4886 1 5 3JHNHA . 1 1 19 19 LYS H . . . . 1 1 19 19 LYS HA . . . 4.0 . . 0.5 . . . . . . . . . . . 4886 1 6 3JHNHA . 1 1 21 21 ILE H . . . . 1 1 21 21 ILE HA . . . 6.3 . . 0.5 . . . . . . . . . . . 4886 1 7 3JHNHA . 1 1 22 22 LYS H . . . . 1 1 22 22 LYS HA . . . 3.2 . . 0.5 . . . . . . . . . . . 4886 1 8 3JHNHA . 1 1 24 24 ARG H . . . . 1 1 24 24 ARG HA . . . 8.1 . . 0.5 . . . . . . . . . . . 4886 1 9 3JHNHA . 1 1 25 25 PHE H . . . . 1 1 25 25 PHE HA . . . 9.4 . . 0.5 . . . . . . . . . . . 4886 1 10 3JHNHA . 1 1 26 26 ASP H . . . . 1 1 26 26 ASP HA . . . 6.0 . . 0.5 . . . . . . . . . . . 4886 1 11 3JHNHA . 1 1 31 31 SER H . . . . 1 1 31 31 SER HA . . . 4.3 . . 0.5 . . . . . . . . . . . 4886 1 12 3JHNHA . 1 1 33 33 ALA H . . . . 1 1 33 33 ALA HA . . . 5.0 . . 0.5 . . . . . . . . . . . 4886 1 13 3JHNHA . 1 1 42 42 GLU H . . . . 1 1 42 42 GLU HA . . . 3.8 . . 0.5 . . . . . . . . . . . 4886 1 14 3JHNHA . 1 1 45 45 ALA H . . . . 1 1 45 45 ALA HA . . . 3.9 . . 0.5 . . . . . . . . . . . 4886 1 15 3JHNHA . 1 1 46 46 GLN H . . . . 1 1 46 46 GLN HA . . . 5.8 . . 0.5 . . . . . . . . . . . 4886 1 16 3JHNHA . 1 1 47 47 TYR H . . . . 1 1 47 47 TYR HA . . . 6.1 . . 0.5 . . . . . . . . . . . 4886 1 17 3JHNHA . 1 1 48 48 GLN H . . . . 1 1 48 48 GLN HA . . . 7.5 . . 0.5 . . . . . . . . . . . 4886 1 18 3JHNHA . 1 1 49 49 PHE H . . . . 1 1 49 49 PHE HA . . . 10.2 . . 0.5 . . . . . . . . . . . 4886 1 19 3JHNHA . 1 1 51 51 ILE H . . . . 1 1 51 51 ILE HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4886 1 20 3JHNHA . 1 1 52 52 LEU H . . . . 1 1 52 52 LEU HA . . . 9.4 . . 0.5 . . . . . . . . . . . 4886 1 21 3JHNHA . 1 1 69 69 ALA H . . . . 1 1 69 69 ALA HA . . . 5.7 . . 0.5 . . . . . . . . . . . 4886 1 22 3JHNHA . 1 1 74 74 TRP H . . . . 1 1 74 74 TRP HA . . . 5.7 . . 0.5 . . . . . . . . . . . 4886 1 23 3JHNHA . 1 1 80 80 LYS H . . . . 1 1 80 80 LYS HA . . . 3.8 . . 0.5 . . . . . . . . . . . 4886 1 24 3JHNHA . 1 1 81 81 ILE H . . . . 1 1 81 81 ILE HA . . . 10.5 . . 0.5 . . . . . . . . . . . 4886 1 25 3JHNHA . 1 1 82 82 GLU H . . . . 1 1 82 82 GLU HA . . . 1.9 . . 0.5 . . . . . . . . . . . 4886 1 26 3JHNHA . 1 1 83 83 GLY H . . . . 1 1 83 83 GLY HA2 . . . 4.5 . . 0.5 . . . . . . . . . . . 4886 1 27 3JHNHA . 1 1 84 84 LEU H . . . . 1 1 84 84 LEU HA . . . 7.7 . . 0.5 . . . . . . . . . . . 4886 1 28 3JHNHA . 1 1 85 85 ASP H . . . . 1 1 85 85 ASP HA . . . 8.7 . . 0.5 . . . . . . . . . . . 4886 1 29 3JHNHA . 1 1 88 88 GLY H . . . . 1 1 88 88 GLY HA2 . . . 3.0 . . 0.5 . . . . . . . . . . . 4886 1 30 3JHNHA . 1 1 90 90 THR H . . . . 1 1 90 90 THR HA . . . 8.5 . . 0.5 . . . . . . . . . . . 4886 1 31 3JHNHA . 1 1 91 91 VAL H . . . . 1 1 91 91 VAL HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4886 1 32 3JHNHA . 1 1 92 92 ALA H . . . . 1 1 92 92 ALA HA . . . 8.8 . . 0.5 . . . . . . . . . . . 4886 1 33 3JHNHA . 1 1 93 93 LEU H . . . . 1 1 93 93 LEU HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4886 1 34 3JHNHA . 1 1 94 94 PHE H . . . . 1 1 94 94 PHE HA . . . 8.4 . . 0.5 . . . . . . . . . . . 4886 1 35 3JHNHA . 1 1 101 101 GLY H . . . . 1 1 101 101 GLY HA2 . . . 4.7 . . 0.5 . . . . . . . . . . . 4886 1 36 3JHNHA . 1 1 101 101 GLY H . . . . 1 1 101 101 GLY HA3 . . . 5.6 . . 0.5 . . . . . . . . . . . 4886 1 37 3JHNHA . 1 1 102 102 TYR H . . . . 1 1 102 102 TYR HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4886 1 38 3JHNHA . 1 1 110 110 LEU H . . . . 1 1 110 110 LEU HA . . . 6.4 . . 0.5 . . . . . . . . . . . 4886 1 39 3JHNHA . 1 1 115 115 SER H . . . . 1 1 115 115 SER HA . . . 3.1 . . 0.5 . . . . . . . . . . . 4886 1 40 3JHNHA . 1 1 117 117 PHE H . . . . 1 1 117 117 PHE HA . . . 5.9 . . 0.5 . . . . . . . . . . . 4886 1 41 3JHNHA . 1 1 120 120 ARG H . . . . 1 1 120 120 ARG HA . . . 10.0 . . 0.5 . . . . . . . . . . . 4886 1 42 3JHNHA . 1 1 121 121 GLY H . . . . 1 1 121 121 GLY HA2 . . . 4.1 . . 0.5 . . . . . . . . . . . 4886 1 43 3JHNHA . 1 1 123 123 LYS H . . . . 1 1 123 123 LYS HA . . . 9.3 . . 0.5 . . . . . . . . . . . 4886 1 44 3JHNHA . 1 1 124 124 ILE H . . . . 1 1 124 124 ILE HA . . . 9.6 . . 0.5 . . . . . . . . . . . 4886 1 45 3JHNHA . 1 1 125 125 VAL H . . . . 1 1 125 125 VAL HA . . . 10.5 . . 0.5 . . . . . . . . . . . 4886 1 46 3JHNHA . 1 1 126 126 GLY H . . . . 1 1 126 126 GLY HA2 . . . 3.0 . . 0.5 . . . . . . . . . . . 4886 1 47 3JHNHA . 1 1 128 128 TRP H . . . . 1 1 128 128 TRP HA . . . 10.2 . . 0.5 . . . . . . . . . . . 4886 1 48 3JHNHA . 1 1 129 129 SER H . . . . 1 1 129 129 SER HA . . . 3.5 . . 0.5 . . . . . . . . . . . 4886 1 49 3JHNHA . 1 1 131 131 ASP H . . . . 1 1 131 131 ASP HA . . . 3.2 . . 0.5 . . . . . . . . . . . 4886 1 50 3JHNHA . 1 1 132 132 GLY H . . . . 1 1 132 132 GLY HA2 . . . 4.3 . . 0.5 . . . . . . . . . . . 4886 1 51 3JHNHA . 1 1 134 134 GLU H . . . . 1 1 134 134 GLU HA . . . 10.0 . . 0.5 . . . . . . . . . . . 4886 1 52 3JHNHA . 1 1 136 136 GLU H . . . . 1 1 136 136 GLU HA . . . 10.9 . . 0.5 . . . . . . . . . . . 4886 1 53 3JHNHA . 1 1 140 140 ALA H . . . . 1 1 140 140 ALA HA . . . 8.7 . . 0.5 . . . . . . . . . . . 4886 1 54 3JHNHA . 1 1 141 141 VAL H . . . . 1 1 141 141 VAL HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4886 1 55 3JHNHA . 1 1 142 142 VAL H . . . . 1 1 142 142 VAL HA . . . 10.0 . . 0.5 . . . . . . . . . . . 4886 1 56 3JHNHA . 1 1 143 143 ASP H . . . . 1 1 143 143 ASP HA . . . 7.1 . . 0.5 . . . . . . . . . . . 4886 1 57 3JHNHA . 1 1 144 144 GLY H . . . . 1 1 144 144 GLY HA2 . . . 3.8 . . 0.5 . . . . . . . . . . . 4886 1 58 3JHNHA . 1 1 144 144 GLY H . . . . 1 1 144 144 GLY HA3 . . . 5.7 . . 0.5 . . . . . . . . . . . 4886 1 59 3JHNHA . 1 1 145 145 LYS H . . . . 1 1 145 145 LYS HA . . . 8.9 . . 0.5 . . . . . . . . . . . 4886 1 60 3JHNHA . 1 1 146 146 PHE H . . . . 1 1 146 146 PHE HA . . . 6.1 . . 0.5 . . . . . . . . . . . 4886 1 61 3JHNHA . 1 1 148 148 GLY H . . . . 1 1 148 148 GLY HA2 . . . 1.5 . . 0.5 . . . . . . . . . . . 4886 1 62 3JHNHA . 1 1 150 150 ALA H . . . . 1 1 150 150 ALA HA . . . 8.8 . . 0.5 . . . . . . . . . . . 4886 1 63 3JHNHA . 1 1 151 151 LEU H . . . . 1 1 151 151 LEU HA . . . 8.8 . . 0.5 . . . . . . . . . . . 4886 1 64 3JHNHA . 1 1 154 154 ASP H . . . . 1 1 154 154 ASP HA . . . 8.5 . . 0.5 . . . . . . . . . . . 4886 1 65 3JHNHA . 1 1 155 155 ASN H . . . . 1 1 155 155 ASN HA . . . 5.8 . . 0.5 . . . . . . . . . . . 4886 1 66 3JHNHA . 1 1 161 161 ASP H . . . . 1 1 161 161 ASP HA . . . 3.0 . . 0.5 . . . . . . . . . . . 4886 1 67 3JHNHA . 1 1 162 162 GLU H . . . . 1 1 162 162 GLU HA . . . 3.7 . . 0.5 . . . . . . . . . . . 4886 1 68 3JHNHA . 1 1 167 167 TRP H . . . . 1 1 167 167 TRP HA . . . 3.6 . . 0.5 . . . . . . . . . . . 4886 1 69 3JHNHA . 1 1 168 168 LEU H . . . . 1 1 168 168 LEU HA . . . 2.7 . . 0.5 . . . . . . . . . . . 4886 1 70 3JHNHA . 1 1 170 170 GLN H . . . . 1 1 170 170 GLN HA . . . 5.5 . . 0.5 . . . . . . . . . . . 4886 1 71 3JHNHA . 1 1 171 171 ILE H . . . . 1 1 171 171 ILE HA . . . 8.3 . . 0.5 . . . . . . . . . . . 4886 1 72 3JHNHA . 1 1 172 172 ALA H . . . . 1 1 172 172 ALA HA . . . 0.4 . . 0.5 . . . . . . . . . . . 4886 1 73 3JHNHA . 1 1 174 174 GLU H . . . . 1 1 174 174 GLU HA . . . 7.7 . . 0.5 . . . . . . . . . . . 4886 1 74 3JHNHA . 1 1 177 177 LEU H . . . . 1 1 177 177 LEU HA . . . 8.9 . . 0.5 . . . . . . . . . . . 4886 1 75 3JHNHA . 1 1 178 178 SER H . . . . 1 1 178 178 SER HA . . . 8.8 . . 0.5 . . . . . . . . . . . 4886 1 76 3JHNHA . 1 1 179 179 LEU H . . . . 1 1 179 179 LEU HA . . . 9.5 . . 0.5 . . . . . . . . . . . 4886 1 stop_ save_