data_5480 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5480 _Entry.Title ; 1H,15N and 13C assigned Chemical Shifts for a complex of calmodulin with a peptide of the olfactory CNGC channel ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2002-07-25 _Entry.Accession_date 2002-07-25 _Entry.Last_release_date 2003-12-08 _Entry.Original_release_date 2003-12-08 _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 Maria Orsale . . . 5480 2 Sonia Melino . . . 5480 3 Vincent Torre . . . 5480 4 Andrea Motta . . . 5480 5 Maurizio Paci . . . 5480 6 Alessandro Desideri . . . 5480 7 Daniel Cicero . . . 5480 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5480 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 1141 5480 '13C chemical shifts' 664 5480 '15N chemical shifts' 157 5480 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 . . 2003-12-08 2002-07-25 original author . 5480 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5480 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12885399 _Citation.Full_citation . _Citation.Title ; Two distinct calcium-calmodulin interactions with N-terminal regions of the olfactory and rod cyclic nucleotide-gated channels characterized by NMR spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full . _Citation.Journal_volume 548 _Citation.Journal_issue 1-3 _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 11 _Citation.Page_last 16 _Citation.Year 2003 _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 Maria Orsale . . . 5480 1 2 Sonia Melino . . . 5480 1 3 G. Contessa . M. . 5480 1 4 Vincent Torre . . . 5480 1 5 G. Andreotti . . . 5480 1 6 Andrea Motta . . . 5480 1 7 Maurizio Paci . . . 5480 1 8 Alessandro Desideri . . . 5480 1 9 Daniel Cicero . . . 5480 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5480 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10493800 _Citation.Full_citation ; Elshorst B, Hennig M, Forsterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E. NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Biochemistry. 1999 Sep 21;38(38):12320-32. ; _Citation.Title 'NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 38 _Citation.Journal_issue 38 _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 12320 _Citation.Page_last 12332 _Citation.Year 1999 _Citation.Details ; The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the plasma membrane calcium pump, the peptide C20W, has been solved by heteronuclear three-dimensional nuclear magnetic resonance (NMR) spectroscopy. The structure calculation is based on a total of 1808 intramolecular NOEs and 49 intermolecular NOEs between the peptide C20W and calmodulin from heteronuclear-filtered NOESY spectra and a half-filtered experiment, respectively. Chemical shift differences between free Ca(2+)-saturated CaM and its complex with C20W as well as the structure calculation reveal that C20W binds solely to the C-terminal half of CaM. In addition, comparison of the methyl resonances of the nine assigned methionine residues of free Ca(2+)-saturated CaM with those of the CaM/C20W complex revealed a significant difference between the N-terminal and the C-terminal domain; i.e., resonances in the N-terminal domain of the complex were much more similar to those reported for free CaM in contrast to those in the C-terminal half which were significantly different not only from the resonances of free CaM but also from those reported for the CaM/M13 complex. As a consequence, the global structure of the CaM/C20W complex is unusual, i.e., different from other peptide calmodulin complexes, since we find no indication for a collapsed structure. The fine modulation in the peptide protein interface shows a number of differences to the CaM/M13 complex studied by Ikura et al. [Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Science 256, 632-638]. The unusual binding mode to only the C-terminal half of CaM is in agreement with the biochemical observation that the calcium pump can be activated by the C-terminal half of CaM alone [Guerini, D., Krebs, J., and Carafoli, E. (1984) J. Biol. Chem. 259, 15172-15177]. ; 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 B. Elshorst B. . . 5480 2 2 M. Hennig M. . . 5480 2 3 H. Forsterling H. . . 5480 2 4 A. Diener A. . . 5480 2 5 M. Maurer M. . . 5480 2 6 P. Schulte P. . . 5480 2 7 H. Schwalbe H. . . 5480 2 8 C. Griesinger C. . . 5480 2 9 J. Krebs J. . . 5480 2 10 H. Schmid H. . . 5480 2 11 T. Vorherr T. . . 5480 2 12 E. Carafoli E. . . 5480 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5480 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7552747 _Citation.Full_citation ; Zhang M, Tanaka T, Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol. 1995 Sep;2(9):758-67. ; _Citation.Title 'Calcium-induced conformational transition revealed by the solution structure of apo calmodulin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature structural biology' _Citation.Journal_volume 2 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1072-8368 _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 758 _Citation.Page_last 767 _Citation.Year 1995 _Citation.Details ; The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains. ; 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. Zhang M. . . 5480 3 2 T. Tanaka T. . . 5480 3 3 M. Ikura M. . . 5480 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5480 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1519061 _Citation.Full_citation ; Meador WE, Means AR, Quiocho FA. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science. 1992 Aug 28;257(5074):1251-5. ; _Citation.Title 'Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Science _Citation.Journal_name_full 'Science (New York, N.Y.)' _Citation.Journal_volume 257 _Citation.Journal_issue 5074 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0036-8075 _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 1251 _Citation.Page_last 1255 _Citation.Year 1992 _Citation.Details ; The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (A). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (less than 4 A) are formed between CaM and the peptide, with van der Waals contacts comprising approximately 80% of this total. ; 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 W.E. Meador W. E. . 5480 4 2 A.R. Means A. R. . 5480 4 3 F.A. Quiocho F. A. . 5480 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 5480 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7552748 _Citation.Full_citation ; Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol. 1995 Sep;2(9):768-76. ; _Citation.Title 'Solution structure of calcium-free calmodulin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature structural biology' _Citation.Journal_volume 2 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1072-8368 _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 768 _Citation.Page_last 776 _Citation.Year 1995 _Citation.Details ; The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings. In analogy with the Ca(2+)-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel beta-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca(2+)-free N-terminal domain of troponin C. ; 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 H. Kuboniwa H. . . 5480 5 2 N. Tjandra N. . . 5480 5 3 S. Grzesiek S. . . 5480 5 4 H. Ren H. . . 5480 5 5 C.B. Klee C. B. . 5480 5 6 A. Bax A. . . 5480 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 5480 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7803388 _Citation.Full_citation ; Cook WJ, Walter LJ, Walter MR. Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex. Biochemistry. 1994 Dec 27;33(51):15259-65. ; _Citation.Title 'Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 33 _Citation.Journal_issue 51 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 15259 _Citation.Page_last 15265 _Citation.Year 1994 _Citation.Details ; The crystal structure of calmodulin (CaM) bound to trifluoperazine (TFP) has been determined and refined to a resolution of 2.45 A. Only one TFP is bound to CaM, but that is sufficient to cause distortion of the central alpha-helix and juxtaposition of the N- and C-terminal domains similar to that seen in CaM-polypeptide complexes. The drug makes extensive contacts with residues in the C-terminal domain of CaM but only a few contacts with one residue in the N-terminal domain. The structure suggests that substrate binding to the C-terminal domain is sufficient to cause the conformational changes in calmodulin that lead to activation of its targets. ; 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 W.J. Cook W. J. . 5480 6 2 L.J. Walter L. J. . 5480 6 3 M.R. Walter M. R. . 5480 6 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 5480 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1474585 _Citation.Full_citation ; Chattopadhyaya R, Meador WE, Means AR, Quiocho FA. Calmodulin structure refined at 1.7 A resolution. J Mol Biol. 1992 Dec 20;228(4):1177-92. ; _Citation.Title 'Calmodulin structure refined at 1.7 A resolution.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 228 _Citation.Journal_issue 4 _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 1177 _Citation.Page_last 1192 _Citation.Year 1992 _Citation.Details ; We have determined and refined the crystal structure of a recombinant calmodulin at 1.7 A resolution. The structure was determined by molecular replacement, using the 2.2 A published native bovine brain structure as the starting model. The final crystallographic R-factor, using 14,469 reflections in the 10.0 to 1.7 A range with structure factors exceeding 0.5 sigma, is 0.216. Bond lengths and bond angle distances have root-mean-square deviations from ideal values of 0.009 A and 0.032 A, respectively. The final model consists of 1279 non-hydrogen atoms, including four calcium ions, 1130 protein atoms, including three Asp118 side-chain atoms in double conformation, 139 water molecules and one ethanol molecule. The electron densities for residues 1 to 4 and 148 of calmodulin are poorly defined, and not included in our model, except for main-chain atoms of residue 4. The calmodulin structure from our crystals is very similar to the earlier 2.2 A structure described by Babu and coworkers with a root-mean-square deviation of 0.36 A. Calmodulin remains a dumb-bell-shaped molecule, with similar lobes and connected by a central alpha-helix. Each lobe contains three alpha-helices and two Ca2+ binding EF hand loops, with a short antiparallel beta-sheet between adjacent EF hand loops and one non-EF hand loop. There are some differences in the structure of the central helix. The crystal packing is extensively studied, and facile crystal growth along the z-axis of the triclinic crystals is explained. Herein, we describe hydrogen bonding in the various secondary structure elements and hydration of calmodulin. ; 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 R. Chattopadhyaya R. . . 5480 7 2 W.E. Meador W. E. . 5480 7 3 A.R. Means A. R. . 5480 7 4 F.A. Quiocho F. A. . 5480 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 5480 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7634090 _Citation.Full_citation ; Vandonselaar M, Hickie RA, Quail JW, Delbaere LT. Trifluoperazine-induced conformational change in Ca(2+)-calmodulin. Nat Struct Biol. 1994 Nov;1(11):795-801. ; _Citation.Title 'Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature structural biology' _Citation.Journal_volume 1 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1072-8368 _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 795 _Citation.Page_last 801 _Citation.Year 1994 _Citation.Details ; Here we show that, as a consequence of binding the drug trifluoperazine, a major conformational movement occurs in Ca(2+)-calmodulin (CaM). The tertiary structure changes from an elongated dumb-bell, with exposed hydrophobic surfaces, to a compact globular form which can no longer interact with its target enzymes. It is likely that inactivation of Ca(2+)-CaM by trifluoperazine is due to this major tertiary-structural alteration in Ca(2+)-CaM, which is initiated and stabilized by drug binding. This conformational change is similar to that which occurs on the binding of Ca(2+)-CaM to target peptides. Two hydrophobic binding pockets, created by amino acid residues adjacent to Ca(2+)-coordinating residues, form the key recognition sites on Ca(2+)-CaM for both inhibitors and target enzymes. ; 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. Vandonselaar M. . . 5480 8 2 R.A. Hickie R. A. . 5480 8 3 J.W. Quail J. W. . 5480 8 4 L.T. Delbaere L. T. . 5480 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 5480 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9438860 _Citation.Full_citation ; Wall ME, Clarage JB, Phillips GN. Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering. Structure. 1997 Dec 15;5(12):1599-612. ; _Citation.Title 'Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full 'Structure (London, England : 1993)' _Citation.Journal_volume 5 _Citation.Journal_issue 12 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0969-2126 _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 1599 _Citation.Page_last 1612 _Citation.Year 1997 _Citation.Details ; BACKGROUND: Calmodulin is a calcium-activated regulatory protein which can bind to many different targets. The protein resembles a highly flexible dumbbell, and bends in the middle as it binds. This and other motions must be understood to formulate a realistic model of calmodulin function. RESULTS: Using the Bragg reflections from X-ray crystallography, a multiple-conformer refinement of a calmodulin-peptide complex shows anisotropic displacements, with high variations of dihedral angles in several nonhelical domains: the flexible linker; three of the four calcium-binding sites (including both of the N-terminal sites); and a turn connecting the C-terminal EF-hand calcium-binding domains. Three-dimensional maps of the large scale diffuse X-ray scattering data show isotropic liquid-like motions with an unusually small correlation length. Three-dimensional maps of the small scale diffuse streaks show highly coupled, anisotropic motions along the head-to-tail molecular packing direction in the unit cell. There is also weak coupling perpendicular to the head-to-tail packing direction, particularly across a cavity occupied by the disordered linker domain of the molecule. CONCLUSIONS: Together, the Bragg and diffuse scattering present a self-consistent description of the motions in the flexible linker of calmodulin. The other mobile regions of the protein are also of great interest. In particular, the high variations in the calcium-binding sites are likely to influence how strongly they bind ions. This is especially important in the N-terminal sites, which regulate the activity of the molecule. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M.E. Wall M. E. . 5480 9 2 J.B. Clarage J. B. . 5480 9 3 G.N. Phillips G. N. . 5480 9 stop_ save_ save_ref_10 _Citation.Sf_category citations _Citation.Sf_framecode ref_10 _Citation.Entry_ID 5480 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9514729 _Citation.Full_citation ; Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M. Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition. J Mol Biol. 1998 Feb 13;276(1):165-76. ; _Citation.Title 'Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 276 _Citation.Journal_issue 1 _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 165 _Citation.Page_last 176 _Citation.Year 1998 _Citation.Details ; The solution structure of calcium-bound calmodulin (CaM) complexed with an antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has been determined by multidimensional NMR spectroscopy. The structure consists of one molecule of W-7 binding to each of the two domains of CaM. In each domain, the W-7 chloronaphthalene ring interacts with four methionine methyl groups and other aliphatic or aromatic side-chains in a deep hydrophobic pocket, the site responsible for CaM binding to CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM kinase II. This competitive binding at the same site between W-7 and CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to activate the enzymes. The orientation of the W-7 naphthalene ring in the N-terminal pocket is rotated approximately 40 degrees with respect to that in the C-terminal pocket. The W-7 ring orientation differs significantly from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal pocket and the phenothiazine ring of trifluoperazine bound to the N or C-terminal pocket. These comparative structural analyses demonstrate that the two hydrophobic pockets of CaM can accommodate a variety of bulky aromatic rings, which provides a plausible structural basis for the diversity in CaM-mediated molecular recognition. ; 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. Osawa M. . . 5480 10 2 M.B. Swindells M. B. . 5480 10 3 J. Tanikawa J. . . 5480 10 4 T. Tanaka T. . . 5480 10 5 T. Mase T. . . 5480 10 6 T. Furuya T. . . 5480 10 7 M. Ikura M. . . 5480 10 stop_ save_ save_ref_11 _Citation.Sf_category citations _Citation.Sf_framecode ref_11 _Citation.Entry_ID 5480 _Citation.ID 11 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10467092 _Citation.Full_citation ; Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M. A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase. Nat Struct Biol. 1999 Sep;6(9):819-24. ; _Citation.Title 'A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature structural biology' _Citation.Journal_volume 6 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1072-8368 _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 819 _Citation.Page_last 824 _Citation.Year 1999 _Citation.Details ; The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins. ; 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. Osawa M. . . 5480 11 2 H. Tokumitsu H. . . 5480 11 3 M.B. Swindells M. B. . 5480 11 4 H. Kurihara H. . . 5480 11 5 M. Orita M. . . 5480 11 6 T. Shibanuma T. . . 5480 11 7 T. Furuya T. . . 5480 11 8 M. Ikura M. . . 5480 11 stop_ save_ save_ref_15 _Citation.Sf_category citations _Citation.Sf_framecode ref_15 _Citation.Entry_ID 5480 _Citation.ID 12 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; 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 F. Delaglio F. . . 5480 12 2 S. Grzesiek S. . . 5480 12 3 G.W. Vuister G. W. . 5480 12 4 G. Zhu G. . . 5480 12 5 J. Pfeifer J. . . 5480 12 6 A. Bax A. . . 5480 12 stop_ save_ save_ref_16 _Citation.Sf_category citations _Citation.Sf_framecode ref_16 _Citation.Entry_ID 5480 _Citation.ID 13 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Johnson, B. and Blevins R.A.(1994) J.Biomol.NMR, 4, 603-614 A computer program for the visualisation and analysis of NMR data. ; _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_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CaM-bOCNC_complex _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CaM-bOCNC_complex _Assembly.Entry_ID 5480 _Assembly.ID 1 _Assembly.Name 'Calmodulin-olfactory channel peptide complex' _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 ; PDB 1CFF A Chain A,NMR solution structure of A complex of calmodulin with A Binding Peptide Of The Ca2+-Pump. PDB 1DMO Calmodulin, NMR ,30 structures. PDB 1CDL B Chain B, calmodulin complexed with calmodulin-binding peptide F. PDB 1CFC Calcium-free calmodulin. PDB 1CTR Calcium complexed with Trifluoperazine (1:1). PDB 1CLL Calmodulin (vertebrate). PDB 1LIN Calmodulin complexed with Trifluoperazine (1:4). PDB 1CM1 A Chain A,Motions of calmodulin-Single-conformer-refinement. PDB 1CM4 A Chain A,Motions of calmodulin-Four-conformer-refinement. PDB 1MUX Solution NMR structureof calmodulinW-7 Complex: the basis of diversity in molecular recognition, 30 structures. PDB 1CKK A chain A,calmodulinRAT Ca2+calmodulin dependent protein kinase fragment. PDB 1A29 Calmodulin Complexed With Trifluoperazine (1:2 Complex). PDB 1QIV A Chain A, Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'- [1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex. PDB 1QIW A Chain A, Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'- [1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd). ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5480 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 calmodulin 1 $CaM . . . native . . . . . 5480 1 2 'olfactory channel peptide' 2 $bOCNC . . . native . . . . . 5480 1 3 'Calcium ion, I' 3 $CA . . . native . . . . . 5480 1 4 'Calcium ion, II' 3 $CA . . . native . . . . . 5480 1 5 'Calcium ion, III' 3 $CA . . . native . . . . . 5480 1 6 'Calcium ion, IV' 3 $CA . . . native . . . . . 5480 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1CFF . . . . . 'A Chain A,NMR solution structure of A complex of calmodulin with A Binding Peptide Of The Ca2+-Pump' 5480 1 . PDB 1DMO . . . . . 'Calmodulin, NMR ,30 structures' 5480 1 . PDB 1CDL . . . . . 'B Chain B, calmodulin complexed with calmodulin-binding peptide F.' 5480 1 . PDB 1CFC . . . . . 'Calcium-free calmodulin' 5480 1 . PDB 1CTR . . . . . 'Calcium complexed with Trifluoperazine (1:1)' 5480 1 . PDB 1CLL . . . . . 'Calmodulin (vertebrate)' 5480 1 . PDB 1LIN . . . . . 'Calmodulin complexed with Trifluoperazine (1:4)' 5480 1 . PDB 1CM1 . . . . . 'A Chain A,Motions of calmodulin-Single-conformer-refinement' 5480 1 . PDB 1CM4 . . . . . 'A Chain A,Motions of calmodulin-Four-conformer-refinement' 5480 1 . PDB 1MUX . . . . . ; Solution NMR structureof calmodulinW-7 Complex: the basis of diversity in molecular recognition,30 structures ; 5480 1 . PDB 1CKK . . . . . 'A chain A,calmodulinRAT Ca2+calmodulin dependent protein kinase fragment.' 5480 1 . PDB 1A29 . . . . . 'Calmodulin Complexed With Trifluoperazine (1:2 Complex)' 5480 1 . PDB 1QIV . . . . . '\\"A Chain A, Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex\\' 5480 1 . PDB 1QIW . . . . . '\\"A Chain A, Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)\\' 5480 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Calmodulin-olfactory channel peptide complex' system 5480 1 'CaM-bOCNC complex' abbreviation 5480 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CaM _Entity.Sf_category entity _Entity.Sf_framecode CaM _Entity.Entry_ID 5480 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Calmodulin _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 ; ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK ; _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 CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers 148 _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 16700 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1SY9 . "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" . . . . . 100.00 26 100.00 100.00 1.62e-07 . . . . 5480 1 2 no EMBL CAA38754 . "cAMP-gated channel [Bos taurus]" . . . . . 100.00 663 100.00 100.00 8.30e-09 . . . . 5480 1 3 no PRF 1616224A . "cAMP-gated channel" . . . . . 100.00 663 100.00 100.00 8.30e-09 . . . . 5480 1 4 no REF NP_001001139 . "cyclic nucleotide-gated olfactory channel [Bos taurus]" . . . . . 100.00 663 100.00 100.00 8.30e-09 . . . . 5480 1 5 no REF XP_005227654 . "PREDICTED: cyclic nucleotide-gated olfactory channel isoform X1 [Bos taurus]" . . . . . 100.00 663 100.00 100.00 8.79e-09 . . . . 5480 1 6 no REF XP_010841839 . "PREDICTED: LOW QUALITY PROTEIN: cyclic nucleotide-gated olfactory channel [Bison bison bison]" . . . . . 100.00 666 100.00 100.00 6.53e-09 . . . . 5480 1 7 no SP Q03041 . "RecName: Full=Cyclic nucleotide-gated olfactory channel; AltName: Full=Cyclic nucleotide-gated cation channel 2; AltName: Full=" . . . . . 100.00 663 100.00 100.00 8.30e-09 . . . . 5480 1 8 no TPG DAA13266 . "TPA: cyclic nucleotide-gated olfactory channel [Bos taurus]" . . . . . 100.00 663 100.00 100.00 8.79e-09 . . . . 5480 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Calmodulin common 5480 1 CaM abbreviation 5480 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 . 5480 1 2 . ASP . 5480 1 3 . GLN . 5480 1 4 . LEU . 5480 1 5 . THR . 5480 1 6 . GLU . 5480 1 7 . GLU . 5480 1 8 . GLN . 5480 1 9 . ILE . 5480 1 10 . ALA . 5480 1 11 . GLU . 5480 1 12 . PHE . 5480 1 13 . LYS . 5480 1 14 . GLU . 5480 1 15 . ALA . 5480 1 16 . PHE . 5480 1 17 . SER . 5480 1 18 . LEU . 5480 1 19 . PHE . 5480 1 20 . ASP . 5480 1 21 . LYS . 5480 1 22 . ASP . 5480 1 23 . GLY . 5480 1 24 . ASP . 5480 1 25 . GLY . 5480 1 26 . THR . 5480 1 27 . ILE . 5480 1 28 . THR . 5480 1 29 . THR . 5480 1 30 . LYS . 5480 1 31 . GLU . 5480 1 32 . LEU . 5480 1 33 . GLY . 5480 1 34 . THR . 5480 1 35 . VAL . 5480 1 36 . MET . 5480 1 37 . ARG . 5480 1 38 . SER . 5480 1 39 . LEU . 5480 1 40 . GLY . 5480 1 41 . GLN . 5480 1 42 . ASN . 5480 1 43 . PRO . 5480 1 44 . THR . 5480 1 45 . GLU . 5480 1 46 . ALA . 5480 1 47 . GLU . 5480 1 48 . LEU . 5480 1 49 . GLN . 5480 1 50 . ASP . 5480 1 51 . MET . 5480 1 52 . ILE . 5480 1 53 . ASN . 5480 1 54 . GLU . 5480 1 55 . VAL . 5480 1 56 . ASP . 5480 1 57 . ALA . 5480 1 58 . ASP . 5480 1 59 . GLY . 5480 1 60 . ASN . 5480 1 61 . GLY . 5480 1 62 . THR . 5480 1 63 . ILE . 5480 1 64 . ASP . 5480 1 65 . PHE . 5480 1 66 . PRO . 5480 1 67 . GLU . 5480 1 68 . PHE . 5480 1 69 . LEU . 5480 1 70 . THR . 5480 1 71 . MET . 5480 1 72 . MET . 5480 1 73 . ALA . 5480 1 74 . ARG . 5480 1 75 . LYS . 5480 1 76 . MET . 5480 1 77 . LYS . 5480 1 78 . ASP . 5480 1 79 . THR . 5480 1 80 . ASP . 5480 1 81 . SER . 5480 1 82 . GLU . 5480 1 83 . GLU . 5480 1 84 . GLU . 5480 1 85 . ILE . 5480 1 86 . ARG . 5480 1 87 . GLU . 5480 1 88 . ALA . 5480 1 89 . PHE . 5480 1 90 . ARG . 5480 1 91 . VAL . 5480 1 92 . PHE . 5480 1 93 . ASP . 5480 1 94 . LYS . 5480 1 95 . ASP . 5480 1 96 . GLY . 5480 1 97 . ASN . 5480 1 98 . GLY . 5480 1 99 . TYR . 5480 1 100 . ILE . 5480 1 101 . SER . 5480 1 102 . ALA . 5480 1 103 . ALA . 5480 1 104 . GLU . 5480 1 105 . LEU . 5480 1 106 . ARG . 5480 1 107 . HIS . 5480 1 108 . VAL . 5480 1 109 . MET . 5480 1 110 . THR . 5480 1 111 . ASN . 5480 1 112 . LEU . 5480 1 113 . GLY . 5480 1 114 . GLU . 5480 1 115 . LYS . 5480 1 116 . LEU . 5480 1 117 . THR . 5480 1 118 . ASP . 5480 1 119 . GLU . 5480 1 120 . GLU . 5480 1 121 . VAL . 5480 1 122 . ASP . 5480 1 123 . GLU . 5480 1 124 . MET . 5480 1 125 . ILE . 5480 1 126 . ARG . 5480 1 127 . GLU . 5480 1 128 . ALA . 5480 1 129 . ASP . 5480 1 130 . ILE . 5480 1 131 . ASP . 5480 1 132 . GLY . 5480 1 133 . ASP . 5480 1 134 . GLY . 5480 1 135 . GLN . 5480 1 136 . VAL . 5480 1 137 . ASN . 5480 1 138 . TYR . 5480 1 139 . GLU . 5480 1 140 . GLU . 5480 1 141 . PHE . 5480 1 142 . VAL . 5480 1 143 . GLN . 5480 1 144 . MET . 5480 1 145 . MET . 5480 1 146 . THR . 5480 1 147 . ALA . 5480 1 148 . LYS . 5480 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 5480 1 . ASP 2 2 5480 1 . GLN 3 3 5480 1 . LEU 4 4 5480 1 . THR 5 5 5480 1 . GLU 6 6 5480 1 . GLU 7 7 5480 1 . GLN 8 8 5480 1 . ILE 9 9 5480 1 . ALA 10 10 5480 1 . GLU 11 11 5480 1 . PHE 12 12 5480 1 . LYS 13 13 5480 1 . GLU 14 14 5480 1 . ALA 15 15 5480 1 . PHE 16 16 5480 1 . SER 17 17 5480 1 . LEU 18 18 5480 1 . PHE 19 19 5480 1 . ASP 20 20 5480 1 . LYS 21 21 5480 1 . ASP 22 22 5480 1 . GLY 23 23 5480 1 . ASP 24 24 5480 1 . GLY 25 25 5480 1 . THR 26 26 5480 1 . ILE 27 27 5480 1 . THR 28 28 5480 1 . THR 29 29 5480 1 . LYS 30 30 5480 1 . GLU 31 31 5480 1 . LEU 32 32 5480 1 . GLY 33 33 5480 1 . THR 34 34 5480 1 . VAL 35 35 5480 1 . MET 36 36 5480 1 . ARG 37 37 5480 1 . SER 38 38 5480 1 . LEU 39 39 5480 1 . GLY 40 40 5480 1 . GLN 41 41 5480 1 . ASN 42 42 5480 1 . PRO 43 43 5480 1 . THR 44 44 5480 1 . GLU 45 45 5480 1 . ALA 46 46 5480 1 . GLU 47 47 5480 1 . LEU 48 48 5480 1 . GLN 49 49 5480 1 . ASP 50 50 5480 1 . MET 51 51 5480 1 . ILE 52 52 5480 1 . ASN 53 53 5480 1 . GLU 54 54 5480 1 . VAL 55 55 5480 1 . ASP 56 56 5480 1 . ALA 57 57 5480 1 . ASP 58 58 5480 1 . GLY 59 59 5480 1 . ASN 60 60 5480 1 . GLY 61 61 5480 1 . THR 62 62 5480 1 . ILE 63 63 5480 1 . ASP 64 64 5480 1 . PHE 65 65 5480 1 . PRO 66 66 5480 1 . GLU 67 67 5480 1 . PHE 68 68 5480 1 . LEU 69 69 5480 1 . THR 70 70 5480 1 . MET 71 71 5480 1 . MET 72 72 5480 1 . ALA 73 73 5480 1 . ARG 74 74 5480 1 . LYS 75 75 5480 1 . MET 76 76 5480 1 . LYS 77 77 5480 1 . ASP 78 78 5480 1 . THR 79 79 5480 1 . ASP 80 80 5480 1 . SER 81 81 5480 1 . GLU 82 82 5480 1 . GLU 83 83 5480 1 . GLU 84 84 5480 1 . ILE 85 85 5480 1 . ARG 86 86 5480 1 . GLU 87 87 5480 1 . ALA 88 88 5480 1 . PHE 89 89 5480 1 . ARG 90 90 5480 1 . VAL 91 91 5480 1 . PHE 92 92 5480 1 . ASP 93 93 5480 1 . LYS 94 94 5480 1 . ASP 95 95 5480 1 . GLY 96 96 5480 1 . ASN 97 97 5480 1 . GLY 98 98 5480 1 . TYR 99 99 5480 1 . ILE 100 100 5480 1 . SER 101 101 5480 1 . ALA 102 102 5480 1 . ALA 103 103 5480 1 . GLU 104 104 5480 1 . LEU 105 105 5480 1 . ARG 106 106 5480 1 . HIS 107 107 5480 1 . VAL 108 108 5480 1 . MET 109 109 5480 1 . THR 110 110 5480 1 . ASN 111 111 5480 1 . LEU 112 112 5480 1 . GLY 113 113 5480 1 . GLU 114 114 5480 1 . LYS 115 115 5480 1 . LEU 116 116 5480 1 . THR 117 117 5480 1 . ASP 118 118 5480 1 . GLU 119 119 5480 1 . GLU 120 120 5480 1 . VAL 121 121 5480 1 . ASP 122 122 5480 1 . GLU 123 123 5480 1 . MET 124 124 5480 1 . ILE 125 125 5480 1 . ARG 126 126 5480 1 . GLU 127 127 5480 1 . ALA 128 128 5480 1 . ASP 129 129 5480 1 . ILE 130 130 5480 1 . ASP 131 131 5480 1 . GLY 132 132 5480 1 . ASP 133 133 5480 1 . GLY 134 134 5480 1 . GLN 135 135 5480 1 . VAL 136 136 5480 1 . ASN 137 137 5480 1 . TYR 138 138 5480 1 . GLU 139 139 5480 1 . GLU 140 140 5480 1 . PHE 141 141 5480 1 . VAL 142 142 5480 1 . GLN 143 143 5480 1 . MET 144 144 5480 1 . MET 145 145 5480 1 . THR 146 146 5480 1 . ALA 147 147 5480 1 . LYS 148 148 5480 1 stop_ save_ save_bOCNC _Entity.Sf_category entity _Entity.Sf_framecode bOCNC _Entity.Entry_ID 5480 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'olfactory channel peptide' _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 ; QQRRGGFRRIARLVGVLREW AYRNFR ; _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 CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers 26 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 2900 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . SWISS-PROT Q03041 . 'Cyclic nucleotide-gated olfactory channel (Cyclic nucleotide-gated cation channel 2) (CNG channel alpha-2) (CNG-2) (CNG2)' . . . . . 100.00 663 100.00 100.00 1.14e-07 . . . . 5480 2 . . REF NP_001001139 . 'cyclic nucleotide gated channel alpha 2 [Bos taurus]' . . . . . 100.00 663 100.00 100.00 1.14e-07 . . . . 5480 2 . . PRF 1616224A . 'cAMP-gated channel' . . . . . 100.00 663 100.00 100.00 1.14e-07 . . . . 5480 2 . . EMBL CAA38754 . 'cAMP-gated channel [Bos taurus]' . . . . . 100.00 663 100.00 100.00 1.14e-07 . . . . 5480 2 . . PDB 1SY9 . 'Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel' . . . . . 100.00 26 100.00 100.00 2.83e-05 . . . . 5480 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'olfactory channel peptide' common 5480 2 bOCNC abbreviation 5480 2 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 . GLN . 5480 2 2 . GLN . 5480 2 3 . ARG . 5480 2 4 . ARG . 5480 2 5 . GLY . 5480 2 6 . GLY . 5480 2 7 . PHE . 5480 2 8 . ARG . 5480 2 9 . ARG . 5480 2 10 . ILE . 5480 2 11 . ALA . 5480 2 12 . ARG . 5480 2 13 . LEU . 5480 2 14 . VAL . 5480 2 15 . GLY . 5480 2 16 . VAL . 5480 2 17 . LEU . 5480 2 18 . ARG . 5480 2 19 . GLU . 5480 2 20 . TRP . 5480 2 21 . ALA . 5480 2 22 . TYR . 5480 2 23 . ARG . 5480 2 24 . ASN . 5480 2 25 . PHE . 5480 2 26 . ARG . 5480 2 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 . GLN 1 1 5480 2 . GLN 2 2 5480 2 . ARG 3 3 5480 2 . ARG 4 4 5480 2 . GLY 5 5 5480 2 . GLY 6 6 5480 2 . PHE 7 7 5480 2 . ARG 8 8 5480 2 . ARG 9 9 5480 2 . ILE 10 10 5480 2 . ALA 11 11 5480 2 . ARG 12 12 5480 2 . LEU 13 13 5480 2 . VAL 14 14 5480 2 . GLY 15 15 5480 2 . VAL 16 16 5480 2 . LEU 17 17 5480 2 . ARG 18 18 5480 2 . GLU 19 19 5480 2 . TRP 20 20 5480 2 . ALA 21 21 5480 2 . TYR 22 22 5480 2 . ARG 23 23 5480 2 . ASN 24 24 5480 2 . PHE 25 25 5480 2 . ARG 26 26 5480 2 stop_ save_ save_CA _Entity.Sf_category entity _Entity.Sf_framecode CA _Entity.Entry_ID 5480 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name CA _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . CA . 5480 3 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 5480 _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 $CaM . 8355 organism . 'Xenopus laevis' 'African clawed frog' . . Eukaryota Metazoa Xenopus laevis . . . . . . . . . . . . . . . . . . . . . 5480 1 2 2 $bOCNC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5480 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 5480 _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 $CaM . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli AR58 . . . . . . . . . . . . plasmid . . Cam71-pTNco12 . . . . . . 5480 1 2 2 $bOCNC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5480 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 5480 _Chem_comp.ID CA _Chem_comp.Provenance . _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CA _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 10:35:28 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Ca+2] SMILES ACDLabs 10.04 5480 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 5480 CA [Ca++] SMILES CACTVS 3.341 5480 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5480 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 5480 CA InChI=1S/Ca/q+2 InChI InChI 1.03 5480 CA BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 5480 CA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID calcium 'SYSTEMATIC NAME' ACDLabs 10.04 5480 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5480 CA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CA . CA . . CA . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5480 CA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5480 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Calmodulin '[U-95% 13C; U-95% 15N]' . . 1 $CaM . . 1.2 . . mM . . . . 5480 1 2 'olfactory channel peptide' . . . 2 $bOCNC . . 1.2 . . mM . . . . 5480 1 3 KCl . . . . . . . 140 . . mM . . . . 5480 1 4 CaCl2 . . . . . . . 7 . . mM . . . . 5480 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5480 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Calmodulin [U-15N] . . 1 $CaM . . 0.4 . . mM . . . . 5480 2 2 'olfactory channel peptide' . . . 2 $bOCNC . . 0.4 . . mM . . . . 5480 2 3 KCl . . . . . . . 140 . . mM . . . . 5480 2 4 CaCl2 . . . . . . . 7 . . mM . . . . 5480 2 stop_ save_ ####################### # Sample conditions # ####################### save_Exp-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Exp-cond_1 _Sample_condition_list.Entry_ID 5480 _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 6.7 0.1 n/a 5480 1 temperature 308 1 K 5480 1 'ionic strength' 0.15 0.02 M 5480 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5480 _Software.ID 1 _Software.Name NMRPipe _Software.Version 2 _Software.Details ; A multidimensional spectral processing system based on UNIX pipes. Delaglio,F.,Grzesiek,S.,Vuister,G.W.,Zhu,G.,Pfeifer,J. and Bax,A.(1995) J.Biomol. NMR,6,277-293. ; save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 5480 _Software.ID 2 _Software.Name NMRView _Software.Version 5 _Software.Details ; A computer program for the visualisation and analysis of NMR data. Johnson,B. and Blevins,R.A. (1994) J.Biomol. NMR,4,603-614. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5480 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5480 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker Avance . 700 . . . 5480 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 5480 _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 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 2 '15N edited TOCSY (40ms)' . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 3 '15N edited NOESY (80ms)' . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 4 HNHA . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 5 '1H-15N NOE' . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 6 HNCA . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 7 HN(CO)CA . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 8 HNCO . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 9 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 10 HBHA(CO)NH . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 11 '15N-filtered TOCSY (40 ms)' . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 12 '15N-filtered TOCSY (60 ms)' . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 13 '15N-13C filtered NOESY (80ms)' . . . . . . . . . . . . . . . . 1 $Exp-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5480 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '15N edited TOCSY (40ms)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '15N edited NOESY (80ms)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HNHA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '1H-15N NOE' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name HBHA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_11 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_11 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 11 _NMR_spec_expt.Name '15N-filtered TOCSY (40 ms)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_12 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_12 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 12 _NMR_spec_expt.Name '15N-filtered TOCSY (60 ms)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_13 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_13 _NMR_spec_expt.Entry_ID 5480 _NMR_spec_expt.ID 13 _NMR_spec_expt.Name '15N-13C filtered NOESY (80ms)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5480 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5480 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5480 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5480 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_1 _Assigned_chem_shift_list.Entry_ID 5480 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Exp-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 5480 1 . . 2 $sample_2 . 5480 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 CA C 13 51.920 0.10 . 1 . . . . . . . . 5480 1 2 . 1 1 1 1 ALA HA H 1 3.846 0.050 . 1 . . . . . . . . 5480 1 3 . 1 1 1 1 ALA CB C 13 20.143 0.10 . 1 . . . . . . . . 5480 1 4 . 1 1 1 1 ALA HB1 H 1 1.364 0.050 . 1 . . . . . . . . 5480 1 5 . 1 1 1 1 ALA HB2 H 1 1.364 0.050 . 1 . . . . . . . . 5480 1 6 . 1 1 1 1 ALA HB3 H 1 1.364 0.050 . 1 . . . . . . . . 5480 1 7 . 1 1 1 1 ALA C C 13 174.200 0.10 . 1 . . . . . . . . 5480 1 8 . 1 1 2 2 ASP N N 15 120.180 0.10 . 1 . . . . . . . . 5480 1 9 . 1 1 2 2 ASP H H 1 8.510 0.050 . 1 . . . . . . . . 5480 1 10 . 1 1 2 2 ASP CA C 13 54.570 0.10 . 1 . . . . . . . . 5480 1 11 . 1 1 2 2 ASP HA H 1 4.529 0.050 . 1 . . . . . . . . 5480 1 12 . 1 1 2 2 ASP CB C 13 41.350 0.10 . 1 . . . . . . . . 5480 1 13 . 1 1 2 2 ASP HB3 H 1 2.473 0.050 . 2 . . . . . . . . 5480 1 14 . 1 1 2 2 ASP HB2 H 1 2.600 0.050 . 2 . . . . . . . . 5480 1 15 . 1 1 2 2 ASP CG C 13 180.100 0.10 . 1 . . . . . . . . 5480 1 16 . 1 1 2 2 ASP C C 13 175.600 0.10 . 1 . . . . . . . . 5480 1 17 . 1 1 3 3 GLN N N 15 119.700 0.10 . 1 . . . . . . . . 5480 1 18 . 1 1 3 3 GLN H H 1 8.268 0.050 . 1 . . . . . . . . 5480 1 19 . 1 1 3 3 GLN CA C 13 55.430 0.10 . 1 . . . . . . . . 5480 1 20 . 1 1 3 3 GLN HA H 1 4.285 0.050 . 1 . . . . . . . . 5480 1 21 . 1 1 3 3 GLN CB C 13 29.590 0.10 . 1 . . . . . . . . 5480 1 22 . 1 1 3 3 GLN HB3 H 1 1.906 0.050 . 2 . . . . . . . . 5480 1 23 . 1 1 3 3 GLN HB2 H 1 2.021 0.050 . 2 . . . . . . . . 5480 1 24 . 1 1 3 3 GLN CG C 13 33.640 0.10 . 1 . . . . . . . . 5480 1 25 . 1 1 3 3 GLN HG3 H 1 2.279 0.050 . 1 . . . . . . . . 5480 1 26 . 1 1 3 3 GLN HG2 H 1 2.279 0.050 . 1 . . . . . . . . 5480 1 27 . 1 1 3 3 GLN CD C 13 180.800 0.10 . 1 . . . . . . . . 5480 1 28 . 1 1 3 3 GLN NE2 N 15 111.810 0.10 . 1 . . . . . . . . 5480 1 29 . 1 1 3 3 GLN HE21 H 1 7.404 0.050 . 2 . . . . . . . . 5480 1 30 . 1 1 3 3 GLN HE22 H 1 6.713 0.050 . 2 . . . . . . . . 5480 1 31 . 1 1 3 3 GLN C C 13 175.600 0.10 . 1 . . . . . . . . 5480 1 32 . 1 1 4 4 LEU N N 15 122.920 0.10 . 1 . . . . . . . . 5480 1 33 . 1 1 4 4 LEU H H 1 8.178 0.050 . 1 . . . . . . . . 5480 1 34 . 1 1 4 4 LEU CA C 13 54.254 0.10 . 1 . . . . . . . . 5480 1 35 . 1 1 4 4 LEU HA H 1 4.613 0.050 . 1 . . . . . . . . 5480 1 36 . 1 1 4 4 LEU CB C 13 43.523 0.10 . 1 . . . . . . . . 5480 1 37 . 1 1 4 4 LEU HB3 H 1 1.421 0.050 . 2 . . . . . . . . 5480 1 38 . 1 1 4 4 LEU HB2 H 1 1.649 0.050 . 2 . . . . . . . . 5480 1 39 . 1 1 4 4 LEU CG C 13 27.130 0.10 . 1 . . . . . . . . 5480 1 40 . 1 1 4 4 LEU HG H 1 1.639 0.050 . 1 . . . . . . . . 5480 1 41 . 1 1 4 4 LEU CD1 C 13 26.720 0.10 . 1 . . . . . . . . 5480 1 42 . 1 1 4 4 LEU HD11 H 1 0.877 0.050 . 2 . . . . . . . . 5480 1 43 . 1 1 4 4 LEU HD12 H 1 0.877 0.050 . 2 . . . . . . . . 5480 1 44 . 1 1 4 4 LEU HD13 H 1 0.877 0.050 . 2 . . . . . . . . 5480 1 45 . 1 1 4 4 LEU CD2 C 13 23.743 0.10 . 1 . . . . . . . . 5480 1 46 . 1 1 4 4 LEU HD21 H 1 0.843 0.050 . 2 . . . . . . . . 5480 1 47 . 1 1 4 4 LEU HD22 H 1 0.843 0.050 . 2 . . . . . . . . 5480 1 48 . 1 1 4 4 LEU HD23 H 1 0.843 0.050 . 2 . . . . . . . . 5480 1 49 . 1 1 4 4 LEU C C 13 177.700 0.10 . 1 . . . . . . . . 5480 1 50 . 1 1 5 5 THR N N 15 112.560 0.10 . 1 . . . . . . . . 5480 1 51 . 1 1 5 5 THR H H 1 8.552 0.050 . 1 . . . . . . . . 5480 1 52 . 1 1 5 5 THR CA C 13 60.252 0.10 . 1 . . . . . . . . 5480 1 53 . 1 1 5 5 THR HA H 1 4.405 0.050 . 1 . . . . . . . . 5480 1 54 . 1 1 5 5 THR CB C 13 71.071 0.10 . 1 . . . . . . . . 5480 1 55 . 1 1 5 5 THR HB H 1 4.679 0.050 . 1 . . . . . . . . 5480 1 56 . 1 1 5 5 THR CG2 C 13 21.710 0.10 . 1 . . . . . . . . 5480 1 57 . 1 1 5 5 THR HG21 H 1 1.269 0.050 . 1 . . . . . . . . 5480 1 58 . 1 1 5 5 THR HG22 H 1 1.269 0.050 . 1 . . . . . . . . 5480 1 59 . 1 1 5 5 THR HG23 H 1 1.269 0.050 . 1 . . . . . . . . 5480 1 60 . 1 1 5 5 THR C C 13 175.500 0.10 . 1 . . . . . . . . 5480 1 61 . 1 1 6 6 GLU N N 15 120.070 0.10 . 1 . . . . . . . . 5480 1 62 . 1 1 6 6 GLU H H 1 8.909 0.050 . 1 . . . . . . . . 5480 1 63 . 1 1 6 6 GLU CA C 13 59.900 0.10 . 1 . . . . . . . . 5480 1 64 . 1 1 6 6 GLU HA H 1 3.900 0.050 . 1 . . . . . . . . 5480 1 65 . 1 1 6 6 GLU CB C 13 29.160 0.10 . 1 . . . . . . . . 5480 1 66 . 1 1 6 6 GLU HB3 H 1 1.987 0.050 . 1 . . . . . . . . 5480 1 67 . 1 1 6 6 GLU HB2 H 1 1.987 0.050 . 1 . . . . . . . . 5480 1 68 . 1 1 6 6 GLU CG C 13 36.150 0.10 . 1 . . . . . . . . 5480 1 69 . 1 1 6 6 GLU HG3 H 1 2.269 0.050 . 1 . . . . . . . . 5480 1 70 . 1 1 6 6 GLU HG2 H 1 2.269 0.050 . 1 . . . . . . . . 5480 1 71 . 1 1 6 6 GLU C C 13 178.800 0.10 . 1 . . . . . . . . 5480 1 72 . 1 1 7 7 GLU N N 15 118.950 0.10 . 1 . . . . . . . . 5480 1 73 . 1 1 7 7 GLU H H 1 8.500 0.050 . 1 . . . . . . . . 5480 1 74 . 1 1 7 7 GLU CA C 13 59.390 0.10 . 1 . . . . . . . . 5480 1 75 . 1 1 7 7 GLU HA H 1 3.979 0.050 . 1 . . . . . . . . 5480 1 76 . 1 1 7 7 GLU CB C 13 29.160 0.10 . 1 . . . . . . . . 5480 1 77 . 1 1 7 7 GLU HB3 H 1 2.103 0.050 . 1 . . . . . . . . 5480 1 78 . 1 1 7 7 GLU HB2 H 1 2.103 0.050 . 1 . . . . . . . . 5480 1 79 . 1 1 7 7 GLU CG C 13 36.543 0.10 . 1 . . . . . . . . 5480 1 80 . 1 1 7 7 GLU HG3 H 1 2.259 0.050 . 1 . . . . . . . . 5480 1 81 . 1 1 7 7 GLU HG2 H 1 2.259 0.050 . 1 . . . . . . . . 5480 1 82 . 1 1 7 7 GLU C C 13 179.270 0.10 . 1 . . . . . . . . 5480 1 83 . 1 1 8 8 GLN N N 15 119.690 0.10 . 1 . . . . . . . . 5480 1 84 . 1 1 8 8 GLN H H 1 7.598 0.050 . 1 . . . . . . . . 5480 1 85 . 1 1 8 8 GLN CA C 13 58.793 0.10 . 1 . . . . . . . . 5480 1 86 . 1 1 8 8 GLN HA H 1 3.703 0.050 . 1 . . . . . . . . 5480 1 87 . 1 1 8 8 GLN CB C 13 29.120 0.10 . 1 . . . . . . . . 5480 1 88 . 1 1 8 8 GLN HB3 H 1 2.247 0.050 . 2 . . . . . . . . 5480 1 89 . 1 1 8 8 GLN HB2 H 1 1.509 0.050 . 2 . . . . . . . . 5480 1 90 . 1 1 8 8 GLN CG C 13 34.820 0.10 . 1 . . . . . . . . 5480 1 91 . 1 1 8 8 GLN HG3 H 1 2.180 0.050 . 2 . . . . . . . . 5480 1 92 . 1 1 8 8 GLN HG2 H 1 2.242 0.050 . 2 . . . . . . . . 5480 1 93 . 1 1 8 8 GLN CD C 13 179.900 0.10 . 1 . . . . . . . . 5480 1 94 . 1 1 8 8 GLN NE2 N 15 110.720 0.10 . 1 . . . . . . . . 5480 1 95 . 1 1 8 8 GLN HE21 H 1 7.304 0.050 . 2 . . . . . . . . 5480 1 96 . 1 1 8 8 GLN HE22 H 1 6.660 0.050 . 2 . . . . . . . . 5480 1 97 . 1 1 8 8 GLN C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 98 . 1 1 9 9 ILE N N 15 118.746 0.10 . 1 . . . . . . . . 5480 1 99 . 1 1 9 9 ILE H H 1 8.211 0.050 . 1 . . . . . . . . 5480 1 100 . 1 1 9 9 ILE CA C 13 66.110 0.10 . 1 . . . . . . . . 5480 1 101 . 1 1 9 9 ILE HA H 1 3.541 0.050 . 1 . . . . . . . . 5480 1 102 . 1 1 9 9 ILE CB C 13 37.790 0.10 . 1 . . . . . . . . 5480 1 103 . 1 1 9 9 ILE HB H 1 1.847 0.050 . 1 . . . . . . . . 5480 1 104 . 1 1 9 9 ILE CG1 C 13 30.180 0.10 . 2 . . . . . . . . 5480 1 105 . 1 1 9 9 ILE HG13 H 1 1.711 0.050 . 1 . . . . . . . . 5480 1 106 . 1 1 9 9 ILE HG12 H 1 1.018 0.050 . 1 . . . . . . . . 5480 1 107 . 1 1 9 9 ILE CD1 C 13 12.869 0.10 . 1 . . . . . . . . 5480 1 108 . 1 1 9 9 ILE HD11 H 1 0.782 0.050 . 1 . . . . . . . . 5480 1 109 . 1 1 9 9 ILE HD12 H 1 0.782 0.050 . 1 . . . . . . . . 5480 1 110 . 1 1 9 9 ILE HD13 H 1 0.782 0.050 . 1 . . . . . . . . 5480 1 111 . 1 1 9 9 ILE CG2 C 13 17.386 0.10 . 1 . . . . . . . . 5480 1 112 . 1 1 9 9 ILE HG21 H 1 1.036 0.050 . 1 . . . . . . . . 5480 1 113 . 1 1 9 9 ILE HG22 H 1 1.036 0.050 . 1 . . . . . . . . 5480 1 114 . 1 1 9 9 ILE HG23 H 1 1.036 0.050 . 1 . . . . . . . . 5480 1 115 . 1 1 9 9 ILE C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 116 . 1 1 10 10 ALA N N 15 120.730 0.10 . 1 . . . . . . . . 5480 1 117 . 1 1 10 10 ALA H H 1 7.947 0.050 . 1 . . . . . . . . 5480 1 118 . 1 1 10 10 ALA CA C 13 55.300 0.10 . 1 . . . . . . . . 5480 1 119 . 1 1 10 10 ALA HA H 1 4.008 0.050 . 1 . . . . . . . . 5480 1 120 . 1 1 10 10 ALA CB C 13 17.770 0.10 . 1 . . . . . . . . 5480 1 121 . 1 1 10 10 ALA HB1 H 1 1.454 0.050 . 1 . . . . . . . . 5480 1 122 . 1 1 10 10 ALA HB2 H 1 1.454 0.050 . 1 . . . . . . . . 5480 1 123 . 1 1 10 10 ALA HB3 H 1 1.454 0.050 . 1 . . . . . . . . 5480 1 124 . 1 1 10 10 ALA C C 13 180.900 0.10 . 1 . . . . . . . . 5480 1 125 . 1 1 11 11 GLU N N 15 119.100 0.10 . 1 . . . . . . . . 5480 1 126 . 1 1 11 11 GLU H H 1 7.721 0.050 . 1 . . . . . . . . 5480 1 127 . 1 1 11 11 GLU CA C 13 59.300 0.10 . 1 . . . . . . . . 5480 1 128 . 1 1 11 11 GLU HA H 1 4.036 0.050 . 1 . . . . . . . . 5480 1 129 . 1 1 11 11 GLU CB C 13 29.309 0.10 . 1 . . . . . . . . 5480 1 130 . 1 1 11 11 GLU HB3 H 1 1.826 0.050 . 2 . . . . . . . . 5480 1 131 . 1 1 11 11 GLU HB2 H 1 2.006 0.050 . 2 . . . . . . . . 5480 1 132 . 1 1 11 11 GLU CG C 13 36.190 0.10 . 1 . . . . . . . . 5480 1 133 . 1 1 11 11 GLU HG3 H 1 2.097 0.050 . 2 . . . . . . . . 5480 1 134 . 1 1 11 11 GLU HG2 H 1 2.285 0.050 . 2 . . . . . . . . 5480 1 135 . 1 1 11 11 GLU CD C 13 183.300 0.10 . 1 . . . . . . . . 5480 1 136 . 1 1 11 11 GLU C C 13 180.100 0.10 . 1 . . . . . . . . 5480 1 137 . 1 1 12 12 PHE N N 15 119.510 0.10 . 1 . . . . . . . . 5480 1 138 . 1 1 12 12 PHE H H 1 8.469 0.050 . 1 . . . . . . . . 5480 1 139 . 1 1 12 12 PHE CA C 13 58.570 0.10 . 1 . . . . . . . . 5480 1 140 . 1 1 12 12 PHE HA H 1 4.955 0.050 . 1 . . . . . . . . 5480 1 141 . 1 1 12 12 PHE CB C 13 37.026 0.10 . 1 . . . . . . . . 5480 1 142 . 1 1 12 12 PHE HB3 H 1 3.483 0.050 . 2 . . . . . . . . 5480 1 143 . 1 1 12 12 PHE HB2 H 1 3.376 0.050 . 2 . . . . . . . . 5480 1 144 . 1 1 12 12 PHE CD1 C 13 130.070 0.10 . 1 . . . . . . . . 5480 1 145 . 1 1 12 12 PHE HD1 H 1 7.074 0.050 . 1 . . . . . . . . 5480 1 146 . 1 1 12 12 PHE CE1 C 13 131.260 0.10 . 1 . . . . . . . . 5480 1 147 . 1 1 12 12 PHE HE1 H 1 7.197 0.050 . 1 . . . . . . . . 5480 1 148 . 1 1 12 12 PHE CZ C 13 129.470 0.10 . 1 . . . . . . . . 5480 1 149 . 1 1 12 12 PHE HZ H 1 7.160 0.050 . 1 . . . . . . . . 5480 1 150 . 1 1 12 12 PHE CE2 C 13 131.260 0.10 . 1 . . . . . . . . 5480 1 151 . 1 1 12 12 PHE HE2 H 1 7.197 0.050 . 1 . . . . . . . . 5480 1 152 . 1 1 12 12 PHE CD2 C 13 130.070 0.10 . 1 . . . . . . . . 5480 1 153 . 1 1 12 12 PHE HD2 H 1 7.074 0.050 . 1 . . . . . . . . 5480 1 154 . 1 1 12 12 PHE C C 13 178.900 0.10 . 1 . . . . . . . . 5480 1 155 . 1 1 13 13 LYS N N 15 123.357 0.10 . 1 . . . . . . . . 5480 1 156 . 1 1 13 13 LYS H H 1 9.173 0.050 . 1 . . . . . . . . 5480 1 157 . 1 1 13 13 LYS CA C 13 60.000 0.10 . 1 . . . . . . . . 5480 1 158 . 1 1 13 13 LYS HA H 1 3.981 0.050 . 1 . . . . . . . . 5480 1 159 . 1 1 13 13 LYS CB C 13 31.800 0.10 . 1 . . . . . . . . 5480 1 160 . 1 1 13 13 LYS HB3 H 1 1.861 0.050 . 1 . . . . . . . . 5480 1 161 . 1 1 13 13 LYS HB2 H 1 1.861 0.050 . 1 . . . . . . . . 5480 1 162 . 1 1 13 13 LYS CG C 13 25.520 0.10 . 1 . . . . . . . . 5480 1 163 . 1 1 13 13 LYS HG3 H 1 1.139 0.050 . 2 . . . . . . . . 5480 1 164 . 1 1 13 13 LYS HG2 H 1 0.977 0.050 . 2 . . . . . . . . 5480 1 165 . 1 1 13 13 LYS CD C 13 28.641 0.10 . 1 . . . . . . . . 5480 1 166 . 1 1 13 13 LYS HD3 H 1 1.159 0.050 . 2 . . . . . . . . 5480 1 167 . 1 1 13 13 LYS HD2 H 1 1.298 0.050 . 2 . . . . . . . . 5480 1 168 . 1 1 13 13 LYS CE C 13 41.557 0.10 . 1 . . . . . . . . 5480 1 169 . 1 1 13 13 LYS HE3 H 1 2.515 0.050 . 1 . . . . . . . . 5480 1 170 . 1 1 13 13 LYS HE2 H 1 2.515 0.050 . 1 . . . . . . . . 5480 1 171 . 1 1 13 13 LYS C C 13 179.300 0.10 . 1 . . . . . . . . 5480 1 172 . 1 1 14 14 GLU N N 15 119.990 0.10 . 1 . . . . . . . . 5480 1 173 . 1 1 14 14 GLU H H 1 7.850 0.050 . 1 . . . . . . . . 5480 1 174 . 1 1 14 14 GLU CA C 13 59.300 0.10 . 1 . . . . . . . . 5480 1 175 . 1 1 14 14 GLU HA H 1 4.100 0.050 . 1 . . . . . . . . 5480 1 176 . 1 1 14 14 GLU CB C 13 29.188 0.10 . 1 . . . . . . . . 5480 1 177 . 1 1 14 14 GLU HB3 H 1 2.130 0.050 . 1 . . . . . . . . 5480 1 178 . 1 1 14 14 GLU HB2 H 1 2.130 0.050 . 1 . . . . . . . . 5480 1 179 . 1 1 14 14 GLU CG C 13 36.160 0.10 . 1 . . . . . . . . 5480 1 180 . 1 1 14 14 GLU HG3 H 1 2.270 0.050 . 2 . . . . . . . . 5480 1 181 . 1 1 14 14 GLU HG2 H 1 2.334 0.050 . 2 . . . . . . . . 5480 1 182 . 1 1 14 14 GLU C C 13 179.800 0.10 . 1 . . . . . . . . 5480 1 183 . 1 1 15 15 ALA N N 15 121.080 0.10 . 1 . . . . . . . . 5480 1 184 . 1 1 15 15 ALA H H 1 7.950 0.050 . 1 . . . . . . . . 5480 1 185 . 1 1 15 15 ALA CA C 13 55.200 0.10 . 1 . . . . . . . . 5480 1 186 . 1 1 15 15 ALA HA H 1 4.193 0.050 . 1 . . . . . . . . 5480 1 187 . 1 1 15 15 ALA CB C 13 18.100 0.10 . 1 . . . . . . . . 5480 1 188 . 1 1 15 15 ALA HB1 H 1 1.975 0.050 . 1 . . . . . . . . 5480 1 189 . 1 1 15 15 ALA HB2 H 1 1.975 0.050 . 1 . . . . . . . . 5480 1 190 . 1 1 15 15 ALA HB3 H 1 1.975 0.050 . 1 . . . . . . . . 5480 1 191 . 1 1 15 15 ALA C C 13 178.500 0.10 . 1 . . . . . . . . 5480 1 192 . 1 1 16 16 PHE N N 15 118.300 0.10 . 1 . . . . . . . . 5480 1 193 . 1 1 16 16 PHE H H 1 8.687 0.050 . 1 . . . . . . . . 5480 1 194 . 1 1 16 16 PHE CA C 13 62.100 0.10 . 1 . . . . . . . . 5480 1 195 . 1 1 16 16 PHE HA H 1 3.257 0.050 . 1 . . . . . . . . 5480 1 196 . 1 1 16 16 PHE CB C 13 39.150 0.10 . 1 . . . . . . . . 5480 1 197 . 1 1 16 16 PHE HB3 H 1 2.809 0.050 . 2 . . . . . . . . 5480 1 198 . 1 1 16 16 PHE HB2 H 1 3.204 0.050 . 2 . . . . . . . . 5480 1 199 . 1 1 16 16 PHE CD1 C 13 131.760 0.10 . 1 . . . . . . . . 5480 1 200 . 1 1 16 16 PHE HD1 H 1 6.548 0.050 . 1 . . . . . . . . 5480 1 201 . 1 1 16 16 PHE CE1 C 13 131.280 0.10 . 1 . . . . . . . . 5480 1 202 . 1 1 16 16 PHE HE1 H 1 7.107 0.050 . 1 . . . . . . . . 5480 1 203 . 1 1 16 16 PHE HZ H 1 7.120 0.050 . 1 . . . . . . . . 5480 1 204 . 1 1 16 16 PHE CE2 C 13 131.280 0.10 . 1 . . . . . . . . 5480 1 205 . 1 1 16 16 PHE HE2 H 1 7.107 0.050 . 1 . . . . . . . . 5480 1 206 . 1 1 16 16 PHE CD2 C 13 131.760 0.10 . 1 . . . . . . . . 5480 1 207 . 1 1 16 16 PHE HD2 H 1 6.548 0.050 . 1 . . . . . . . . 5480 1 208 . 1 1 16 16 PHE C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 209 . 1 1 17 17 SER N N 15 112.930 0.10 . 1 . . . . . . . . 5480 1 210 . 1 1 17 17 SER H H 1 8.048 0.050 . 1 . . . . . . . . 5480 1 211 . 1 1 17 17 SER CA C 13 61.400 0.10 . 1 . . . . . . . . 5480 1 212 . 1 1 17 17 SER HA H 1 4.068 0.050 . 1 . . . . . . . . 5480 1 213 . 1 1 17 17 SER CB C 13 63.210 0.10 . 1 . . . . . . . . 5480 1 214 . 1 1 17 17 SER HB3 H 1 3.982 0.050 . 1 . . . . . . . . 5480 1 215 . 1 1 17 17 SER HB2 H 1 3.982 0.050 . 1 . . . . . . . . 5480 1 216 . 1 1 17 17 SER C C 13 174.650 0.10 . 1 . . . . . . . . 5480 1 217 . 1 1 18 18 LEU N N 15 119.710 0.10 . 1 . . . . . . . . 5480 1 218 . 1 1 18 18 LEU H H 1 7.345 0.050 . 1 . . . . . . . . 5480 1 219 . 1 1 18 18 LEU CA C 13 57.180 0.10 . 1 . . . . . . . . 5480 1 220 . 1 1 18 18 LEU HA H 1 3.946 0.050 . 1 . . . . . . . . 5480 1 221 . 1 1 18 18 LEU CB C 13 41.640 0.10 . 1 . . . . . . . . 5480 1 222 . 1 1 18 18 LEU HB3 H 1 1.389 0.050 . 2 . . . . . . . . 5480 1 223 . 1 1 18 18 LEU HB2 H 1 1.782 0.050 . 2 . . . . . . . . 5480 1 224 . 1 1 18 18 LEU CG C 13 26.690 0.10 . 1 . . . . . . . . 5480 1 225 . 1 1 18 18 LEU HG H 1 1.634 0.050 . 1 . . . . . . . . 5480 1 226 . 1 1 18 18 LEU CD1 C 13 23.860 0.10 . 1 . . . . . . . . 5480 1 227 . 1 1 18 18 LEU HD11 H 1 0.623 0.050 . 2 . . . . . . . . 5480 1 228 . 1 1 18 18 LEU HD12 H 1 0.623 0.050 . 2 . . . . . . . . 5480 1 229 . 1 1 18 18 LEU HD13 H 1 0.623 0.050 . 2 . . . . . . . . 5480 1 230 . 1 1 18 18 LEU CD2 C 13 25.334 0.10 . 1 . . . . . . . . 5480 1 231 . 1 1 18 18 LEU HD21 H 1 0.783 0.050 . 2 . . . . . . . . 5480 1 232 . 1 1 18 18 LEU HD22 H 1 0.783 0.050 . 2 . . . . . . . . 5480 1 233 . 1 1 18 18 LEU HD23 H 1 0.783 0.050 . 2 . . . . . . . . 5480 1 234 . 1 1 18 18 LEU C C 13 177.380 0.10 . 1 . . . . . . . . 5480 1 235 . 1 1 19 19 PHE N N 15 112.670 0.10 . 1 . . . . . . . . 5480 1 236 . 1 1 19 19 PHE H H 1 7.104 0.050 . 1 . . . . . . . . 5480 1 237 . 1 1 19 19 PHE CA C 13 58.800 0.10 . 1 . . . . . . . . 5480 1 238 . 1 1 19 19 PHE HA H 1 4.150 0.050 . 1 . . . . . . . . 5480 1 239 . 1 1 19 19 PHE CB C 13 41.700 0.10 . 1 . . . . . . . . 5480 1 240 . 1 1 19 19 PHE HB3 H 1 2.593 0.050 . 2 . . . . . . . . 5480 1 241 . 1 1 19 19 PHE HB2 H 1 2.723 0.050 . 2 . . . . . . . . 5480 1 242 . 1 1 19 19 PHE CD1 C 13 130.510 0.10 . 1 . . . . . . . . 5480 1 243 . 1 1 19 19 PHE HD1 H 1 7.354 0.050 . 1 . . . . . . . . 5480 1 244 . 1 1 19 19 PHE CE1 C 13 132.480 0.10 . 1 . . . . . . . . 5480 1 245 . 1 1 19 19 PHE HE1 H 1 7.374 0.050 . 1 . . . . . . . . 5480 1 246 . 1 1 19 19 PHE CZ C 13 128.390 0.10 . 1 . . . . . . . . 5480 1 247 . 1 1 19 19 PHE HZ H 1 7.311 0.050 . 1 . . . . . . . . 5480 1 248 . 1 1 19 19 PHE CE2 C 13 132.480 0.10 . 1 . . . . . . . . 5480 1 249 . 1 1 19 19 PHE HE2 H 1 7.374 0.050 . 1 . . . . . . . . 5480 1 250 . 1 1 19 19 PHE CD2 C 13 130.510 0.10 . 1 . . . . . . . . 5480 1 251 . 1 1 19 19 PHE HD2 H 1 7.354 0.050 . 1 . . . . . . . . 5480 1 252 . 1 1 19 19 PHE C C 13 177.100 0.10 . 1 . . . . . . . . 5480 1 253 . 1 1 20 20 ASP N N 15 116.370 0.10 . 1 . . . . . . . . 5480 1 254 . 1 1 20 20 ASP H H 1 7.657 0.050 . 1 . . . . . . . . 5480 1 255 . 1 1 20 20 ASP CA C 13 52.597 0.10 . 1 . . . . . . . . 5480 1 256 . 1 1 20 20 ASP HA H 1 4.541 0.050 . 1 . . . . . . . . 5480 1 257 . 1 1 20 20 ASP CB C 13 39.237 0.10 . 1 . . . . . . . . 5480 1 258 . 1 1 20 20 ASP HB3 H 1 1.462 0.050 . 2 . . . . . . . . 5480 1 259 . 1 1 20 20 ASP HB2 H 1 2.287 0.050 . 2 . . . . . . . . 5480 1 260 . 1 1 20 20 ASP CG C 13 179.000 0.10 . 1 . . . . . . . . 5480 1 261 . 1 1 20 20 ASP C C 13 177.100 0.10 . 1 . . . . . . . . 5480 1 262 . 1 1 21 21 LYS N N 15 124.048 0.10 . 1 . . . . . . . . 5480 1 263 . 1 1 21 21 LYS H H 1 7.759 0.050 . 1 . . . . . . . . 5480 1 264 . 1 1 21 21 LYS CA C 13 57.750 0.10 . 1 . . . . . . . . 5480 1 265 . 1 1 21 21 LYS HA H 1 3.952 0.050 . 1 . . . . . . . . 5480 1 266 . 1 1 21 21 LYS CB C 13 32.510 0.10 . 1 . . . . . . . . 5480 1 267 . 1 1 21 21 LYS HB3 H 1 1.852 0.050 . 1 . . . . . . . . 5480 1 268 . 1 1 21 21 LYS HB2 H 1 1.852 0.050 . 1 . . . . . . . . 5480 1 269 . 1 1 21 21 LYS CG C 13 24.300 0.10 . 1 . . . . . . . . 5480 1 270 . 1 1 21 21 LYS HG3 H 1 1.435 0.050 . 2 . . . . . . . . 5480 1 271 . 1 1 21 21 LYS HG2 H 1 1.534 0.050 . 2 . . . . . . . . 5480 1 272 . 1 1 21 21 LYS CD C 13 28.030 0.10 . 1 . . . . . . . . 5480 1 273 . 1 1 21 21 LYS HD3 H 1 1.633 0.050 . 1 . . . . . . . . 5480 1 274 . 1 1 21 21 LYS HD2 H 1 1.633 0.050 . 1 . . . . . . . . 5480 1 275 . 1 1 21 21 LYS CE C 13 42.030 0.10 . 1 . . . . . . . . 5480 1 276 . 1 1 21 21 LYS HE3 H 1 2.974 0.050 . 1 . . . . . . . . 5480 1 277 . 1 1 21 21 LYS HE2 H 1 2.974 0.050 . 1 . . . . . . . . 5480 1 278 . 1 1 21 21 LYS C C 13 178.300 0.10 . 1 . . . . . . . . 5480 1 279 . 1 1 22 22 ASP N N 15 113.695 0.10 . 1 . . . . . . . . 5480 1 280 . 1 1 22 22 ASP H H 1 7.975 0.050 . 1 . . . . . . . . 5480 1 281 . 1 1 22 22 ASP CA C 13 52.760 0.10 . 1 . . . . . . . . 5480 1 282 . 1 1 22 22 ASP HA H 1 4.553 0.050 . 1 . . . . . . . . 5480 1 283 . 1 1 22 22 ASP CB C 13 39.800 0.10 . 1 . . . . . . . . 5480 1 284 . 1 1 22 22 ASP HB3 H 1 2.587 0.050 . 2 . . . . . . . . 5480 1 285 . 1 1 22 22 ASP HB2 H 1 3.023 0.050 . 2 . . . . . . . . 5480 1 286 . 1 1 22 22 ASP CG C 13 180.900 0.10 . 1 . . . . . . . . 5480 1 287 . 1 1 22 22 ASP C C 13 177.700 0.10 . 1 . . . . . . . . 5480 1 288 . 1 1 23 23 GLY N N 15 108.780 0.10 . 1 . . . . . . . . 5480 1 289 . 1 1 23 23 GLY H H 1 7.590 0.050 . 1 . . . . . . . . 5480 1 290 . 1 1 23 23 GLY CA C 13 47.030 0.10 . 1 . . . . . . . . 5480 1 291 . 1 1 23 23 GLY HA3 H 1 3.800 0.050 . 1 . . . . . . . . 5480 1 292 . 1 1 23 23 GLY HA2 H 1 3.800 0.050 . 1 . . . . . . . . 5480 1 293 . 1 1 23 23 GLY C C 13 175.200 0.10 . 1 . . . . . . . . 5480 1 294 . 1 1 24 24 ASP N N 15 120.410 0.10 . 1 . . . . . . . . 5480 1 295 . 1 1 24 24 ASP H H 1 8.384 0.050 . 1 . . . . . . . . 5480 1 296 . 1 1 24 24 ASP CA C 13 53.500 0.10 . 1 . . . . . . . . 5480 1 297 . 1 1 24 24 ASP HA H 1 4.460 0.050 . 1 . . . . . . . . 5480 1 298 . 1 1 24 24 ASP CB C 13 40.320 0.10 . 1 . . . . . . . . 5480 1 299 . 1 1 24 24 ASP HB3 H 1 2.990 0.050 . 2 . . . . . . . . 5480 1 300 . 1 1 24 24 ASP HB2 H 1 2.390 0.050 . 2 . . . . . . . . 5480 1 301 . 1 1 24 24 ASP CG C 13 182.100 0.10 . 1 . . . . . . . . 5480 1 302 . 1 1 24 24 ASP C C 13 177.500 0.10 . 1 . . . . . . . . 5480 1 303 . 1 1 25 25 GLY N N 15 112.420 0.10 . 1 . . . . . . . . 5480 1 304 . 1 1 25 25 GLY H H 1 10.494 0.050 . 1 . . . . . . . . 5480 1 305 . 1 1 25 25 GLY CA C 13 45.250 0.10 . 1 . . . . . . . . 5480 1 306 . 1 1 25 25 GLY HA3 H 1 4.290 0.050 . 2 . . . . . . . . 5480 1 307 . 1 1 25 25 GLY HA2 H 1 3.650 0.050 . 2 . . . . . . . . 5480 1 308 . 1 1 25 25 GLY C C 13 173.900 0.10 . 1 . . . . . . . . 5480 1 309 . 1 1 26 26 THR N N 15 111.830 0.10 . 1 . . . . . . . . 5480 1 310 . 1 1 26 26 THR H H 1 8.144 0.050 . 1 . . . . . . . . 5480 1 311 . 1 1 26 26 THR CA C 13 59.630 0.10 . 1 . . . . . . . . 5480 1 312 . 1 1 26 26 THR HA H 1 5.370 0.050 . 1 . . . . . . . . 5480 1 313 . 1 1 26 26 THR CB C 13 72.620 0.10 . 1 . . . . . . . . 5480 1 314 . 1 1 26 26 THR HB H 1 3.780 0.050 . 1 . . . . . . . . 5480 1 315 . 1 1 26 26 THR CG2 C 13 21.800 0.10 . 1 . . . . . . . . 5480 1 316 . 1 1 26 26 THR HG21 H 1 0.990 0.050 . 1 . . . . . . . . 5480 1 317 . 1 1 26 26 THR HG22 H 1 0.990 0.050 . 1 . . . . . . . . 5480 1 318 . 1 1 26 26 THR HG23 H 1 0.990 0.050 . 1 . . . . . . . . 5480 1 319 . 1 1 26 26 THR C C 13 173.200 0.10 . 1 . . . . . . . . 5480 1 320 . 1 1 27 27 ILE N N 15 126.016 0.10 . 1 . . . . . . . . 5480 1 321 . 1 1 27 27 ILE H H 1 9.801 0.050 . 1 . . . . . . . . 5480 1 322 . 1 1 27 27 ILE CA C 13 60.900 0.10 . 1 . . . . . . . . 5480 1 323 . 1 1 27 27 ILE HA H 1 4.820 0.050 . 1 . . . . . . . . 5480 1 324 . 1 1 27 27 ILE CB C 13 39.904 0.10 . 1 . . . . . . . . 5480 1 325 . 1 1 27 27 ILE HB H 1 1.716 0.050 . 1 . . . . . . . . 5480 1 326 . 1 1 27 27 ILE CG1 C 13 26.670 0.10 . 2 . . . . . . . . 5480 1 327 . 1 1 27 27 ILE HG13 H 1 1.208 0.050 . 1 . . . . . . . . 5480 1 328 . 1 1 27 27 ILE HG12 H 1 0.161 0.050 . 1 . . . . . . . . 5480 1 329 . 1 1 27 27 ILE CD1 C 13 15.250 0.10 . 1 . . . . . . . . 5480 1 330 . 1 1 27 27 ILE HD11 H 1 0.170 0.050 . 1 . . . . . . . . 5480 1 331 . 1 1 27 27 ILE HD12 H 1 0.170 0.050 . 1 . . . . . . . . 5480 1 332 . 1 1 27 27 ILE HD13 H 1 0.170 0.050 . 1 . . . . . . . . 5480 1 333 . 1 1 27 27 ILE CG2 C 13 17.500 0.10 . 1 . . . . . . . . 5480 1 334 . 1 1 27 27 ILE HG21 H 1 0.900 0.050 . 1 . . . . . . . . 5480 1 335 . 1 1 27 27 ILE HG22 H 1 0.900 0.050 . 1 . . . . . . . . 5480 1 336 . 1 1 27 27 ILE HG23 H 1 0.900 0.050 . 1 . . . . . . . . 5480 1 337 . 1 1 27 27 ILE C C 13 176.200 0.10 . 1 . . . . . . . . 5480 1 338 . 1 1 28 28 THR N N 15 115.980 0.10 . 1 . . . . . . . . 5480 1 339 . 1 1 28 28 THR H H 1 8.304 0.050 . 1 . . . . . . . . 5480 1 340 . 1 1 28 28 THR CA C 13 59.300 0.10 . 1 . . . . . . . . 5480 1 341 . 1 1 28 28 THR HA H 1 4.810 0.050 . 1 . . . . . . . . 5480 1 342 . 1 1 28 28 THR CB C 13 72.454 0.10 . 1 . . . . . . . . 5480 1 343 . 1 1 28 28 THR HB H 1 4.739 0.050 . 1 . . . . . . . . 5480 1 344 . 1 1 28 28 THR CG2 C 13 21.800 0.10 . 1 . . . . . . . . 5480 1 345 . 1 1 28 28 THR HG21 H 1 1.217 0.050 . 1 . . . . . . . . 5480 1 346 . 1 1 28 28 THR HG22 H 1 1.217 0.050 . 1 . . . . . . . . 5480 1 347 . 1 1 28 28 THR HG23 H 1 1.217 0.050 . 1 . . . . . . . . 5480 1 348 . 1 1 28 28 THR C C 13 176.800 0.10 . 1 . . . . . . . . 5480 1 349 . 1 1 29 29 THR N N 15 112.120 0.10 . 1 . . . . . . . . 5480 1 350 . 1 1 29 29 THR H H 1 9.043 0.050 . 1 . . . . . . . . 5480 1 351 . 1 1 29 29 THR CA C 13 66.200 0.10 . 1 . . . . . . . . 5480 1 352 . 1 1 29 29 THR HA H 1 3.676 0.050 . 1 . . . . . . . . 5480 1 353 . 1 1 29 29 THR CB C 13 67.770 0.10 . 1 . . . . . . . . 5480 1 354 . 1 1 29 29 THR HB H 1 4.123 0.050 . 1 . . . . . . . . 5480 1 355 . 1 1 29 29 THR CG2 C 13 23.270 0.10 . 1 . . . . . . . . 5480 1 356 . 1 1 29 29 THR HG21 H 1 1.205 0.050 . 1 . . . . . . . . 5480 1 357 . 1 1 29 29 THR HG22 H 1 1.205 0.050 . 1 . . . . . . . . 5480 1 358 . 1 1 29 29 THR HG23 H 1 1.205 0.050 . 1 . . . . . . . . 5480 1 359 . 1 1 29 29 THR C C 13 177.300 0.10 . 1 . . . . . . . . 5480 1 360 . 1 1 30 30 LYS N N 15 120.400 0.10 . 1 . . . . . . . . 5480 1 361 . 1 1 30 30 LYS H H 1 7.530 0.050 . 1 . . . . . . . . 5480 1 362 . 1 1 30 30 LYS CA C 13 59.000 0.10 . 1 . . . . . . . . 5480 1 363 . 1 1 30 30 LYS HA H 1 4.040 0.050 . 1 . . . . . . . . 5480 1 364 . 1 1 30 30 LYS CB C 13 32.430 0.10 . 1 . . . . . . . . 5480 1 365 . 1 1 30 30 LYS HB3 H 1 1.744 0.050 . 2 . . . . . . . . 5480 1 366 . 1 1 30 30 LYS HB2 H 1 1.806 0.050 . 2 . . . . . . . . 5480 1 367 . 1 1 30 30 LYS CG C 13 24.780 0.10 . 1 . . . . . . . . 5480 1 368 . 1 1 30 30 LYS HG3 H 1 1.320 0.050 . 2 . . . . . . . . 5480 1 369 . 1 1 30 30 LYS HG2 H 1 1.426 0.050 . 2 . . . . . . . . 5480 1 370 . 1 1 30 30 LYS CD C 13 28.910 0.10 . 1 . . . . . . . . 5480 1 371 . 1 1 30 30 LYS HD3 H 1 1.632 0.050 . 1 . . . . . . . . 5480 1 372 . 1 1 30 30 LYS HD2 H 1 1.632 0.050 . 1 . . . . . . . . 5480 1 373 . 1 1 30 30 LYS CE C 13 41.850 0.10 . 1 . . . . . . . . 5480 1 374 . 1 1 30 30 LYS HE3 H 1 2.934 0.050 . 1 . . . . . . . . 5480 1 375 . 1 1 30 30 LYS HE2 H 1 2.934 0.050 . 1 . . . . . . . . 5480 1 376 . 1 1 30 30 LYS C C 13 180.000 0.10 . 1 . . . . . . . . 5480 1 377 . 1 1 31 31 GLU N N 15 121.400 0.10 . 1 . . . . . . . . 5480 1 378 . 1 1 31 31 GLU H H 1 7.627 0.050 . 1 . . . . . . . . 5480 1 379 . 1 1 31 31 GLU CA C 13 59.300 0.10 . 1 . . . . . . . . 5480 1 380 . 1 1 31 31 GLU HA H 1 3.990 0.050 . 1 . . . . . . . . 5480 1 381 . 1 1 31 31 GLU CB C 13 28.330 0.10 . 1 . . . . . . . . 5480 1 382 . 1 1 31 31 GLU HB3 H 1 2.340 0.050 . 2 . . . . . . . . 5480 1 383 . 1 1 31 31 GLU HB2 H 1 2.260 0.050 . 2 . . . . . . . . 5480 1 384 . 1 1 31 31 GLU CG C 13 37.100 0.10 . 1 . . . . . . . . 5480 1 385 . 1 1 31 31 GLU HG3 H 1 2.300 0.050 . 1 . . . . . . . . 5480 1 386 . 1 1 31 31 GLU HG2 H 1 2.300 0.050 . 1 . . . . . . . . 5480 1 387 . 1 1 31 31 GLU C C 13 179.600 0.10 . 1 . . . . . . . . 5480 1 388 . 1 1 32 32 LEU N N 15 120.300 0.10 . 1 . . . . . . . . 5480 1 389 . 1 1 32 32 LEU H H 1 8.555 0.050 . 1 . . . . . . . . 5480 1 390 . 1 1 32 32 LEU CA C 13 58.190 0.10 . 1 . . . . . . . . 5480 1 391 . 1 1 32 32 LEU HA H 1 4.120 0.050 . 1 . . . . . . . . 5480 1 392 . 1 1 32 32 LEU CB C 13 42.540 0.10 . 1 . . . . . . . . 5480 1 393 . 1 1 32 32 LEU HB3 H 1 1.313 0.050 . 2 . . . . . . . . 5480 1 394 . 1 1 32 32 LEU HB2 H 1 1.796 0.050 . 2 . . . . . . . . 5480 1 395 . 1 1 32 32 LEU CD1 C 13 26.180 0.10 . 1 . . . . . . . . 5480 1 396 . 1 1 32 32 LEU HD11 H 1 0.461 0.050 . 2 . . . . . . . . 5480 1 397 . 1 1 32 32 LEU HD12 H 1 0.461 0.050 . 2 . . . . . . . . 5480 1 398 . 1 1 32 32 LEU HD13 H 1 0.461 0.050 . 2 . . . . . . . . 5480 1 399 . 1 1 32 32 LEU CD2 C 13 23.690 0.10 . 1 . . . . . . . . 5480 1 400 . 1 1 32 32 LEU HD21 H 1 0.609 0.050 . 2 . . . . . . . . 5480 1 401 . 1 1 32 32 LEU HD22 H 1 0.609 0.050 . 2 . . . . . . . . 5480 1 402 . 1 1 32 32 LEU HD23 H 1 0.609 0.050 . 2 . . . . . . . . 5480 1 403 . 1 1 32 32 LEU C C 13 178.900 0.10 . 1 . . . . . . . . 5480 1 404 . 1 1 33 33 GLY N N 15 105.190 0.10 . 1 . . . . . . . . 5480 1 405 . 1 1 33 33 GLY H H 1 8.659 0.050 . 1 . . . . . . . . 5480 1 406 . 1 1 33 33 GLY CA C 13 48.220 0.10 . 1 . . . . . . . . 5480 1 407 . 1 1 33 33 GLY HA3 H 1 3.870 0.050 . 2 . . . . . . . . 5480 1 408 . 1 1 33 33 GLY HA2 H 1 3.468 0.050 . 2 . . . . . . . . 5480 1 409 . 1 1 33 33 GLY C C 13 175.100 0.10 . 1 . . . . . . . . 5480 1 410 . 1 1 34 34 THR N N 15 117.670 0.10 . 1 . . . . . . . . 5480 1 411 . 1 1 34 34 THR H H 1 7.894 0.050 . 1 . . . . . . . . 5480 1 412 . 1 1 34 34 THR CA C 13 66.880 0.10 . 1 . . . . . . . . 5480 1 413 . 1 1 34 34 THR HA H 1 3.870 0.050 . 1 . . . . . . . . 5480 1 414 . 1 1 34 34 THR CB C 13 68.600 0.10 . 1 . . . . . . . . 5480 1 415 . 1 1 34 34 THR HB H 1 4.320 0.050 . 1 . . . . . . . . 5480 1 416 . 1 1 34 34 THR CG2 C 13 21.300 0.10 . 1 . . . . . . . . 5480 1 417 . 1 1 34 34 THR HG21 H 1 1.236 0.050 . 1 . . . . . . . . 5480 1 418 . 1 1 34 34 THR HG22 H 1 1.236 0.050 . 1 . . . . . . . . 5480 1 419 . 1 1 34 34 THR HG23 H 1 1.236 0.050 . 1 . . . . . . . . 5480 1 420 . 1 1 34 34 THR C C 13 177.100 0.10 . 1 . . . . . . . . 5480 1 421 . 1 1 35 35 VAL N N 15 121.799 0.10 . 1 . . . . . . . . 5480 1 422 . 1 1 35 35 VAL H H 1 7.432 0.050 . 1 . . . . . . . . 5480 1 423 . 1 1 35 35 VAL CA C 13 66.680 0.10 . 1 . . . . . . . . 5480 1 424 . 1 1 35 35 VAL HA H 1 3.454 0.050 . 1 . . . . . . . . 5480 1 425 . 1 1 35 35 VAL CB C 13 31.300 0.10 . 1 . . . . . . . . 5480 1 426 . 1 1 35 35 VAL HB H 1 1.870 0.050 . 1 . . . . . . . . 5480 1 427 . 1 1 35 35 VAL CG2 C 13 20.960 0.10 . 1 . . . . . . . . 5480 1 428 . 1 1 35 35 VAL HG21 H 1 0.352 0.050 . 2 . . . . . . . . 5480 1 429 . 1 1 35 35 VAL HG22 H 1 0.352 0.050 . 2 . . . . . . . . 5480 1 430 . 1 1 35 35 VAL HG23 H 1 0.352 0.050 . 2 . . . . . . . . 5480 1 431 . 1 1 35 35 VAL CG1 C 13 23.110 0.10 . 1 . . . . . . . . 5480 1 432 . 1 1 35 35 VAL HG11 H 1 0.660 0.050 . 2 . . . . . . . . 5480 1 433 . 1 1 35 35 VAL HG12 H 1 0.660 0.050 . 2 . . . . . . . . 5480 1 434 . 1 1 35 35 VAL HG13 H 1 0.660 0.050 . 2 . . . . . . . . 5480 1 435 . 1 1 35 35 VAL C C 13 178.150 0.10 . 1 . . . . . . . . 5480 1 436 . 1 1 36 36 MET N N 15 116.570 0.10 . 1 . . . . . . . . 5480 1 437 . 1 1 36 36 MET H H 1 8.218 0.050 . 1 . . . . . . . . 5480 1 438 . 1 1 36 36 MET CA C 13 59.260 0.10 . 1 . . . . . . . . 5480 1 439 . 1 1 36 36 MET HA H 1 3.875 0.050 . 1 . . . . . . . . 5480 1 440 . 1 1 36 36 MET CB C 13 32.237 0.10 . 1 . . . . . . . . 5480 1 441 . 1 1 36 36 MET HB3 H 1 1.756 0.050 . 1 . . . . . . . . 5480 1 442 . 1 1 36 36 MET HB2 H 1 1.756 0.050 . 1 . . . . . . . . 5480 1 443 . 1 1 36 36 MET CG C 13 33.310 0.10 . 1 . . . . . . . . 5480 1 444 . 1 1 36 36 MET HG3 H 1 2.366 0.050 . 2 . . . . . . . . 5480 1 445 . 1 1 36 36 MET HG2 H 1 2.445 0.050 . 2 . . . . . . . . 5480 1 446 . 1 1 36 36 MET CE C 13 17.490 0.10 . 1 . . . . . . . . 5480 1 447 . 1 1 36 36 MET HE1 H 1 1.754 0.050 . 1 . . . . . . . . 5480 1 448 . 1 1 36 36 MET HE2 H 1 1.754 0.050 . 1 . . . . . . . . 5480 1 449 . 1 1 36 36 MET HE3 H 1 1.754 0.050 . 1 . . . . . . . . 5480 1 450 . 1 1 36 36 MET C C 13 179.100 0.10 . 1 . . . . . . . . 5480 1 451 . 1 1 37 37 ARG N N 15 118.300 0.10 . 1 . . . . . . . . 5480 1 452 . 1 1 37 37 ARG H H 1 8.479 0.050 . 1 . . . . . . . . 5480 1 453 . 1 1 37 37 ARG CA C 13 58.800 0.10 . 1 . . . . . . . . 5480 1 454 . 1 1 37 37 ARG HA H 1 4.660 0.050 . 1 . . . . . . . . 5480 1 455 . 1 1 37 37 ARG CB C 13 30.160 0.10 . 1 . . . . . . . . 5480 1 456 . 1 1 37 37 ARG HB3 H 1 1.800 0.050 . 2 . . . . . . . . 5480 1 457 . 1 1 37 37 ARG HB2 H 1 1.910 0.050 . 2 . . . . . . . . 5480 1 458 . 1 1 37 37 ARG CG C 13 29.360 0.10 . 1 . . . . . . . . 5480 1 459 . 1 1 37 37 ARG HG3 H 1 1.810 0.050 . 1 . . . . . . . . 5480 1 460 . 1 1 37 37 ARG HG2 H 1 1.810 0.050 . 1 . . . . . . . . 5480 1 461 . 1 1 37 37 ARG CD C 13 43.360 0.10 . 1 . . . . . . . . 5480 1 462 . 1 1 37 37 ARG HD3 H 1 3.234 0.050 . 2 . . . . . . . . 5480 1 463 . 1 1 37 37 ARG HD2 H 1 3.054 0.050 . 2 . . . . . . . . 5480 1 464 . 1 1 37 37 ARG C C 13 181.100 0.10 . 1 . . . . . . . . 5480 1 465 . 1 1 38 38 SER N N 15 118.000 0.10 . 1 . . . . . . . . 5480 1 466 . 1 1 38 38 SER H H 1 7.891 0.050 . 1 . . . . . . . . 5480 1 467 . 1 1 38 38 SER CA C 13 61.733 0.10 . 1 . . . . . . . . 5480 1 468 . 1 1 38 38 SER HA H 1 4.225 0.050 . 1 . . . . . . . . 5480 1 469 . 1 1 38 38 SER CB C 13 62.800 0.10 . 1 . . . . . . . . 5480 1 470 . 1 1 38 38 SER HB3 H 1 3.687 0.050 . 2 . . . . . . . . 5480 1 471 . 1 1 38 38 SER HB2 H 1 4.010 0.050 . 2 . . . . . . . . 5480 1 472 . 1 1 38 38 SER C C 13 174.600 0.10 . 1 . . . . . . . . 5480 1 473 . 1 1 39 39 LEU N N 15 118.630 0.10 . 1 . . . . . . . . 5480 1 474 . 1 1 39 39 LEU H H 1 7.238 0.050 . 1 . . . . . . . . 5480 1 475 . 1 1 39 39 LEU CA C 13 53.600 0.10 . 1 . . . . . . . . 5480 1 476 . 1 1 39 39 LEU HA H 1 4.300 0.050 . 1 . . . . . . . . 5480 1 477 . 1 1 39 39 LEU CB C 13 41.220 0.10 . 1 . . . . . . . . 5480 1 478 . 1 1 39 39 LEU HB3 H 1 1.732 0.050 . 2 . . . . . . . . 5480 1 479 . 1 1 39 39 LEU HB2 H 1 1.690 0.050 . 2 . . . . . . . . 5480 1 480 . 1 1 39 39 LEU CG C 13 26.250 0.10 . 1 . . . . . . . . 5480 1 481 . 1 1 39 39 LEU CD1 C 13 26.030 0.10 . 1 . . . . . . . . 5480 1 482 . 1 1 39 39 LEU HD11 H 1 0.690 0.050 . 2 . . . . . . . . 5480 1 483 . 1 1 39 39 LEU HD12 H 1 0.690 0.050 . 2 . . . . . . . . 5480 1 484 . 1 1 39 39 LEU HD13 H 1 0.690 0.050 . 2 . . . . . . . . 5480 1 485 . 1 1 39 39 LEU CD2 C 13 22.580 0.10 . 1 . . . . . . . . 5480 1 486 . 1 1 39 39 LEU HD21 H 1 0.612 0.050 . 2 . . . . . . . . 5480 1 487 . 1 1 39 39 LEU HD22 H 1 0.612 0.050 . 2 . . . . . . . . 5480 1 488 . 1 1 39 39 LEU HD23 H 1 0.612 0.050 . 2 . . . . . . . . 5480 1 489 . 1 1 39 39 LEU C C 13 176.600 0.10 . 1 . . . . . . . . 5480 1 490 . 1 1 40 40 GLY N N 15 105.510 0.10 . 1 . . . . . . . . 5480 1 491 . 1 1 40 40 GLY H H 1 7.645 0.050 . 1 . . . . . . . . 5480 1 492 . 1 1 40 40 GLY CA C 13 45.880 0.10 . 1 . . . . . . . . 5480 1 493 . 1 1 40 40 GLY HA3 H 1 4.091 0.050 . 2 . . . . . . . . 5480 1 494 . 1 1 40 40 GLY HA2 H 1 3.728 0.050 . 2 . . . . . . . . 5480 1 495 . 1 1 40 40 GLY C C 13 174.500 0.10 . 1 . . . . . . . . 5480 1 496 . 1 1 41 41 GLN N N 15 117.570 0.10 . 1 . . . . . . . . 5480 1 497 . 1 1 41 41 GLN H H 1 7.780 0.050 . 1 . . . . . . . . 5480 1 498 . 1 1 41 41 GLN CA C 13 53.800 0.10 . 1 . . . . . . . . 5480 1 499 . 1 1 41 41 GLN HA H 1 4.410 0.050 . 1 . . . . . . . . 5480 1 500 . 1 1 41 41 GLN CB C 13 30.740 0.10 . 1 . . . . . . . . 5480 1 501 . 1 1 41 41 GLN HB3 H 1 2.030 0.050 . 2 . . . . . . . . 5480 1 502 . 1 1 41 41 GLN HB2 H 1 1.540 0.050 . 2 . . . . . . . . 5480 1 503 . 1 1 41 41 GLN CG C 13 33.640 0.10 . 1 . . . . . . . . 5480 1 504 . 1 1 41 41 GLN HG3 H 1 2.150 0.050 . 2 . . . . . . . . 5480 1 505 . 1 1 41 41 GLN HG2 H 1 2.004 0.050 . 2 . . . . . . . . 5480 1 506 . 1 1 41 41 GLN CD C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 507 . 1 1 41 41 GLN NE2 N 15 110.510 0.10 . 1 . . . . . . . . 5480 1 508 . 1 1 41 41 GLN HE21 H 1 7.189 0.050 . 2 . . . . . . . . 5480 1 509 . 1 1 41 41 GLN HE22 H 1 6.372 0.050 . 2 . . . . . . . . 5480 1 510 . 1 1 41 41 GLN C C 13 174.100 0.10 . 1 . . . . . . . . 5480 1 511 . 1 1 42 42 ASN N N 15 116.130 0.10 . 1 . . . . . . . . 5480 1 512 . 1 1 42 42 ASN H H 1 8.554 0.050 . 1 . . . . . . . . 5480 1 513 . 1 1 42 42 ASN CA C 13 51.170 0.10 . 1 . . . . . . . . 5480 1 514 . 1 1 42 42 ASN HA H 1 5.122 0.050 . 1 . . . . . . . . 5480 1 515 . 1 1 42 42 ASN CB C 13 39.074 0.10 . 1 . . . . . . . . 5480 1 516 . 1 1 42 42 ASN HB3 H 1 2.430 0.050 . 2 . . . . . . . . 5480 1 517 . 1 1 42 42 ASN HB2 H 1 2.700 0.050 . 2 . . . . . . . . 5480 1 518 . 1 1 42 42 ASN CG C 13 178.200 0.10 . 1 . . . . . . . . 5480 1 519 . 1 1 42 42 ASN ND2 N 15 111.600 0.10 . 1 . . . . . . . . 5480 1 520 . 1 1 42 42 ASN HD21 H 1 7.378 0.050 . 2 . . . . . . . . 5480 1 521 . 1 1 42 42 ASN HD22 H 1 6.591 0.050 . 2 . . . . . . . . 5480 1 522 . 1 1 42 42 ASN C C 13 171.900 0.10 . 1 . . . . . . . . 5480 1 523 . 1 1 43 43 PRO CA C 13 62.200 0.10 . 1 . . . . . . . . 5480 1 524 . 1 1 43 43 PRO HA H 1 4.680 0.050 . 1 . . . . . . . . 5480 1 525 . 1 1 43 43 PRO CB C 13 32.130 0.10 . 1 . . . . . . . . 5480 1 526 . 1 1 43 43 PRO HB3 H 1 2.000 0.050 . 2 . . . . . . . . 5480 1 527 . 1 1 43 43 PRO HB2 H 1 1.860 0.050 . 2 . . . . . . . . 5480 1 528 . 1 1 43 43 PRO CG C 13 27.300 0.10 . 1 . . . . . . . . 5480 1 529 . 1 1 43 43 PRO HG3 H 1 1.840 0.050 . 1 . . . . . . . . 5480 1 530 . 1 1 43 43 PRO HG2 H 1 1.840 0.050 . 1 . . . . . . . . 5480 1 531 . 1 1 43 43 PRO CD C 13 49.800 0.10 . 1 . . . . . . . . 5480 1 532 . 1 1 43 43 PRO HD3 H 1 3.170 0.050 . 2 . . . . . . . . 5480 1 533 . 1 1 43 43 PRO HD2 H 1 3.520 0.050 . 2 . . . . . . . . 5480 1 534 . 1 1 43 43 PRO C C 13 177.500 0.10 . 1 . . . . . . . . 5480 1 535 . 1 1 44 44 THR N N 15 112.210 0.10 . 1 . . . . . . . . 5480 1 536 . 1 1 44 44 THR H H 1 8.634 0.050 . 1 . . . . . . . . 5480 1 537 . 1 1 44 44 THR CA C 13 60.420 0.10 . 1 . . . . . . . . 5480 1 538 . 1 1 44 44 THR HA H 1 4.364 0.050 . 1 . . . . . . . . 5480 1 539 . 1 1 44 44 THR CB C 13 70.814 0.10 . 1 . . . . . . . . 5480 1 540 . 1 1 44 44 THR HB H 1 4.620 0.050 . 1 . . . . . . . . 5480 1 541 . 1 1 44 44 THR CG2 C 13 21.680 0.10 . 1 . . . . . . . . 5480 1 542 . 1 1 44 44 THR HG21 H 1 1.246 0.050 . 1 . . . . . . . . 5480 1 543 . 1 1 44 44 THR HG22 H 1 1.246 0.050 . 1 . . . . . . . . 5480 1 544 . 1 1 44 44 THR HG23 H 1 1.246 0.050 . 1 . . . . . . . . 5480 1 545 . 1 1 44 44 THR C C 13 175.200 0.10 . 1 . . . . . . . . 5480 1 546 . 1 1 45 45 GLU N N 15 120.170 0.10 . 1 . . . . . . . . 5480 1 547 . 1 1 45 45 GLU H H 1 8.667 0.050 . 1 . . . . . . . . 5480 1 548 . 1 1 45 45 GLU CA C 13 59.810 0.10 . 1 . . . . . . . . 5480 1 549 . 1 1 45 45 GLU HA H 1 3.880 0.050 . 1 . . . . . . . . 5480 1 550 . 1 1 45 45 GLU CB C 13 29.075 0.10 . 1 . . . . . . . . 5480 1 551 . 1 1 45 45 GLU HB3 H 1 1.974 0.050 . 1 . . . . . . . . 5480 1 552 . 1 1 45 45 GLU HB2 H 1 1.974 0.050 . 1 . . . . . . . . 5480 1 553 . 1 1 45 45 GLU CG C 13 36.100 0.10 . 1 . . . . . . . . 5480 1 554 . 1 1 45 45 GLU HG3 H 1 2.270 0.050 . 1 . . . . . . . . 5480 1 555 . 1 1 45 45 GLU HG2 H 1 2.270 0.050 . 1 . . . . . . . . 5480 1 556 . 1 1 45 45 GLU C C 13 178.900 0.10 . 1 . . . . . . . . 5480 1 557 . 1 1 46 46 ALA N N 15 120.150 0.10 . 1 . . . . . . . . 5480 1 558 . 1 1 46 46 ALA H H 1 8.109 0.050 . 1 . . . . . . . . 5480 1 559 . 1 1 46 46 ALA CA C 13 54.890 0.10 . 1 . . . . . . . . 5480 1 560 . 1 1 46 46 ALA HA H 1 4.024 0.050 . 1 . . . . . . . . 5480 1 561 . 1 1 46 46 ALA CB C 13 18.100 0.10 . 1 . . . . . . . . 5480 1 562 . 1 1 46 46 ALA HB1 H 1 1.320 0.050 . 1 . . . . . . . . 5480 1 563 . 1 1 46 46 ALA HB2 H 1 1.320 0.050 . 1 . . . . . . . . 5480 1 564 . 1 1 46 46 ALA HB3 H 1 1.320 0.050 . 1 . . . . . . . . 5480 1 565 . 1 1 46 46 ALA C C 13 180.300 0.10 . 1 . . . . . . . . 5480 1 566 . 1 1 47 47 GLU N N 15 118.180 0.10 . 1 . . . . . . . . 5480 1 567 . 1 1 47 47 GLU H H 1 7.469 0.050 . 1 . . . . . . . . 5480 1 568 . 1 1 47 47 GLU CA C 13 58.880 0.10 . 1 . . . . . . . . 5480 1 569 . 1 1 47 47 GLU HA H 1 3.972 0.050 . 1 . . . . . . . . 5480 1 570 . 1 1 47 47 GLU CB C 13 29.100 0.10 . 1 . . . . . . . . 5480 1 571 . 1 1 47 47 GLU HB3 H 1 2.196 0.050 . 2 . . . . . . . . 5480 1 572 . 1 1 47 47 GLU HB2 H 1 1.800 0.050 . 2 . . . . . . . . 5480 1 573 . 1 1 47 47 GLU CG C 13 37.340 0.10 . 1 . . . . . . . . 5480 1 574 . 1 1 47 47 GLU HG3 H 1 2.210 0.050 . 1 . . . . . . . . 5480 1 575 . 1 1 47 47 GLU HG2 H 1 2.210 0.050 . 1 . . . . . . . . 5480 1 576 . 1 1 47 47 GLU C C 13 179.500 0.10 . 1 . . . . . . . . 5480 1 577 . 1 1 48 48 LEU N N 15 118.720 0.10 . 1 . . . . . . . . 5480 1 578 . 1 1 48 48 LEU H H 1 7.930 0.050 . 1 . . . . . . . . 5480 1 579 . 1 1 48 48 LEU CA C 13 57.500 0.10 . 1 . . . . . . . . 5480 1 580 . 1 1 48 48 LEU HA H 1 3.870 0.050 . 1 . . . . . . . . 5480 1 581 . 1 1 48 48 LEU CB C 13 42.508 0.10 . 1 . . . . . . . . 5480 1 582 . 1 1 48 48 LEU HB3 H 1 1.058 0.050 . 2 . . . . . . . . 5480 1 583 . 1 1 48 48 LEU HB2 H 1 1.964 0.050 . 2 . . . . . . . . 5480 1 584 . 1 1 48 48 LEU CG C 13 26.560 0.10 . 1 . . . . . . . . 5480 1 585 . 1 1 48 48 LEU HG H 1 1.730 0.050 . 1 . . . . . . . . 5480 1 586 . 1 1 48 48 LEU CD1 C 13 25.920 0.10 . 1 . . . . . . . . 5480 1 587 . 1 1 48 48 LEU HD11 H 1 0.746 0.050 . 2 . . . . . . . . 5480 1 588 . 1 1 48 48 LEU HD12 H 1 0.746 0.050 . 2 . . . . . . . . 5480 1 589 . 1 1 48 48 LEU HD13 H 1 0.746 0.050 . 2 . . . . . . . . 5480 1 590 . 1 1 48 48 LEU CD2 C 13 26.130 0.10 . 1 . . . . . . . . 5480 1 591 . 1 1 48 48 LEU HD21 H 1 0.780 0.050 . 2 . . . . . . . . 5480 1 592 . 1 1 48 48 LEU HD22 H 1 0.780 0.050 . 2 . . . . . . . . 5480 1 593 . 1 1 48 48 LEU HD23 H 1 0.780 0.050 . 2 . . . . . . . . 5480 1 594 . 1 1 48 48 LEU C C 13 178.800 0.10 . 1 . . . . . . . . 5480 1 595 . 1 1 49 49 GLN N N 15 117.740 0.10 . 1 . . . . . . . . 5480 1 596 . 1 1 49 49 GLN H H 1 8.109 0.050 . 1 . . . . . . . . 5480 1 597 . 1 1 49 49 GLN CA C 13 58.500 0.10 . 1 . . . . . . . . 5480 1 598 . 1 1 49 49 GLN HA H 1 3.720 0.050 . 1 . . . . . . . . 5480 1 599 . 1 1 49 49 GLN CB C 13 28.130 0.10 . 1 . . . . . . . . 5480 1 600 . 1 1 49 49 GLN HB3 H 1 2.098 0.050 . 2 . . . . . . . . 5480 1 601 . 1 1 49 49 GLN HB2 H 1 2.141 0.050 . 2 . . . . . . . . 5480 1 602 . 1 1 49 49 GLN CG C 13 34.100 0.10 . 1 . . . . . . . . 5480 1 603 . 1 1 49 49 GLN HG3 H 1 2.354 0.050 . 2 . . . . . . . . 5480 1 604 . 1 1 49 49 GLN HG2 H 1 2.411 0.050 . 2 . . . . . . . . 5480 1 605 . 1 1 49 49 GLN CD C 13 180.300 0.10 . 1 . . . . . . . . 5480 1 606 . 1 1 49 49 GLN NE2 N 15 112.280 0.10 . 1 . . . . . . . . 5480 1 607 . 1 1 49 49 GLN HE21 H 1 7.391 0.050 . 2 . . . . . . . . 5480 1 608 . 1 1 49 49 GLN HE22 H 1 6.776 0.050 . 2 . . . . . . . . 5480 1 609 . 1 1 49 49 GLN C C 13 178.500 0.10 . 1 . . . . . . . . 5480 1 610 . 1 1 50 50 ASP N N 15 120.180 0.10 . 1 . . . . . . . . 5480 1 611 . 1 1 50 50 ASP H H 1 7.965 0.050 . 1 . . . . . . . . 5480 1 612 . 1 1 50 50 ASP CA C 13 57.580 0.10 . 1 . . . . . . . . 5480 1 613 . 1 1 50 50 ASP HA H 1 4.361 0.050 . 1 . . . . . . . . 5480 1 614 . 1 1 50 50 ASP CB C 13 40.192 0.10 . 1 . . . . . . . . 5480 1 615 . 1 1 50 50 ASP HB3 H 1 2.659 0.050 . 2 . . . . . . . . 5480 1 616 . 1 1 50 50 ASP HB2 H 1 2.758 0.050 . 2 . . . . . . . . 5480 1 617 . 1 1 50 50 ASP CG C 13 179.300 0.10 . 1 . . . . . . . . 5480 1 618 . 1 1 50 50 ASP C C 13 179.000 0.10 . 1 . . . . . . . . 5480 1 619 . 1 1 51 51 MET N N 15 119.400 0.10 . 1 . . . . . . . . 5480 1 620 . 1 1 51 51 MET H H 1 7.882 0.050 . 1 . . . . . . . . 5480 1 621 . 1 1 51 51 MET CA C 13 59.950 0.10 . 1 . . . . . . . . 5480 1 622 . 1 1 51 51 MET HA H 1 3.880 0.050 . 1 . . . . . . . . 5480 1 623 . 1 1 51 51 MET CB C 13 33.070 0.10 . 1 . . . . . . . . 5480 1 624 . 1 1 51 51 MET HB3 H 1 2.000 0.050 . 1 . . . . . . . . 5480 1 625 . 1 1 51 51 MET HB2 H 1 2.000 0.050 . 1 . . . . . . . . 5480 1 626 . 1 1 51 51 MET CG C 13 32.660 0.10 . 1 . . . . . . . . 5480 1 627 . 1 1 51 51 MET HG3 H 1 2.464 0.050 . 1 . . . . . . . . 5480 1 628 . 1 1 51 51 MET HG2 H 1 2.464 0.050 . 1 . . . . . . . . 5480 1 629 . 1 1 51 51 MET CE C 13 16.630 0.10 . 1 . . . . . . . . 5480 1 630 . 1 1 51 51 MET HE1 H 1 1.802 0.050 . 1 . . . . . . . . 5480 1 631 . 1 1 51 51 MET HE2 H 1 1.802 0.050 . 1 . . . . . . . . 5480 1 632 . 1 1 51 51 MET HE3 H 1 1.802 0.050 . 1 . . . . . . . . 5480 1 633 . 1 1 51 51 MET C C 13 179.400 0.10 . 1 . . . . . . . . 5480 1 634 . 1 1 52 52 ILE N N 15 118.190 0.10 . 1 . . . . . . . . 5480 1 635 . 1 1 52 52 ILE H H 1 7.786 0.050 . 1 . . . . . . . . 5480 1 636 . 1 1 52 52 ILE CA C 13 64.720 0.10 . 1 . . . . . . . . 5480 1 637 . 1 1 52 52 ILE HA H 1 3.696 0.050 . 1 . . . . . . . . 5480 1 638 . 1 1 52 52 ILE CB C 13 36.540 0.10 . 1 . . . . . . . . 5480 1 639 . 1 1 52 52 ILE HB H 1 1.977 0.050 . 1 . . . . . . . . 5480 1 640 . 1 1 52 52 ILE CG1 C 13 28.970 0.10 . 2 . . . . . . . . 5480 1 641 . 1 1 52 52 ILE HG13 H 1 1.580 0.050 . 1 . . . . . . . . 5480 1 642 . 1 1 52 52 ILE HG12 H 1 1.175 0.050 . 1 . . . . . . . . 5480 1 643 . 1 1 52 52 ILE CD1 C 13 12.110 0.10 . 1 . . . . . . . . 5480 1 644 . 1 1 52 52 ILE HD11 H 1 0.660 0.050 . 1 . . . . . . . . 5480 1 645 . 1 1 52 52 ILE HD12 H 1 0.660 0.050 . 1 . . . . . . . . 5480 1 646 . 1 1 52 52 ILE HD13 H 1 0.660 0.050 . 1 . . . . . . . . 5480 1 647 . 1 1 52 52 ILE CG2 C 13 16.250 0.10 . 1 . . . . . . . . 5480 1 648 . 1 1 52 52 ILE HG21 H 1 0.713 0.050 . 1 . . . . . . . . 5480 1 649 . 1 1 52 52 ILE HG22 H 1 0.713 0.050 . 1 . . . . . . . . 5480 1 650 . 1 1 52 52 ILE HG23 H 1 0.713 0.050 . 1 . . . . . . . . 5480 1 651 . 1 1 52 52 ILE C C 13 178.100 0.10 . 1 . . . . . . . . 5480 1 652 . 1 1 53 53 ASN N N 15 117.580 0.10 . 1 . . . . . . . . 5480 1 653 . 1 1 53 53 ASN H H 1 8.672 0.050 . 1 . . . . . . . . 5480 1 654 . 1 1 53 53 ASN CA C 13 55.800 0.10 . 1 . . . . . . . . 5480 1 655 . 1 1 53 53 ASN HA H 1 4.370 0.050 . 1 . . . . . . . . 5480 1 656 . 1 1 53 53 ASN CB C 13 37.990 0.10 . 1 . . . . . . . . 5480 1 657 . 1 1 53 53 ASN HB3 H 1 2.990 0.050 . 2 . . . . . . . . 5480 1 658 . 1 1 53 53 ASN HB2 H 1 2.850 0.050 . 2 . . . . . . . . 5480 1 659 . 1 1 53 53 ASN CG C 13 176.500 0.10 . 1 . . . . . . . . 5480 1 660 . 1 1 53 53 ASN ND2 N 15 111.050 0.10 . 1 . . . . . . . . 5480 1 661 . 1 1 53 53 ASN HD21 H 1 7.745 0.050 . 2 . . . . . . . . 5480 1 662 . 1 1 53 53 ASN HD22 H 1 6.842 0.050 . 2 . . . . . . . . 5480 1 663 . 1 1 53 53 ASN C C 13 177.000 0.10 . 1 . . . . . . . . 5480 1 664 . 1 1 54 54 GLU N N 15 116.065 0.10 . 1 . . . . . . . . 5480 1 665 . 1 1 54 54 GLU H H 1 7.585 0.050 . 1 . . . . . . . . 5480 1 666 . 1 1 54 54 GLU CA C 13 58.977 0.10 . 1 . . . . . . . . 5480 1 667 . 1 1 54 54 GLU HA H 1 4.027 0.050 . 1 . . . . . . . . 5480 1 668 . 1 1 54 54 GLU CB C 13 30.500 0.10 . 1 . . . . . . . . 5480 1 669 . 1 1 54 54 GLU HB3 H 1 2.300 0.050 . 2 . . . . . . . . 5480 1 670 . 1 1 54 54 GLU HB2 H 1 2.200 0.050 . 2 . . . . . . . . 5480 1 671 . 1 1 54 54 GLU CG C 13 36.190 0.10 . 1 . . . . . . . . 5480 1 672 . 1 1 54 54 GLU HG3 H 1 2.423 0.050 . 1 . . . . . . . . 5480 1 673 . 1 1 54 54 GLU HG2 H 1 2.423 0.050 . 1 . . . . . . . . 5480 1 674 . 1 1 54 54 GLU C C 13 177.400 0.10 . 1 . . . . . . . . 5480 1 675 . 1 1 55 55 VAL N N 15 110.470 0.10 . 1 . . . . . . . . 5480 1 676 . 1 1 55 55 VAL H H 1 7.153 0.050 . 1 . . . . . . . . 5480 1 677 . 1 1 55 55 VAL CA C 13 60.650 0.10 . 1 . . . . . . . . 5480 1 678 . 1 1 55 55 VAL HA H 1 4.235 0.050 . 1 . . . . . . . . 5480 1 679 . 1 1 55 55 VAL CB C 13 33.034 0.10 . 1 . . . . . . . . 5480 1 680 . 1 1 55 55 VAL HB H 1 2.120 0.050 . 1 . . . . . . . . 5480 1 681 . 1 1 55 55 VAL CG2 C 13 20.760 0.10 . 1 . . . . . . . . 5480 1 682 . 1 1 55 55 VAL HG21 H 1 0.840 0.050 . 2 . . . . . . . . 5480 1 683 . 1 1 55 55 VAL HG22 H 1 0.840 0.050 . 2 . . . . . . . . 5480 1 684 . 1 1 55 55 VAL HG23 H 1 0.840 0.050 . 2 . . . . . . . . 5480 1 685 . 1 1 55 55 VAL CG1 C 13 22.150 0.10 . 1 . . . . . . . . 5480 1 686 . 1 1 55 55 VAL HG11 H 1 0.713 0.050 . 2 . . . . . . . . 5480 1 687 . 1 1 55 55 VAL HG12 H 1 0.713 0.050 . 2 . . . . . . . . 5480 1 688 . 1 1 55 55 VAL HG13 H 1 0.713 0.050 . 2 . . . . . . . . 5480 1 689 . 1 1 55 55 VAL C C 13 175.500 0.10 . 1 . . . . . . . . 5480 1 690 . 1 1 56 56 ASP N N 15 121.218 0.10 . 1 . . . . . . . . 5480 1 691 . 1 1 56 56 ASP H H 1 7.698 0.050 . 1 . . . . . . . . 5480 1 692 . 1 1 56 56 ASP CA C 13 53.704 0.10 . 1 . . . . . . . . 5480 1 693 . 1 1 56 56 ASP HA H 1 4.505 0.050 . 1 . . . . . . . . 5480 1 694 . 1 1 56 56 ASP CB C 13 40.600 0.10 . 1 . . . . . . . . 5480 1 695 . 1 1 56 56 ASP HB3 H 1 2.710 0.050 . 2 . . . . . . . . 5480 1 696 . 1 1 56 56 ASP HB2 H 1 2.490 0.050 . 2 . . . . . . . . 5480 1 697 . 1 1 56 56 ASP CG C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 698 . 1 1 56 56 ASP C C 13 176.000 0.10 . 1 . . . . . . . . 5480 1 699 . 1 1 57 57 ALA N N 15 131.060 0.10 . 1 . . . . . . . . 5480 1 700 . 1 1 57 57 ALA H H 1 8.094 0.050 . 1 . . . . . . . . 5480 1 701 . 1 1 57 57 ALA CA C 13 54.200 0.10 . 1 . . . . . . . . 5480 1 702 . 1 1 57 57 ALA HA H 1 4.150 0.050 . 1 . . . . . . . . 5480 1 703 . 1 1 57 57 ALA CB C 13 19.600 0.10 . 1 . . . . . . . . 5480 1 704 . 1 1 57 57 ALA HB1 H 1 1.475 0.050 . 1 . . . . . . . . 5480 1 705 . 1 1 57 57 ALA HB2 H 1 1.475 0.050 . 1 . . . . . . . . 5480 1 706 . 1 1 57 57 ALA HB3 H 1 1.475 0.050 . 1 . . . . . . . . 5480 1 707 . 1 1 57 57 ALA C C 13 178.800 0.10 . 1 . . . . . . . . 5480 1 708 . 1 1 58 58 ASP N N 15 113.560 0.10 . 1 . . . . . . . . 5480 1 709 . 1 1 58 58 ASP H H 1 8.182 0.050 . 1 . . . . . . . . 5480 1 710 . 1 1 58 58 ASP CA C 13 52.790 0.10 . 1 . . . . . . . . 5480 1 711 . 1 1 58 58 ASP HA H 1 4.577 0.050 . 1 . . . . . . . . 5480 1 712 . 1 1 58 58 ASP CB C 13 39.740 0.10 . 1 . . . . . . . . 5480 1 713 . 1 1 58 58 ASP HB3 H 1 2.999 0.050 . 2 . . . . . . . . 5480 1 714 . 1 1 58 58 ASP HB2 H 1 2.621 0.050 . 2 . . . . . . . . 5480 1 715 . 1 1 58 58 ASP CG C 13 180.900 0.10 . 1 . . . . . . . . 5480 1 716 . 1 1 58 58 ASP C C 13 177.860 0.10 . 1 . . . . . . . . 5480 1 717 . 1 1 59 59 GLY N N 15 108.150 0.10 . 1 . . . . . . . . 5480 1 718 . 1 1 59 59 GLY H H 1 7.524 0.050 . 1 . . . . . . . . 5480 1 719 . 1 1 59 59 GLY CA C 13 47.000 0.10 . 1 . . . . . . . . 5480 1 720 . 1 1 59 59 GLY HA3 H 1 3.745 0.050 . 2 . . . . . . . . 5480 1 721 . 1 1 59 59 GLY HA2 H 1 3.830 0.050 . 2 . . . . . . . . 5480 1 722 . 1 1 59 59 GLY C C 13 175.100 0.10 . 1 . . . . . . . . 5480 1 723 . 1 1 60 60 ASN N N 15 118.400 0.10 . 1 . . . . . . . . 5480 1 724 . 1 1 60 60 ASN H H 1 8.121 0.050 . 1 . . . . . . . . 5480 1 725 . 1 1 60 60 ASN CA C 13 52.530 0.10 . 1 . . . . . . . . 5480 1 726 . 1 1 60 60 ASN HA H 1 4.580 0.050 . 1 . . . . . . . . 5480 1 727 . 1 1 60 60 ASN CB C 13 37.460 0.10 . 1 . . . . . . . . 5480 1 728 . 1 1 60 60 ASN HB3 H 1 3.250 0.050 . 2 . . . . . . . . 5480 1 729 . 1 1 60 60 ASN HB2 H 1 2.600 0.050 . 2 . . . . . . . . 5480 1 730 . 1 1 60 60 ASN CG C 13 178.900 0.10 . 1 . . . . . . . . 5480 1 731 . 1 1 60 60 ASN ND2 N 15 114.660 0.10 . 1 . . . . . . . . 5480 1 732 . 1 1 60 60 ASN HD21 H 1 7.644 0.050 . 2 . . . . . . . . 5480 1 733 . 1 1 60 60 ASN HD22 H 1 6.882 0.050 . 2 . . . . . . . . 5480 1 734 . 1 1 60 60 ASN C C 13 176.900 0.10 . 1 . . . . . . . . 5480 1 735 . 1 1 61 61 GLY N N 15 113.010 0.10 . 1 . . . . . . . . 5480 1 736 . 1 1 61 61 GLY H H 1 10.518 0.050 . 1 . . . . . . . . 5480 1 737 . 1 1 61 61 GLY CA C 13 45.400 0.10 . 1 . . . . . . . . 5480 1 738 . 1 1 61 61 GLY HA3 H 1 3.440 0.050 . 2 . . . . . . . . 5480 1 739 . 1 1 61 61 GLY HA2 H 1 4.200 0.050 . 2 . . . . . . . . 5480 1 740 . 1 1 61 61 GLY C C 13 173.400 0.10 . 1 . . . . . . . . 5480 1 741 . 1 1 62 62 THR N N 15 107.880 0.10 . 1 . . . . . . . . 5480 1 742 . 1 1 62 62 THR H H 1 7.594 0.050 . 1 . . . . . . . . 5480 1 743 . 1 1 62 62 THR CA C 13 59.350 0.10 . 1 . . . . . . . . 5480 1 744 . 1 1 62 62 THR HA H 1 4.730 0.050 . 1 . . . . . . . . 5480 1 745 . 1 1 62 62 THR CB C 13 72.200 0.10 . 1 . . . . . . . . 5480 1 746 . 1 1 62 62 THR HB H 1 3.960 0.050 . 1 . . . . . . . . 5480 1 747 . 1 1 62 62 THR CG2 C 13 22.400 0.10 . 1 . . . . . . . . 5480 1 748 . 1 1 62 62 THR HG21 H 1 1.060 0.050 . 1 . . . . . . . . 5480 1 749 . 1 1 62 62 THR HG22 H 1 1.060 0.050 . 1 . . . . . . . . 5480 1 750 . 1 1 62 62 THR HG23 H 1 1.060 0.050 . 1 . . . . . . . . 5480 1 751 . 1 1 62 62 THR C C 13 173.500 0.10 . 1 . . . . . . . . 5480 1 752 . 1 1 63 63 ILE N N 15 122.990 0.10 . 1 . . . . . . . . 5480 1 753 . 1 1 63 63 ILE H H 1 8.697 0.050 . 1 . . . . . . . . 5480 1 754 . 1 1 63 63 ILE CA C 13 59.500 0.10 . 1 . . . . . . . . 5480 1 755 . 1 1 63 63 ILE HA H 1 5.140 0.050 . 1 . . . . . . . . 5480 1 756 . 1 1 63 63 ILE CB C 13 39.630 0.10 . 1 . . . . . . . . 5480 1 757 . 1 1 63 63 ILE HB H 1 2.052 0.050 . 1 . . . . . . . . 5480 1 758 . 1 1 63 63 ILE CG1 C 13 27.390 0.10 . 2 . . . . . . . . 5480 1 759 . 1 1 63 63 ILE HG13 H 1 1.113 0.050 . 1 . . . . . . . . 5480 1 760 . 1 1 63 63 ILE HG12 H 1 1.600 0.050 . 1 . . . . . . . . 5480 1 761 . 1 1 63 63 ILE CD1 C 13 13.800 0.10 . 1 . . . . . . . . 5480 1 762 . 1 1 63 63 ILE HD11 H 1 0.990 0.050 . 1 . . . . . . . . 5480 1 763 . 1 1 63 63 ILE HD12 H 1 0.990 0.050 . 1 . . . . . . . . 5480 1 764 . 1 1 63 63 ILE HD13 H 1 0.990 0.050 . 1 . . . . . . . . 5480 1 765 . 1 1 63 63 ILE CG2 C 13 18.390 0.10 . 1 . . . . . . . . 5480 1 766 . 1 1 63 63 ILE HG21 H 1 1.200 0.050 . 1 . . . . . . . . 5480 1 767 . 1 1 63 63 ILE HG22 H 1 1.200 0.050 . 1 . . . . . . . . 5480 1 768 . 1 1 63 63 ILE HG23 H 1 1.200 0.050 . 1 . . . . . . . . 5480 1 769 . 1 1 63 63 ILE C C 13 175.700 0.10 . 1 . . . . . . . . 5480 1 770 . 1 1 64 64 ASP N N 15 128.000 0.10 . 1 . . . . . . . . 5480 1 771 . 1 1 64 64 ASP H H 1 8.876 0.050 . 1 . . . . . . . . 5480 1 772 . 1 1 64 64 ASP CA C 13 51.840 0.10 . 1 . . . . . . . . 5480 1 773 . 1 1 64 64 ASP HA H 1 5.415 0.050 . 1 . . . . . . . . 5480 1 774 . 1 1 64 64 ASP CB C 13 42.200 0.10 . 1 . . . . . . . . 5480 1 775 . 1 1 64 64 ASP HB3 H 1 2.790 0.050 . 2 . . . . . . . . 5480 1 776 . 1 1 64 64 ASP HB2 H 1 3.090 0.050 . 2 . . . . . . . . 5480 1 777 . 1 1 64 64 ASP CG C 13 178.950 0.10 . 1 . . . . . . . . 5480 1 778 . 1 1 64 64 ASP C C 13 176.200 0.10 . 1 . . . . . . . . 5480 1 779 . 1 1 65 65 PHE N N 15 118.010 0.10 . 1 . . . . . . . . 5480 1 780 . 1 1 65 65 PHE H H 1 8.893 0.050 . 1 . . . . . . . . 5480 1 781 . 1 1 65 65 PHE CA C 13 63.242 0.10 . 1 . . . . . . . . 5480 1 782 . 1 1 65 65 PHE HA H 1 3.971 0.050 . 1 . . . . . . . . 5480 1 783 . 1 1 65 65 PHE CB C 13 35.900 0.10 . 1 . . . . . . . . 5480 1 784 . 1 1 65 65 PHE HB3 H 1 2.759 0.050 . 2 . . . . . . . . 5480 1 785 . 1 1 65 65 PHE HB2 H 1 2.006 0.050 . 2 . . . . . . . . 5480 1 786 . 1 1 65 65 PHE CD1 C 13 131.830 0.10 . 1 . . . . . . . . 5480 1 787 . 1 1 65 65 PHE HD1 H 1 6.681 0.050 . 1 . . . . . . . . 5480 1 788 . 1 1 65 65 PHE CE1 C 13 131.050 0.10 . 1 . . . . . . . . 5480 1 789 . 1 1 65 65 PHE HE1 H 1 7.150 0.050 . 1 . . . . . . . . 5480 1 790 . 1 1 65 65 PHE CE2 C 13 131.050 0.10 . 1 . . . . . . . . 5480 1 791 . 1 1 65 65 PHE HE2 H 1 7.150 0.050 . 1 . . . . . . . . 5480 1 792 . 1 1 65 65 PHE CD2 C 13 131.830 0.10 . 1 . . . . . . . . 5480 1 793 . 1 1 65 65 PHE HD2 H 1 6.681 0.050 . 1 . . . . . . . . 5480 1 794 . 1 1 65 65 PHE C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 795 . 1 1 66 66 PRO CA C 13 66.700 0.10 . 1 . . . . . . . . 5480 1 796 . 1 1 66 66 PRO HA H 1 3.782 0.050 . 1 . . . . . . . . 5480 1 797 . 1 1 66 66 PRO CB C 13 30.600 0.10 . 1 . . . . . . . . 5480 1 798 . 1 1 66 66 PRO HB3 H 1 1.830 0.050 . 2 . . . . . . . . 5480 1 799 . 1 1 66 66 PRO HB2 H 1 2.150 0.050 . 2 . . . . . . . . 5480 1 800 . 1 1 66 66 PRO CG C 13 28.320 0.10 . 1 . . . . . . . . 5480 1 801 . 1 1 66 66 PRO HG3 H 1 1.820 0.050 . 2 . . . . . . . . 5480 1 802 . 1 1 66 66 PRO HG2 H 1 2.120 0.050 . 2 . . . . . . . . 5480 1 803 . 1 1 66 66 PRO CD C 13 49.040 0.10 . 1 . . . . . . . . 5480 1 804 . 1 1 66 66 PRO HD3 H 1 3.700 0.050 . 1 . . . . . . . . 5480 1 805 . 1 1 66 66 PRO HD2 H 1 3.700 0.050 . 1 . . . . . . . . 5480 1 806 . 1 1 66 66 PRO C C 13 180.000 0.10 . 1 . . . . . . . . 5480 1 807 . 1 1 67 67 GLU N N 15 117.300 0.10 . 1 . . . . . . . . 5480 1 808 . 1 1 67 67 GLU H H 1 8.137 0.050 . 1 . . . . . . . . 5480 1 809 . 1 1 67 67 GLU CA C 13 58.830 0.10 . 1 . . . . . . . . 5480 1 810 . 1 1 67 67 GLU HA H 1 3.968 0.050 . 1 . . . . . . . . 5480 1 811 . 1 1 67 67 GLU CB C 13 30.150 0.10 . 1 . . . . . . . . 5480 1 812 . 1 1 67 67 GLU HB3 H 1 2.570 0.050 . 2 . . . . . . . . 5480 1 813 . 1 1 67 67 GLU HB2 H 1 2.317 0.050 . 2 . . . . . . . . 5480 1 814 . 1 1 67 67 GLU CG C 13 37.340 0.10 . 1 . . . . . . . . 5480 1 815 . 1 1 67 67 GLU HG3 H 1 2.880 0.050 . 2 . . . . . . . . 5480 1 816 . 1 1 67 67 GLU HG2 H 1 2.940 0.050 . 2 . . . . . . . . 5480 1 817 . 1 1 67 67 GLU C C 13 179.400 0.10 . 1 . . . . . . . . 5480 1 818 . 1 1 68 68 PHE N N 15 122.910 0.10 . 1 . . . . . . . . 5480 1 819 . 1 1 68 68 PHE H H 1 8.607 0.050 . 1 . . . . . . . . 5480 1 820 . 1 1 68 68 PHE CA C 13 61.510 0.10 . 1 . . . . . . . . 5480 1 821 . 1 1 68 68 PHE HA H 1 3.700 0.050 . 1 . . . . . . . . 5480 1 822 . 1 1 68 68 PHE CB C 13 40.510 0.10 . 1 . . . . . . . . 5480 1 823 . 1 1 68 68 PHE HB3 H 1 3.100 0.050 . 2 . . . . . . . . 5480 1 824 . 1 1 68 68 PHE HB2 H 1 3.380 0.050 . 2 . . . . . . . . 5480 1 825 . 1 1 68 68 PHE CD1 C 13 131.840 0.10 . 1 . . . . . . . . 5480 1 826 . 1 1 68 68 PHE HD1 H 1 6.810 0.050 . 1 . . . . . . . . 5480 1 827 . 1 1 68 68 PHE CE1 C 13 131.210 0.10 . 1 . . . . . . . . 5480 1 828 . 1 1 68 68 PHE HE1 H 1 7.023 0.050 . 1 . . . . . . . . 5480 1 829 . 1 1 68 68 PHE CE2 C 13 131.210 0.10 . 1 . . . . . . . . 5480 1 830 . 1 1 68 68 PHE HE2 H 1 7.023 0.050 . 1 . . . . . . . . 5480 1 831 . 1 1 68 68 PHE CD2 C 13 131.840 0.10 . 1 . . . . . . . . 5480 1 832 . 1 1 68 68 PHE HD2 H 1 6.810 0.050 . 1 . . . . . . . . 5480 1 833 . 1 1 68 68 PHE C C 13 176.600 0.10 . 1 . . . . . . . . 5480 1 834 . 1 1 69 69 LEU N N 15 119.450 0.10 . 1 . . . . . . . . 5480 1 835 . 1 1 69 69 LEU H H 1 8.776 0.050 . 1 . . . . . . . . 5480 1 836 . 1 1 69 69 LEU CA C 13 57.940 0.10 . 1 . . . . . . . . 5480 1 837 . 1 1 69 69 LEU HA H 1 3.270 0.050 . 1 . . . . . . . . 5480 1 838 . 1 1 69 69 LEU CB C 13 41.320 0.10 . 1 . . . . . . . . 5480 1 839 . 1 1 69 69 LEU HB3 H 1 1.169 0.050 . 2 . . . . . . . . 5480 1 840 . 1 1 69 69 LEU HB2 H 1 1.193 0.050 . 2 . . . . . . . . 5480 1 841 . 1 1 69 69 LEU CG C 13 26.060 0.10 . 1 . . . . . . . . 5480 1 842 . 1 1 69 69 LEU HG H 1 1.050 0.050 . 1 . . . . . . . . 5480 1 843 . 1 1 69 69 LEU CD1 C 13 24.840 0.10 . 1 . . . . . . . . 5480 1 844 . 1 1 69 69 LEU HD11 H 1 0.650 0.050 . 2 . . . . . . . . 5480 1 845 . 1 1 69 69 LEU HD12 H 1 0.650 0.050 . 2 . . . . . . . . 5480 1 846 . 1 1 69 69 LEU HD13 H 1 0.650 0.050 . 2 . . . . . . . . 5480 1 847 . 1 1 69 69 LEU CD2 C 13 25.500 0.10 . 1 . . . . . . . . 5480 1 848 . 1 1 69 69 LEU HD21 H 1 0.607 0.050 . 2 . . . . . . . . 5480 1 849 . 1 1 69 69 LEU HD22 H 1 0.607 0.050 . 2 . . . . . . . . 5480 1 850 . 1 1 69 69 LEU HD23 H 1 0.607 0.050 . 2 . . . . . . . . 5480 1 851 . 1 1 69 69 LEU C C 13 178.500 0.10 . 1 . . . . . . . . 5480 1 852 . 1 1 70 70 THR N N 15 114.110 0.10 . 1 . . . . . . . . 5480 1 853 . 1 1 70 70 THR H H 1 7.530 0.050 . 1 . . . . . . . . 5480 1 854 . 1 1 70 70 THR CA C 13 66.300 0.10 . 1 . . . . . . . . 5480 1 855 . 1 1 70 70 THR HA H 1 3.610 0.050 . 1 . . . . . . . . 5480 1 856 . 1 1 70 70 THR CB C 13 68.390 0.10 . 1 . . . . . . . . 5480 1 857 . 1 1 70 70 THR HB H 1 4.070 0.050 . 1 . . . . . . . . 5480 1 858 . 1 1 70 70 THR CG2 C 13 21.294 0.10 . 1 . . . . . . . . 5480 1 859 . 1 1 70 70 THR HG21 H 1 1.184 0.050 . 1 . . . . . . . . 5480 1 860 . 1 1 70 70 THR HG22 H 1 1.184 0.050 . 1 . . . . . . . . 5480 1 861 . 1 1 70 70 THR HG23 H 1 1.184 0.050 . 1 . . . . . . . . 5480 1 862 . 1 1 70 70 THR C C 13 176.000 0.10 . 1 . . . . . . . . 5480 1 863 . 1 1 71 71 MET N N 15 120.120 0.10 . 1 . . . . . . . . 5480 1 864 . 1 1 71 71 MET H H 1 7.114 0.050 . 1 . . . . . . . . 5480 1 865 . 1 1 71 71 MET CA C 13 58.700 0.10 . 1 . . . . . . . . 5480 1 866 . 1 1 71 71 MET HA H 1 3.630 0.050 . 1 . . . . . . . . 5480 1 867 . 1 1 71 71 MET CB C 13 30.810 0.10 . 1 . . . . . . . . 5480 1 868 . 1 1 71 71 MET HB3 H 1 1.556 0.050 . 2 . . . . . . . . 5480 1 869 . 1 1 71 71 MET HB2 H 1 1.650 0.050 . 2 . . . . . . . . 5480 1 870 . 1 1 71 71 MET CG C 13 31.060 0.10 . 1 . . . . . . . . 5480 1 871 . 1 1 71 71 MET HG3 H 1 1.410 0.050 . 1 . . . . . . . . 5480 1 872 . 1 1 71 71 MET HG2 H 1 1.410 0.050 . 1 . . . . . . . . 5480 1 873 . 1 1 71 71 MET CE C 13 16.460 0.10 . 1 . . . . . . . . 5480 1 874 . 1 1 71 71 MET HE1 H 1 0.770 0.050 . 1 . . . . . . . . 5480 1 875 . 1 1 71 71 MET HE2 H 1 0.770 0.050 . 1 . . . . . . . . 5480 1 876 . 1 1 71 71 MET HE3 H 1 0.770 0.050 . 1 . . . . . . . . 5480 1 877 . 1 1 71 71 MET C C 13 177.700 0.10 . 1 . . . . . . . . 5480 1 878 . 1 1 72 72 MET N N 15 117.640 0.10 . 1 . . . . . . . . 5480 1 879 . 1 1 72 72 MET H H 1 7.899 0.050 . 1 . . . . . . . . 5480 1 880 . 1 1 72 72 MET CA C 13 56.342 0.10 . 1 . . . . . . . . 5480 1 881 . 1 1 72 72 MET HA H 1 3.520 0.050 . 1 . . . . . . . . 5480 1 882 . 1 1 72 72 MET CB C 13 30.350 0.10 . 1 . . . . . . . . 5480 1 883 . 1 1 72 72 MET HB3 H 1 0.680 0.050 . 2 . . . . . . . . 5480 1 884 . 1 1 72 72 MET HB2 H 1 0.970 0.050 . 2 . . . . . . . . 5480 1 885 . 1 1 72 72 MET CG C 13 32.550 0.10 . 1 . . . . . . . . 5480 1 886 . 1 1 72 72 MET HG3 H 1 1.220 0.050 . 2 . . . . . . . . 5480 1 887 . 1 1 72 72 MET HG2 H 1 1.300 0.050 . 2 . . . . . . . . 5480 1 888 . 1 1 72 72 MET CE C 13 17.390 0.10 . 1 . . . . . . . . 5480 1 889 . 1 1 72 72 MET HE1 H 1 1.595 0.050 . 1 . . . . . . . . 5480 1 890 . 1 1 72 72 MET HE2 H 1 1.595 0.050 . 1 . . . . . . . . 5480 1 891 . 1 1 72 72 MET HE3 H 1 1.595 0.050 . 1 . . . . . . . . 5480 1 892 . 1 1 72 72 MET C C 13 178.200 0.10 . 1 . . . . . . . . 5480 1 893 . 1 1 73 73 ALA N N 15 119.750 0.10 . 1 . . . . . . . . 5480 1 894 . 1 1 73 73 ALA H H 1 8.089 0.050 . 1 . . . . . . . . 5480 1 895 . 1 1 73 73 ALA CA C 13 54.300 0.10 . 1 . . . . . . . . 5480 1 896 . 1 1 73 73 ALA HA H 1 3.920 0.050 . 1 . . . . . . . . 5480 1 897 . 1 1 73 73 ALA CB C 13 18.300 0.10 . 1 . . . . . . . . 5480 1 898 . 1 1 73 73 ALA HB1 H 1 1.310 0.050 . 1 . . . . . . . . 5480 1 899 . 1 1 73 73 ALA HB2 H 1 1.310 0.050 . 1 . . . . . . . . 5480 1 900 . 1 1 73 73 ALA HB3 H 1 1.310 0.050 . 1 . . . . . . . . 5480 1 901 . 1 1 73 73 ALA C C 13 179.600 0.10 . 1 . . . . . . . . 5480 1 902 . 1 1 74 74 ARG N N 15 115.620 0.10 . 1 . . . . . . . . 5480 1 903 . 1 1 74 74 ARG H H 1 7.148 0.050 . 1 . . . . . . . . 5480 1 904 . 1 1 74 74 ARG CA C 13 58.000 0.10 . 1 . . . . . . . . 5480 1 905 . 1 1 74 74 ARG HA H 1 4.030 0.050 . 1 . . . . . . . . 5480 1 906 . 1 1 74 74 ARG CB C 13 30.500 0.10 . 1 . . . . . . . . 5480 1 907 . 1 1 74 74 ARG HB3 H 1 1.770 0.050 . 1 . . . . . . . . 5480 1 908 . 1 1 74 74 ARG HB2 H 1 1.770 0.050 . 1 . . . . . . . . 5480 1 909 . 1 1 74 74 ARG CG C 13 27.280 0.10 . 1 . . . . . . . . 5480 1 910 . 1 1 74 74 ARG HG3 H 1 1.670 0.050 . 2 . . . . . . . . 5480 1 911 . 1 1 74 74 ARG HG2 H 1 1.570 0.050 . 2 . . . . . . . . 5480 1 912 . 1 1 74 74 ARG CD C 13 43.420 0.10 . 1 . . . . . . . . 5480 1 913 . 1 1 74 74 ARG HD3 H 1 3.030 0.050 . 1 . . . . . . . . 5480 1 914 . 1 1 74 74 ARG HD2 H 1 3.030 0.050 . 1 . . . . . . . . 5480 1 915 . 1 1 74 74 ARG C C 13 178.200 0.10 . 1 . . . . . . . . 5480 1 916 . 1 1 75 75 LYS N N 15 117.410 0.10 . 1 . . . . . . . . 5480 1 917 . 1 1 75 75 LYS H H 1 7.876 0.050 . 1 . . . . . . . . 5480 1 918 . 1 1 75 75 LYS CA C 13 56.410 0.10 . 1 . . . . . . . . 5480 1 919 . 1 1 75 75 LYS HA H 1 4.180 0.050 . 1 . . . . . . . . 5480 1 920 . 1 1 75 75 LYS CB C 13 32.300 0.10 . 1 . . . . . . . . 5480 1 921 . 1 1 75 75 LYS HB3 H 1 1.621 0.050 . 2 . . . . . . . . 5480 1 922 . 1 1 75 75 LYS HB2 H 1 1.762 0.050 . 2 . . . . . . . . 5480 1 923 . 1 1 75 75 LYS CG C 13 24.800 0.10 . 1 . . . . . . . . 5480 1 924 . 1 1 75 75 LYS HG3 H 1 1.246 0.050 . 2 . . . . . . . . 5480 1 925 . 1 1 75 75 LYS HG2 H 1 1.320 0.050 . 2 . . . . . . . . 5480 1 926 . 1 1 75 75 LYS CD C 13 28.000 0.10 . 1 . . . . . . . . 5480 1 927 . 1 1 75 75 LYS HD3 H 1 1.526 0.050 . 2 . . . . . . . . 5480 1 928 . 1 1 75 75 LYS HD2 H 1 1.425 0.050 . 2 . . . . . . . . 5480 1 929 . 1 1 75 75 LYS CE C 13 41.670 0.10 . 1 . . . . . . . . 5480 1 930 . 1 1 75 75 LYS HE3 H 1 2.610 0.050 . 2 . . . . . . . . 5480 1 931 . 1 1 75 75 LYS HE2 H 1 2.674 0.050 . 2 . . . . . . . . 5480 1 932 . 1 1 75 75 LYS C C 13 177.500 0.10 . 1 . . . . . . . . 5480 1 933 . 1 1 76 76 MET N N 15 117.910 0.10 . 1 . . . . . . . . 5480 1 934 . 1 1 76 76 MET H H 1 7.965 0.050 . 1 . . . . . . . . 5480 1 935 . 1 1 76 76 MET CA C 13 56.408 0.10 . 1 . . . . . . . . 5480 1 936 . 1 1 76 76 MET HA H 1 4.302 0.050 . 1 . . . . . . . . 5480 1 937 . 1 1 76 76 MET CB C 13 32.600 0.10 . 1 . . . . . . . . 5480 1 938 . 1 1 76 76 MET HB3 H 1 2.110 0.050 . 2 . . . . . . . . 5480 1 939 . 1 1 76 76 MET HB2 H 1 2.040 0.050 . 2 . . . . . . . . 5480 1 940 . 1 1 76 76 MET CG C 13 32.250 0.10 . 1 . . . . . . . . 5480 1 941 . 1 1 76 76 MET HG3 H 1 2.570 0.050 . 1 . . . . . . . . 5480 1 942 . 1 1 76 76 MET HG2 H 1 2.570 0.050 . 1 . . . . . . . . 5480 1 943 . 1 1 76 76 MET CE C 13 17.330 0.10 . 1 . . . . . . . . 5480 1 944 . 1 1 76 76 MET HE1 H 1 2.034 0.050 . 1 . . . . . . . . 5480 1 945 . 1 1 76 76 MET HE2 H 1 2.034 0.050 . 1 . . . . . . . . 5480 1 946 . 1 1 76 76 MET HE3 H 1 2.034 0.050 . 1 . . . . . . . . 5480 1 947 . 1 1 76 76 MET C C 13 176.400 0.10 . 1 . . . . . . . . 5480 1 948 . 1 1 77 77 LYS N N 15 119.450 0.10 . 1 . . . . . . . . 5480 1 949 . 1 1 77 77 LYS H H 1 7.613 0.050 . 1 . . . . . . . . 5480 1 950 . 1 1 77 77 LYS CA C 13 56.201 0.10 . 1 . . . . . . . . 5480 1 951 . 1 1 77 77 LYS HA H 1 4.300 0.050 . 1 . . . . . . . . 5480 1 952 . 1 1 77 77 LYS CB C 13 33.120 0.10 . 1 . . . . . . . . 5480 1 953 . 1 1 77 77 LYS HB3 H 1 1.756 0.050 . 2 . . . . . . . . 5480 1 954 . 1 1 77 77 LYS HB2 H 1 1.836 0.050 . 2 . . . . . . . . 5480 1 955 . 1 1 77 77 LYS CG C 13 24.410 0.10 . 1 . . . . . . . . 5480 1 956 . 1 1 77 77 LYS HG3 H 1 1.407 0.050 . 1 . . . . . . . . 5480 1 957 . 1 1 77 77 LYS HG2 H 1 1.407 0.050 . 1 . . . . . . . . 5480 1 958 . 1 1 77 77 LYS CD C 13 28.800 0.10 . 1 . . . . . . . . 5480 1 959 . 1 1 77 77 LYS HD3 H 1 1.636 0.050 . 1 . . . . . . . . 5480 1 960 . 1 1 77 77 LYS HD2 H 1 1.636 0.050 . 1 . . . . . . . . 5480 1 961 . 1 1 77 77 LYS CE C 13 41.770 0.10 . 1 . . . . . . . . 5480 1 962 . 1 1 77 77 LYS HE3 H 1 2.952 0.050 . 1 . . . . . . . . 5480 1 963 . 1 1 77 77 LYS HE2 H 1 2.952 0.050 . 1 . . . . . . . . 5480 1 964 . 1 1 77 77 LYS C C 13 176.400 0.10 . 1 . . . . . . . . 5480 1 965 . 1 1 78 78 ASP N N 15 119.450 0.10 . 1 . . . . . . . . 5480 1 966 . 1 1 78 78 ASP H H 1 7.824 0.050 . 1 . . . . . . . . 5480 1 967 . 1 1 78 78 ASP CA C 13 54.400 0.10 . 1 . . . . . . . . 5480 1 968 . 1 1 78 78 ASP HA H 1 4.600 0.050 . 1 . . . . . . . . 5480 1 969 . 1 1 78 78 ASP CB C 13 41.370 0.10 . 1 . . . . . . . . 5480 1 970 . 1 1 78 78 ASP HB3 H 1 2.580 0.050 . 2 . . . . . . . . 5480 1 971 . 1 1 78 78 ASP HB2 H 1 2.737 0.050 . 2 . . . . . . . . 5480 1 972 . 1 1 78 78 ASP CG C 13 180.240 0.10 . 1 . . . . . . . . 5480 1 973 . 1 1 78 78 ASP C C 13 176.300 0.10 . 1 . . . . . . . . 5480 1 974 . 1 1 79 79 THR N N 15 113.151 0.10 . 1 . . . . . . . . 5480 1 975 . 1 1 79 79 THR H H 1 7.820 0.050 . 1 . . . . . . . . 5480 1 976 . 1 1 79 79 THR CA C 13 61.516 0.10 . 1 . . . . . . . . 5480 1 977 . 1 1 79 79 THR HA H 1 4.220 0.050 . 1 . . . . . . . . 5480 1 978 . 1 1 79 79 THR CB C 13 69.850 0.10 . 1 . . . . . . . . 5480 1 979 . 1 1 79 79 THR HB H 1 4.100 0.050 . 1 . . . . . . . . 5480 1 980 . 1 1 79 79 THR CG2 C 13 21.530 0.10 . 1 . . . . . . . . 5480 1 981 . 1 1 79 79 THR HG21 H 1 1.144 0.050 . 1 . . . . . . . . 5480 1 982 . 1 1 79 79 THR HG22 H 1 1.144 0.050 . 1 . . . . . . . . 5480 1 983 . 1 1 79 79 THR HG23 H 1 1.144 0.050 . 1 . . . . . . . . 5480 1 984 . 1 1 79 79 THR C C 13 174.000 0.10 . 1 . . . . . . . . 5480 1 985 . 1 1 80 80 ASP N N 15 122.700 0.10 . 1 . . . . . . . . 5480 1 986 . 1 1 80 80 ASP H H 1 8.283 0.050 . 1 . . . . . . . . 5480 1 987 . 1 1 80 80 ASP CA C 13 53.900 0.10 . 1 . . . . . . . . 5480 1 988 . 1 1 80 80 ASP HA H 1 4.700 0.050 . 1 . . . . . . . . 5480 1 989 . 1 1 80 80 ASP CB C 13 41.700 0.10 . 1 . . . . . . . . 5480 1 990 . 1 1 80 80 ASP HB3 H 1 2.570 0.050 . 2 . . . . . . . . 5480 1 991 . 1 1 80 80 ASP HB2 H 1 2.470 0.050 . 2 . . . . . . . . 5480 1 992 . 1 1 80 80 ASP CG C 13 179.900 0.10 . 1 . . . . . . . . 5480 1 993 . 1 1 80 80 ASP C C 13 175.800 0.10 . 1 . . . . . . . . 5480 1 994 . 1 1 81 81 SER N N 15 116.820 0.10 . 1 . . . . . . . . 5480 1 995 . 1 1 81 81 SER H H 1 8.320 0.050 . 1 . . . . . . . . 5480 1 996 . 1 1 81 81 SER CA C 13 57.280 0.10 . 1 . . . . . . . . 5480 1 997 . 1 1 81 81 SER HA H 1 4.500 0.050 . 1 . . . . . . . . 5480 1 998 . 1 1 81 81 SER CB C 13 64.700 0.10 . 1 . . . . . . . . 5480 1 999 . 1 1 81 81 SER HB3 H 1 3.930 0.050 . 2 . . . . . . . . 5480 1 1000 . 1 1 81 81 SER HB2 H 1 4.110 0.050 . 2 . . . . . . . . 5480 1 1001 . 1 1 81 81 SER C C 13 175.100 0.10 . 1 . . . . . . . . 5480 1 1002 . 1 1 82 82 GLU N N 15 122.840 0.10 . 1 . . . . . . . . 5480 1 1003 . 1 1 82 82 GLU H H 1 8.730 0.050 . 1 . . . . . . . . 5480 1 1004 . 1 1 82 82 GLU CA C 13 59.800 0.10 . 1 . . . . . . . . 5480 1 1005 . 1 1 82 82 GLU HA H 1 3.910 0.050 . 1 . . . . . . . . 5480 1 1006 . 1 1 82 82 GLU CB C 13 29.300 0.10 . 1 . . . . . . . . 5480 1 1007 . 1 1 82 82 GLU HB3 H 1 2.030 0.050 . 1 . . . . . . . . 5480 1 1008 . 1 1 82 82 GLU HB2 H 1 2.030 0.050 . 1 . . . . . . . . 5480 1 1009 . 1 1 82 82 GLU CG C 13 36.780 0.10 . 1 . . . . . . . . 5480 1 1010 . 1 1 82 82 GLU HG3 H 1 2.216 0.050 . 1 . . . . . . . . 5480 1 1011 . 1 1 82 82 GLU HG2 H 1 2.216 0.050 . 1 . . . . . . . . 5480 1 1012 . 1 1 82 82 GLU C C 13 178.180 0.10 . 1 . . . . . . . . 5480 1 1013 . 1 1 83 83 GLU N N 15 117.540 0.10 . 1 . . . . . . . . 5480 1 1014 . 1 1 83 83 GLU H H 1 8.410 0.050 . 1 . . . . . . . . 5480 1 1015 . 1 1 83 83 GLU CA C 13 59.740 0.10 . 1 . . . . . . . . 5480 1 1016 . 1 1 83 83 GLU HA H 1 3.994 0.050 . 1 . . . . . . . . 5480 1 1017 . 1 1 83 83 GLU CB C 13 29.200 0.10 . 1 . . . . . . . . 5480 1 1018 . 1 1 83 83 GLU HB3 H 1 2.175 0.050 . 2 . . . . . . . . 5480 1 1019 . 1 1 83 83 GLU HB2 H 1 1.970 0.050 . 2 . . . . . . . . 5480 1 1020 . 1 1 83 83 GLU CG C 13 36.800 0.10 . 1 . . . . . . . . 5480 1 1021 . 1 1 83 83 GLU HG3 H 1 2.257 0.050 . 1 . . . . . . . . 5480 1 1022 . 1 1 83 83 GLU HG2 H 1 2.257 0.050 . 1 . . . . . . . . 5480 1 1023 . 1 1 83 83 GLU C C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 1024 . 1 1 84 84 GLU N N 15 118.200 0.10 . 1 . . . . . . . . 5480 1 1025 . 1 1 84 84 GLU H H 1 7.660 0.050 . 1 . . . . . . . . 5480 1 1026 . 1 1 84 84 GLU CA C 13 59.100 0.10 . 1 . . . . . . . . 5480 1 1027 . 1 1 84 84 GLU HA H 1 3.950 0.050 . 1 . . . . . . . . 5480 1 1028 . 1 1 84 84 GLU CB C 13 29.530 0.10 . 1 . . . . . . . . 5480 1 1029 . 1 1 84 84 GLU HB3 H 1 2.217 0.050 . 2 . . . . . . . . 5480 1 1030 . 1 1 84 84 GLU HB2 H 1 2.020 0.050 . 2 . . . . . . . . 5480 1 1031 . 1 1 84 84 GLU CG C 13 35.600 0.10 . 1 . . . . . . . . 5480 1 1032 . 1 1 84 84 GLU HG3 H 1 2.200 0.050 . 1 . . . . . . . . 5480 1 1033 . 1 1 84 84 GLU HG2 H 1 2.200 0.050 . 1 . . . . . . . . 5480 1 1034 . 1 1 84 84 GLU C C 13 179.600 0.10 . 1 . . . . . . . . 5480 1 1035 . 1 1 85 85 ILE N N 15 121.000 0.10 . 1 . . . . . . . . 5480 1 1036 . 1 1 85 85 ILE H H 1 8.076 0.050 . 1 . . . . . . . . 5480 1 1037 . 1 1 85 85 ILE CA C 13 65.900 0.10 . 1 . . . . . . . . 5480 1 1038 . 1 1 85 85 ILE HA H 1 3.800 0.050 . 1 . . . . . . . . 5480 1 1039 . 1 1 85 85 ILE CB C 13 37.510 0.10 . 1 . . . . . . . . 5480 1 1040 . 1 1 85 85 ILE HB H 1 2.099 0.050 . 1 . . . . . . . . 5480 1 1041 . 1 1 85 85 ILE CG1 C 13 29.370 0.10 . 2 . . . . . . . . 5480 1 1042 . 1 1 85 85 ILE HG13 H 1 1.821 0.050 . 1 . . . . . . . . 5480 1 1043 . 1 1 85 85 ILE HG12 H 1 0.875 0.050 . 1 . . . . . . . . 5480 1 1044 . 1 1 85 85 ILE CD1 C 13 13.350 0.10 . 1 . . . . . . . . 5480 1 1045 . 1 1 85 85 ILE HD11 H 1 0.691 0.050 . 1 . . . . . . . . 5480 1 1046 . 1 1 85 85 ILE HD12 H 1 0.691 0.050 . 1 . . . . . . . . 5480 1 1047 . 1 1 85 85 ILE HD13 H 1 0.691 0.050 . 1 . . . . . . . . 5480 1 1048 . 1 1 85 85 ILE CG2 C 13 19.110 0.10 . 1 . . . . . . . . 5480 1 1049 . 1 1 85 85 ILE HG21 H 1 1.077 0.050 . 1 . . . . . . . . 5480 1 1050 . 1 1 85 85 ILE HG22 H 1 1.077 0.050 . 1 . . . . . . . . 5480 1 1051 . 1 1 85 85 ILE HG23 H 1 1.077 0.050 . 1 . . . . . . . . 5480 1 1052 . 1 1 85 85 ILE C C 13 178.200 0.10 . 1 . . . . . . . . 5480 1 1053 . 1 1 86 86 ARG N N 15 120.530 0.10 . 1 . . . . . . . . 5480 1 1054 . 1 1 86 86 ARG H H 1 8.444 0.050 . 1 . . . . . . . . 5480 1 1055 . 1 1 86 86 ARG CA C 13 59.940 0.10 . 1 . . . . . . . . 5480 1 1056 . 1 1 86 86 ARG HA H 1 4.111 0.050 . 1 . . . . . . . . 5480 1 1057 . 1 1 86 86 ARG CB C 13 29.670 0.10 . 1 . . . . . . . . 5480 1 1058 . 1 1 86 86 ARG HB3 H 1 1.861 0.050 . 2 . . . . . . . . 5480 1 1059 . 1 1 86 86 ARG HB2 H 1 2.012 0.050 . 2 . . . . . . . . 5480 1 1060 . 1 1 86 86 ARG CG C 13 27.300 0.10 . 1 . . . . . . . . 5480 1 1061 . 1 1 86 86 ARG HG3 H 1 1.610 0.050 . 2 . . . . . . . . 5480 1 1062 . 1 1 86 86 ARG HG2 H 1 1.500 0.050 . 2 . . . . . . . . 5480 1 1063 . 1 1 86 86 ARG CD C 13 43.000 0.10 . 1 . . . . . . . . 5480 1 1064 . 1 1 86 86 ARG HD3 H 1 2.924 0.050 . 1 . . . . . . . . 5480 1 1065 . 1 1 86 86 ARG HD2 H 1 2.924 0.050 . 1 . . . . . . . . 5480 1 1066 . 1 1 86 86 ARG C C 13 179.200 0.10 . 1 . . . . . . . . 5480 1 1067 . 1 1 87 87 GLU N N 15 116.520 0.10 . 1 . . . . . . . . 5480 1 1068 . 1 1 87 87 GLU H H 1 8.028 0.050 . 1 . . . . . . . . 5480 1 1069 . 1 1 87 87 GLU CA C 13 58.727 0.10 . 1 . . . . . . . . 5480 1 1070 . 1 1 87 87 GLU HA H 1 4.114 0.050 . 1 . . . . . . . . 5480 1 1071 . 1 1 87 87 GLU CB C 13 29.160 0.10 . 1 . . . . . . . . 5480 1 1072 . 1 1 87 87 GLU HB3 H 1 2.103 0.050 . 2 . . . . . . . . 5480 1 1073 . 1 1 87 87 GLU HB2 H 1 2.212 0.050 . 2 . . . . . . . . 5480 1 1074 . 1 1 87 87 GLU CG C 13 35.880 0.10 . 1 . . . . . . . . 5480 1 1075 . 1 1 87 87 GLU HG3 H 1 2.253 0.050 . 2 . . . . . . . . 5480 1 1076 . 1 1 87 87 GLU HG2 H 1 2.390 0.050 . 2 . . . . . . . . 5480 1 1077 . 1 1 87 87 GLU C C 13 179.300 0.10 . 1 . . . . . . . . 5480 1 1078 . 1 1 88 88 ALA N N 15 121.100 0.10 . 1 . . . . . . . . 5480 1 1079 . 1 1 88 88 ALA H H 1 8.101 0.050 . 1 . . . . . . . . 5480 1 1080 . 1 1 88 88 ALA CA C 13 55.490 0.10 . 1 . . . . . . . . 5480 1 1081 . 1 1 88 88 ALA HA H 1 4.152 0.050 . 1 . . . . . . . . 5480 1 1082 . 1 1 88 88 ALA CB C 13 17.560 0.10 . 1 . . . . . . . . 5480 1 1083 . 1 1 88 88 ALA HB1 H 1 1.840 0.050 . 1 . . . . . . . . 5480 1 1084 . 1 1 88 88 ALA HB2 H 1 1.840 0.050 . 1 . . . . . . . . 5480 1 1085 . 1 1 88 88 ALA HB3 H 1 1.840 0.050 . 1 . . . . . . . . 5480 1 1086 . 1 1 88 88 ALA C C 13 178.800 0.10 . 1 . . . . . . . . 5480 1 1087 . 1 1 89 89 PHE N N 15 118.067 0.10 . 1 . . . . . . . . 5480 1 1088 . 1 1 89 89 PHE H H 1 8.515 0.050 . 1 . . . . . . . . 5480 1 1089 . 1 1 89 89 PHE CA C 13 62.300 0.10 . 1 . . . . . . . . 5480 1 1090 . 1 1 89 89 PHE HA H 1 3.149 0.050 . 1 . . . . . . . . 5480 1 1091 . 1 1 89 89 PHE CB C 13 39.270 0.10 . 1 . . . . . . . . 5480 1 1092 . 1 1 89 89 PHE HB3 H 1 3.241 0.050 . 2 . . . . . . . . 5480 1 1093 . 1 1 89 89 PHE HB2 H 1 2.841 0.050 . 2 . . . . . . . . 5480 1 1094 . 1 1 89 89 PHE CD1 C 13 131.640 0.10 . 1 . . . . . . . . 5480 1 1095 . 1 1 89 89 PHE HD1 H 1 6.554 0.050 . 1 . . . . . . . . 5480 1 1096 . 1 1 89 89 PHE HE1 H 1 6.720 0.050 . 1 . . . . . . . . 5480 1 1097 . 1 1 89 89 PHE HE2 H 1 6.720 0.050 . 1 . . . . . . . . 5480 1 1098 . 1 1 89 89 PHE CD2 C 13 131.640 0.10 . 1 . . . . . . . . 5480 1 1099 . 1 1 89 89 PHE HD2 H 1 6.554 0.050 . 1 . . . . . . . . 5480 1 1100 . 1 1 89 89 PHE C C 13 177.200 0.10 . 1 . . . . . . . . 5480 1 1101 . 1 1 90 90 ARG N N 15 114.880 0.10 . 1 . . . . . . . . 5480 1 1102 . 1 1 90 90 ARG H H 1 7.699 0.050 . 1 . . . . . . . . 5480 1 1103 . 1 1 90 90 ARG CA C 13 58.600 0.10 . 1 . . . . . . . . 5480 1 1104 . 1 1 90 90 ARG HA H 1 3.790 0.050 . 1 . . . . . . . . 5480 1 1105 . 1 1 90 90 ARG CB C 13 30.411 0.10 . 1 . . . . . . . . 5480 1 1106 . 1 1 90 90 ARG HB3 H 1 1.913 0.050 . 1 . . . . . . . . 5480 1 1107 . 1 1 90 90 ARG HB2 H 1 1.913 0.050 . 1 . . . . . . . . 5480 1 1108 . 1 1 90 90 ARG CG C 13 27.840 0.10 . 1 . . . . . . . . 5480 1 1109 . 1 1 90 90 ARG HG3 H 1 1.706 0.050 . 2 . . . . . . . . 5480 1 1110 . 1 1 90 90 ARG HG2 H 1 1.936 0.050 . 2 . . . . . . . . 5480 1 1111 . 1 1 90 90 ARG CD C 13 43.480 0.10 . 1 . . . . . . . . 5480 1 1112 . 1 1 90 90 ARG HD3 H 1 3.146 0.050 . 1 . . . . . . . . 5480 1 1113 . 1 1 90 90 ARG HD2 H 1 3.146 0.050 . 1 . . . . . . . . 5480 1 1114 . 1 1 90 90 ARG C C 13 177.500 0.10 . 1 . . . . . . . . 5480 1 1115 . 1 1 91 91 VAL N N 15 117.490 0.10 . 1 . . . . . . . . 5480 1 1116 . 1 1 91 91 VAL H H 1 7.247 0.050 . 1 . . . . . . . . 5480 1 1117 . 1 1 91 91 VAL CA C 13 65.680 0.10 . 1 . . . . . . . . 5480 1 1118 . 1 1 91 91 VAL HA H 1 3.370 0.050 . 1 . . . . . . . . 5480 1 1119 . 1 1 91 91 VAL CB C 13 31.060 0.10 . 1 . . . . . . . . 5480 1 1120 . 1 1 91 91 VAL HB H 1 2.000 0.050 . 1 . . . . . . . . 5480 1 1121 . 1 1 91 91 VAL CG2 C 13 22.940 0.10 . 1 . . . . . . . . 5480 1 1122 . 1 1 91 91 VAL HG21 H 1 0.946 0.050 . 2 . . . . . . . . 5480 1 1123 . 1 1 91 91 VAL HG22 H 1 0.946 0.050 . 2 . . . . . . . . 5480 1 1124 . 1 1 91 91 VAL HG23 H 1 0.946 0.050 . 2 . . . . . . . . 5480 1 1125 . 1 1 91 91 VAL CG1 C 13 20.840 0.10 . 1 . . . . . . . . 5480 1 1126 . 1 1 91 91 VAL HG11 H 1 0.412 0.050 . 2 . . . . . . . . 5480 1 1127 . 1 1 91 91 VAL HG12 H 1 0.412 0.050 . 2 . . . . . . . . 5480 1 1128 . 1 1 91 91 VAL HG13 H 1 0.412 0.050 . 2 . . . . . . . . 5480 1 1129 . 1 1 91 91 VAL C C 13 176.200 0.10 . 1 . . . . . . . . 5480 1 1130 . 1 1 92 92 PHE N N 15 113.010 0.10 . 1 . . . . . . . . 5480 1 1131 . 1 1 92 92 PHE H H 1 6.780 0.050 . 1 . . . . . . . . 5480 1 1132 . 1 1 92 92 PHE CA C 13 59.980 0.10 . 1 . . . . . . . . 5480 1 1133 . 1 1 92 92 PHE HA H 1 4.142 0.050 . 1 . . . . . . . . 5480 1 1134 . 1 1 92 92 PHE CB C 13 41.560 0.10 . 1 . . . . . . . . 5480 1 1135 . 1 1 92 92 PHE HB3 H 1 2.824 0.050 . 2 . . . . . . . . 5480 1 1136 . 1 1 92 92 PHE HB2 H 1 2.604 0.050 . 2 . . . . . . . . 5480 1 1137 . 1 1 92 92 PHE CD1 C 13 130.440 0.10 . 1 . . . . . . . . 5480 1 1138 . 1 1 92 92 PHE HD1 H 1 7.224 0.050 . 1 . . . . . . . . 5480 1 1139 . 1 1 92 92 PHE CE1 C 13 132.740 0.10 . 1 . . . . . . . . 5480 1 1140 . 1 1 92 92 PHE HE1 H 1 7.385 0.050 . 1 . . . . . . . . 5480 1 1141 . 1 1 92 92 PHE CZ C 13 128.750 0.10 . 1 . . . . . . . . 5480 1 1142 . 1 1 92 92 PHE HZ H 1 7.194 0.050 . 1 . . . . . . . . 5480 1 1143 . 1 1 92 92 PHE CE2 C 13 132.740 0.10 . 1 . . . . . . . . 5480 1 1144 . 1 1 92 92 PHE HE2 H 1 7.385 0.050 . 1 . . . . . . . . 5480 1 1145 . 1 1 92 92 PHE CD2 C 13 130.440 0.10 . 1 . . . . . . . . 5480 1 1146 . 1 1 92 92 PHE HD2 H 1 7.224 0.050 . 1 . . . . . . . . 5480 1 1147 . 1 1 92 92 PHE C C 13 176.600 0.10 . 1 . . . . . . . . 5480 1 1148 . 1 1 93 93 ASP N N 15 115.980 0.10 . 1 . . . . . . . . 5480 1 1149 . 1 1 93 93 ASP H H 1 7.745 0.050 . 1 . . . . . . . . 5480 1 1150 . 1 1 93 93 ASP CA C 13 52.240 0.10 . 1 . . . . . . . . 5480 1 1151 . 1 1 93 93 ASP HA H 1 4.570 0.050 . 1 . . . . . . . . 5480 1 1152 . 1 1 93 93 ASP CB C 13 38.700 0.10 . 1 . . . . . . . . 5480 1 1153 . 1 1 93 93 ASP HB3 H 1 1.335 0.050 . 2 . . . . . . . . 5480 1 1154 . 1 1 93 93 ASP HB2 H 1 2.199 0.050 . 2 . . . . . . . . 5480 1 1155 . 1 1 93 93 ASP CG C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 1156 . 1 1 93 93 ASP C C 13 177.600 0.10 . 1 . . . . . . . . 5480 1 1157 . 1 1 94 94 LYS N N 15 125.320 0.10 . 1 . . . . . . . . 5480 1 1158 . 1 1 94 94 LYS H H 1 7.629 0.050 . 1 . . . . . . . . 5480 1 1159 . 1 1 94 94 LYS CA C 13 58.500 0.10 . 1 . . . . . . . . 5480 1 1160 . 1 1 94 94 LYS HA H 1 3.860 0.050 . 1 . . . . . . . . 5480 1 1161 . 1 1 94 94 LYS CB C 13 32.340 0.10 . 1 . . . . . . . . 5480 1 1162 . 1 1 94 94 LYS HB3 H 1 1.790 0.050 . 1 . . . . . . . . 5480 1 1163 . 1 1 94 94 LYS HB2 H 1 1.790 0.050 . 1 . . . . . . . . 5480 1 1164 . 1 1 94 94 LYS CG C 13 23.840 0.10 . 1 . . . . . . . . 5480 1 1165 . 1 1 94 94 LYS HG3 H 1 1.408 0.050 . 1 . . . . . . . . 5480 1 1166 . 1 1 94 94 LYS HG2 H 1 1.408 0.050 . 1 . . . . . . . . 5480 1 1167 . 1 1 94 94 LYS CD C 13 27.940 0.10 . 1 . . . . . . . . 5480 1 1168 . 1 1 94 94 LYS HD3 H 1 1.529 0.050 . 1 . . . . . . . . 5480 1 1169 . 1 1 94 94 LYS HD2 H 1 1.529 0.050 . 1 . . . . . . . . 5480 1 1170 . 1 1 94 94 LYS CE C 13 41.420 0.10 . 1 . . . . . . . . 5480 1 1171 . 1 1 94 94 LYS HE3 H 1 2.704 0.050 . 2 . . . . . . . . 5480 1 1172 . 1 1 94 94 LYS HE2 H 1 2.795 0.050 . 2 . . . . . . . . 5480 1 1173 . 1 1 94 94 LYS C C 13 178.300 0.10 . 1 . . . . . . . . 5480 1 1174 . 1 1 95 95 ASP N N 15 113.811 0.10 . 1 . . . . . . . . 5480 1 1175 . 1 1 95 95 ASP H H 1 8.182 0.050 . 1 . . . . . . . . 5480 1 1176 . 1 1 95 95 ASP CA C 13 52.910 0.10 . 1 . . . . . . . . 5480 1 1177 . 1 1 95 95 ASP HA H 1 4.500 0.050 . 1 . . . . . . . . 5480 1 1178 . 1 1 95 95 ASP CB C 13 39.547 0.10 . 1 . . . . . . . . 5480 1 1179 . 1 1 95 95 ASP HB3 H 1 2.600 0.050 . 2 . . . . . . . . 5480 1 1180 . 1 1 95 95 ASP HB2 H 1 3.021 0.050 . 2 . . . . . . . . 5480 1 1181 . 1 1 95 95 ASP CG C 13 180.900 0.10 . 1 . . . . . . . . 5480 1 1182 . 1 1 95 95 ASP C C 13 177.800 0.10 . 1 . . . . . . . . 5480 1 1183 . 1 1 96 96 GLY N N 15 108.700 0.10 . 1 . . . . . . . . 5480 1 1184 . 1 1 96 96 GLY H H 1 7.690 0.050 . 1 . . . . . . . . 5480 1 1185 . 1 1 96 96 GLY CA C 13 46.900 0.10 . 1 . . . . . . . . 5480 1 1186 . 1 1 96 96 GLY HA3 H 1 3.800 0.050 . 1 . . . . . . . . 5480 1 1187 . 1 1 96 96 GLY HA2 H 1 3.800 0.050 . 1 . . . . . . . . 5480 1 1188 . 1 1 96 96 GLY C C 13 175.200 0.10 . 1 . . . . . . . . 5480 1 1189 . 1 1 97 97 ASN N N 15 119.220 0.10 . 1 . . . . . . . . 5480 1 1190 . 1 1 97 97 ASN H H 1 8.314 0.050 . 1 . . . . . . . . 5480 1 1191 . 1 1 97 97 ASN CA C 13 52.480 0.10 . 1 . . . . . . . . 5480 1 1192 . 1 1 97 97 ASN HA H 1 4.610 0.050 . 1 . . . . . . . . 5480 1 1193 . 1 1 97 97 ASN CB C 13 38.140 0.10 . 1 . . . . . . . . 5480 1 1194 . 1 1 97 97 ASN HB3 H 1 2.610 0.050 . 2 . . . . . . . . 5480 1 1195 . 1 1 97 97 ASN HB2 H 1 3.360 0.050 . 2 . . . . . . . . 5480 1 1196 . 1 1 97 97 ASN CG C 13 179.900 0.10 . 1 . . . . . . . . 5480 1 1197 . 1 1 97 97 ASN ND2 N 15 116.370 0.10 . 1 . . . . . . . . 5480 1 1198 . 1 1 97 97 ASN HD21 H 1 7.965 0.050 . 2 . . . . . . . . 5480 1 1199 . 1 1 97 97 ASN HD22 H 1 7.321 0.050 . 2 . . . . . . . . 5480 1 1200 . 1 1 97 97 ASN C C 13 176.300 0.10 . 1 . . . . . . . . 5480 1 1201 . 1 1 98 98 GLY N N 15 112.110 0.10 . 1 . . . . . . . . 5480 1 1202 . 1 1 98 98 GLY H H 1 10.489 0.050 . 1 . . . . . . . . 5480 1 1203 . 1 1 98 98 GLY CA C 13 45.000 0.10 . 1 . . . . . . . . 5480 1 1204 . 1 1 98 98 GLY HA3 H 1 3.440 0.050 . 2 . . . . . . . . 5480 1 1205 . 1 1 98 98 GLY HA2 H 1 4.070 0.050 . 2 . . . . . . . . 5480 1 1206 . 1 1 98 98 GLY C C 13 173.000 0.10 . 1 . . . . . . . . 5480 1 1207 . 1 1 99 99 TYR N N 15 116.020 0.10 . 1 . . . . . . . . 5480 1 1208 . 1 1 99 99 TYR H H 1 7.661 0.050 . 1 . . . . . . . . 5480 1 1209 . 1 1 99 99 TYR CA C 13 56.290 0.10 . 1 . . . . . . . . 5480 1 1210 . 1 1 99 99 TYR HA H 1 5.024 0.050 . 1 . . . . . . . . 5480 1 1211 . 1 1 99 99 TYR CB C 13 42.590 0.10 . 1 . . . . . . . . 5480 1 1212 . 1 1 99 99 TYR HB3 H 1 2.492 0.050 . 2 . . . . . . . . 5480 1 1213 . 1 1 99 99 TYR HB2 H 1 2.584 0.050 . 2 . . . . . . . . 5480 1 1214 . 1 1 99 99 TYR CD1 C 13 133.270 0.10 . 3 . . . . . . . . 5480 1 1215 . 1 1 99 99 TYR HD1 H 1 6.781 0.050 . 1 . . . . . . . . 5480 1 1216 . 1 1 99 99 TYR CE1 C 13 118.043 0.10 . 1 . . . . . . . . 5480 1 1217 . 1 1 99 99 TYR HE1 H 1 6.908 0.050 . 1 . . . . . . . . 5480 1 1218 . 1 1 99 99 TYR CE2 C 13 118.043 0.10 . 1 . . . . . . . . 5480 1 1219 . 1 1 99 99 TYR HE2 H 1 6.908 0.050 . 1 . . . . . . . . 5480 1 1220 . 1 1 99 99 TYR CD2 C 13 133.370 0.10 . 3 . . . . . . . . 5480 1 1221 . 1 1 99 99 TYR HD2 H 1 6.781 0.050 . 1 . . . . . . . . 5480 1 1222 . 1 1 99 99 TYR C C 13 175.000 0.10 . 1 . . . . . . . . 5480 1 1223 . 1 1 100 100 ILE N N 15 126.840 0.10 . 1 . . . . . . . . 5480 1 1224 . 1 1 100 100 ILE H H 1 10.022 0.050 . 1 . . . . . . . . 5480 1 1225 . 1 1 100 100 ILE CA C 13 61.100 0.10 . 1 . . . . . . . . 5480 1 1226 . 1 1 100 100 ILE HA H 1 4.600 0.050 . 1 . . . . . . . . 5480 1 1227 . 1 1 100 100 ILE CB C 13 39.270 0.10 . 1 . . . . . . . . 5480 1 1228 . 1 1 100 100 ILE HB H 1 1.804 0.050 . 1 . . . . . . . . 5480 1 1229 . 1 1 100 100 ILE CG1 C 13 26.670 0.10 . 2 . . . . . . . . 5480 1 1230 . 1 1 100 100 ILE HG13 H 1 0.190 0.050 . 1 . . . . . . . . 5480 1 1231 . 1 1 100 100 ILE HG12 H 1 1.240 0.050 . 1 . . . . . . . . 5480 1 1232 . 1 1 100 100 ILE CD1 C 13 16.660 0.10 . 1 . . . . . . . . 5480 1 1233 . 1 1 100 100 ILE HD11 H 1 0.440 0.050 . 1 . . . . . . . . 5480 1 1234 . 1 1 100 100 ILE HD12 H 1 0.440 0.050 . 1 . . . . . . . . 5480 1 1235 . 1 1 100 100 ILE HD13 H 1 0.440 0.050 . 1 . . . . . . . . 5480 1 1236 . 1 1 100 100 ILE CG2 C 13 17.220 0.10 . 1 . . . . . . . . 5480 1 1237 . 1 1 100 100 ILE HG21 H 1 0.847 0.050 . 1 . . . . . . . . 5480 1 1238 . 1 1 100 100 ILE HG22 H 1 0.847 0.050 . 1 . . . . . . . . 5480 1 1239 . 1 1 100 100 ILE HG23 H 1 0.847 0.050 . 1 . . . . . . . . 5480 1 1240 . 1 1 100 100 ILE C C 13 175.400 0.10 . 1 . . . . . . . . 5480 1 1241 . 1 1 101 101 SER N N 15 123.520 0.10 . 1 . . . . . . . . 5480 1 1242 . 1 1 101 101 SER H H 1 8.930 0.050 . 1 . . . . . . . . 5480 1 1243 . 1 1 101 101 SER CA C 13 55.500 0.10 . 1 . . . . . . . . 5480 1 1244 . 1 1 101 101 SER HA H 1 4.830 0.050 . 1 . . . . . . . . 5480 1 1245 . 1 1 101 101 SER CB C 13 66.700 0.10 . 1 . . . . . . . . 5480 1 1246 . 1 1 101 101 SER HB3 H 1 3.860 0.050 . 2 . . . . . . . . 5480 1 1247 . 1 1 101 101 SER HB2 H 1 4.390 0.050 . 2 . . . . . . . . 5480 1 1248 . 1 1 101 101 SER C C 13 175.300 0.10 . 1 . . . . . . . . 5480 1 1249 . 1 1 102 102 ALA N N 15 122.780 0.10 . 1 . . . . . . . . 5480 1 1250 . 1 1 102 102 ALA H H 1 9.267 0.050 . 1 . . . . . . . . 5480 1 1251 . 1 1 102 102 ALA CA C 13 55.700 0.10 . 1 . . . . . . . . 5480 1 1252 . 1 1 102 102 ALA HA H 1 3.797 0.050 . 1 . . . . . . . . 5480 1 1253 . 1 1 102 102 ALA CB C 13 17.830 0.10 . 1 . . . . . . . . 5480 1 1254 . 1 1 102 102 ALA HB1 H 1 1.430 0.050 . 1 . . . . . . . . 5480 1 1255 . 1 1 102 102 ALA HB2 H 1 1.430 0.050 . 1 . . . . . . . . 5480 1 1256 . 1 1 102 102 ALA HB3 H 1 1.430 0.050 . 1 . . . . . . . . 5480 1 1257 . 1 1 102 102 ALA C C 13 179.400 0.10 . 1 . . . . . . . . 5480 1 1258 . 1 1 103 103 ALA N N 15 117.950 0.10 . 1 . . . . . . . . 5480 1 1259 . 1 1 103 103 ALA H H 1 8.126 0.050 . 1 . . . . . . . . 5480 1 1260 . 1 1 103 103 ALA CA C 13 55.050 0.10 . 1 . . . . . . . . 5480 1 1261 . 1 1 103 103 ALA HA H 1 3.960 0.050 . 1 . . . . . . . . 5480 1 1262 . 1 1 103 103 ALA CB C 13 18.200 0.10 . 1 . . . . . . . . 5480 1 1263 . 1 1 103 103 ALA HB1 H 1 1.350 0.050 . 1 . . . . . . . . 5480 1 1264 . 1 1 103 103 ALA HB2 H 1 1.350 0.050 . 1 . . . . . . . . 5480 1 1265 . 1 1 103 103 ALA HB3 H 1 1.350 0.050 . 1 . . . . . . . . 5480 1 1266 . 1 1 103 103 ALA C C 13 181.400 0.10 . 1 . . . . . . . . 5480 1 1267 . 1 1 104 104 GLU N N 15 119.990 0.10 . 1 . . . . . . . . 5480 1 1268 . 1 1 104 104 GLU H H 1 7.831 0.050 . 1 . . . . . . . . 5480 1 1269 . 1 1 104 104 GLU CA C 13 59.040 0.10 . 1 . . . . . . . . 5480 1 1270 . 1 1 104 104 GLU HA H 1 3.900 0.050 . 1 . . . . . . . . 5480 1 1271 . 1 1 104 104 GLU CB C 13 29.540 0.10 . 1 . . . . . . . . 5480 1 1272 . 1 1 104 104 GLU HB3 H 1 2.100 0.050 . 2 . . . . . . . . 5480 1 1273 . 1 1 104 104 GLU CG C 13 37.520 0.10 . 1 . . . . . . . . 5480 1 1274 . 1 1 104 104 GLU HG3 H 1 2.214 0.050 . 2 . . . . . . . . 5480 1 1275 . 1 1 104 104 GLU HG2 H 1 2.256 0.050 . 2 . . . . . . . . 5480 1 1276 . 1 1 104 104 GLU C C 13 179.500 0.10 . 1 . . . . . . . . 5480 1 1277 . 1 1 105 105 LEU N N 15 120.480 0.10 . 1 . . . . . . . . 5480 1 1278 . 1 1 105 105 LEU H H 1 8.165 0.050 . 1 . . . . . . . . 5480 1 1279 . 1 1 105 105 LEU CA C 13 58.400 0.10 . 1 . . . . . . . . 5480 1 1280 . 1 1 105 105 LEU HA H 1 4.110 0.050 . 1 . . . . . . . . 5480 1 1281 . 1 1 105 105 LEU CB C 13 41.750 0.10 . 1 . . . . . . . . 5480 1 1282 . 1 1 105 105 LEU HB3 H 1 1.167 0.050 . 2 . . . . . . . . 5480 1 1283 . 1 1 105 105 LEU HB2 H 1 1.660 0.050 . 2 . . . . . . . . 5480 1 1284 . 1 1 105 105 LEU CG C 13 26.970 0.10 . 1 . . . . . . . . 5480 1 1285 . 1 1 105 105 LEU HG H 1 1.263 0.050 . 1 . . . . . . . . 5480 1 1286 . 1 1 105 105 LEU CD1 C 13 25.530 0.10 . 1 . . . . . . . . 5480 1 1287 . 1 1 105 105 LEU HD11 H 1 0.313 0.050 . 2 . . . . . . . . 5480 1 1288 . 1 1 105 105 LEU HD12 H 1 0.313 0.050 . 2 . . . . . . . . 5480 1 1289 . 1 1 105 105 LEU HD13 H 1 0.313 0.050 . 2 . . . . . . . . 5480 1 1290 . 1 1 105 105 LEU CD2 C 13 24.230 0.10 . 1 . . . . . . . . 5480 1 1291 . 1 1 105 105 LEU HD21 H 1 0.395 0.050 . 2 . . . . . . . . 5480 1 1292 . 1 1 105 105 LEU HD22 H 1 0.395 0.050 . 2 . . . . . . . . 5480 1 1293 . 1 1 105 105 LEU HD23 H 1 0.395 0.050 . 2 . . . . . . . . 5480 1 1294 . 1 1 105 105 LEU C C 13 178.500 0.10 . 1 . . . . . . . . 5480 1 1295 . 1 1 106 106 ARG N N 15 117.820 0.10 . 1 . . . . . . . . 5480 1 1296 . 1 1 106 106 ARG H H 1 8.779 0.050 . 1 . . . . . . . . 5480 1 1297 . 1 1 106 106 ARG CA C 13 59.900 0.10 . 1 . . . . . . . . 5480 1 1298 . 1 1 106 106 ARG HA H 1 3.630 0.050 . 1 . . . . . . . . 5480 1 1299 . 1 1 106 106 ARG CB C 13 30.240 0.10 . 1 . . . . . . . . 5480 1 1300 . 1 1 106 106 ARG HB3 H 1 1.930 0.050 . 1 . . . . . . . . 5480 1 1301 . 1 1 106 106 ARG HB2 H 1 1.930 0.050 . 1 . . . . . . . . 5480 1 1302 . 1 1 106 106 ARG CG C 13 27.770 0.10 . 1 . . . . . . . . 5480 1 1303 . 1 1 106 106 ARG HG3 H 1 1.531 0.050 . 2 . . . . . . . . 5480 1 1304 . 1 1 106 106 ARG HG2 H 1 1.579 0.050 . 2 . . . . . . . . 5480 1 1305 . 1 1 106 106 ARG CD C 13 43.470 0.10 . 1 . . . . . . . . 5480 1 1306 . 1 1 106 106 ARG HD3 H 1 3.128 0.050 . 2 . . . . . . . . 5480 1 1307 . 1 1 106 106 ARG HD2 H 1 3.202 0.050 . 2 . . . . . . . . 5480 1 1308 . 1 1 106 106 ARG C C 13 178.700 0.10 . 1 . . . . . . . . 5480 1 1309 . 1 1 107 107 HIS N N 15 119.680 0.10 . 1 . . . . . . . . 5480 1 1310 . 1 1 107 107 HIS H H 1 8.127 0.050 . 1 . . . . . . . . 5480 1 1311 . 1 1 107 107 HIS CA C 13 60.080 0.10 . 1 . . . . . . . . 5480 1 1312 . 1 1 107 107 HIS HA H 1 4.222 0.050 . 1 . . . . . . . . 5480 1 1313 . 1 1 107 107 HIS CB C 13 30.390 0.10 . 1 . . . . . . . . 5480 1 1314 . 1 1 107 107 HIS HB3 H 1 3.222 0.050 . 2 . . . . . . . . 5480 1 1315 . 1 1 107 107 HIS HB2 H 1 3.418 0.050 . 2 . . . . . . . . 5480 1 1316 . 1 1 107 107 HIS CE1 C 13 139.100 0.10 . 1 . . . . . . . . 5480 1 1317 . 1 1 107 107 HIS HE1 H 1 7.760 0.050 . 3 . . . . . . . . 5480 1 1318 . 1 1 107 107 HIS C C 13 177.300 0.10 . 1 . . . . . . . . 5480 1 1319 . 1 1 108 108 VAL N N 15 118.500 0.10 . 1 . . . . . . . . 5480 1 1320 . 1 1 108 108 VAL H H 1 7.817 0.050 . 1 . . . . . . . . 5480 1 1321 . 1 1 108 108 VAL CA C 13 66.853 0.10 . 1 . . . . . . . . 5480 1 1322 . 1 1 108 108 VAL HA H 1 3.550 0.050 . 1 . . . . . . . . 5480 1 1323 . 1 1 108 108 VAL CB C 13 32.100 0.10 . 1 . . . . . . . . 5480 1 1324 . 1 1 108 108 VAL HB H 1 2.120 0.050 . 1 . . . . . . . . 5480 1 1325 . 1 1 108 108 VAL CG2 C 13 20.603 0.10 . 1 . . . . . . . . 5480 1 1326 . 1 1 108 108 VAL HG21 H 1 0.663 0.050 . 2 . . . . . . . . 5480 1 1327 . 1 1 108 108 VAL HG22 H 1 0.663 0.050 . 2 . . . . . . . . 5480 1 1328 . 1 1 108 108 VAL HG23 H 1 0.663 0.050 . 2 . . . . . . . . 5480 1 1329 . 1 1 108 108 VAL CG1 C 13 23.310 0.10 . 1 . . . . . . . . 5480 1 1330 . 1 1 108 108 VAL HG11 H 1 1.040 0.050 . 2 . . . . . . . . 5480 1 1331 . 1 1 108 108 VAL HG12 H 1 1.040 0.050 . 2 . . . . . . . . 5480 1 1332 . 1 1 108 108 VAL HG13 H 1 1.040 0.050 . 2 . . . . . . . . 5480 1 1333 . 1 1 108 108 VAL C C 13 178.000 0.10 . 1 . . . . . . . . 5480 1 1334 . 1 1 109 109 MET N N 15 114.850 0.10 . 1 . . . . . . . . 5480 1 1335 . 1 1 109 109 MET H H 1 8.137 0.050 . 1 . . . . . . . . 5480 1 1336 . 1 1 109 109 MET CA C 13 57.520 0.10 . 1 . . . . . . . . 5480 1 1337 . 1 1 109 109 MET HA H 1 4.220 0.050 . 1 . . . . . . . . 5480 1 1338 . 1 1 109 109 MET CB C 13 30.275 0.10 . 1 . . . . . . . . 5480 1 1339 . 1 1 109 109 MET HB3 H 1 1.909 0.050 . 2 . . . . . . . . 5480 1 1340 . 1 1 109 109 MET HB2 H 1 2.070 0.050 . 2 . . . . . . . . 5480 1 1341 . 1 1 109 109 MET CG C 13 32.400 0.10 . 1 . . . . . . . . 5480 1 1342 . 1 1 109 109 MET HG3 H 1 2.430 0.050 . 2 . . . . . . . . 5480 1 1343 . 1 1 109 109 MET HG2 H 1 2.690 0.050 . 2 . . . . . . . . 5480 1 1344 . 1 1 109 109 MET CE C 13 16.630 0.10 . 1 . . . . . . . . 5480 1 1345 . 1 1 109 109 MET HE1 H 1 1.903 0.050 . 1 . . . . . . . . 5480 1 1346 . 1 1 109 109 MET HE2 H 1 1.903 0.050 . 1 . . . . . . . . 5480 1 1347 . 1 1 109 109 MET HE3 H 1 1.903 0.050 . 1 . . . . . . . . 5480 1 1348 . 1 1 109 109 MET C C 13 179.000 0.10 . 1 . . . . . . . . 5480 1 1349 . 1 1 110 110 THR N N 15 115.450 0.10 . 1 . . . . . . . . 5480 1 1350 . 1 1 110 110 THR H H 1 8.553 0.050 . 1 . . . . . . . . 5480 1 1351 . 1 1 110 110 THR CA C 13 66.320 0.10 . 1 . . . . . . . . 5480 1 1352 . 1 1 110 110 THR HA H 1 4.038 0.050 . 1 . . . . . . . . 5480 1 1353 . 1 1 110 110 THR CB C 13 68.520 0.10 . 1 . . . . . . . . 5480 1 1354 . 1 1 110 110 THR HB H 1 4.240 0.050 . 1 . . . . . . . . 5480 1 1355 . 1 1 110 110 THR CG2 C 13 21.340 0.10 . 1 . . . . . . . . 5480 1 1356 . 1 1 110 110 THR HG21 H 1 1.117 0.050 . 1 . . . . . . . . 5480 1 1357 . 1 1 110 110 THR HG22 H 1 1.117 0.050 . 1 . . . . . . . . 5480 1 1358 . 1 1 110 110 THR HG23 H 1 1.117 0.050 . 1 . . . . . . . . 5480 1 1359 . 1 1 110 110 THR C C 13 178.500 0.10 . 1 . . . . . . . . 5480 1 1360 . 1 1 111 111 ASN N N 15 123.010 0.10 . 1 . . . . . . . . 5480 1 1361 . 1 1 111 111 ASN H H 1 7.944 0.050 . 1 . . . . . . . . 5480 1 1362 . 1 1 111 111 ASN CA C 13 55.700 0.10 . 1 . . . . . . . . 5480 1 1363 . 1 1 111 111 ASN HA H 1 4.370 0.050 . 1 . . . . . . . . 5480 1 1364 . 1 1 111 111 ASN CB C 13 37.400 0.10 . 1 . . . . . . . . 5480 1 1365 . 1 1 111 111 ASN HB3 H 1 2.700 0.050 . 2 . . . . . . . . 5480 1 1366 . 1 1 111 111 ASN HB2 H 1 2.650 0.050 . 2 . . . . . . . . 5480 1 1367 . 1 1 111 111 ASN CG C 13 176.200 0.10 . 1 . . . . . . . . 5480 1 1368 . 1 1 111 111 ASN ND2 N 15 109.909 0.10 . 1 . . . . . . . . 5480 1 1369 . 1 1 111 111 ASN HD21 H 1 7.294 0.050 . 2 . . . . . . . . 5480 1 1370 . 1 1 111 111 ASN HD22 H 1 6.353 0.050 . 2 . . . . . . . . 5480 1 1371 . 1 1 111 111 ASN C C 13 177.200 0.10 . 1 . . . . . . . . 5480 1 1372 . 1 1 112 112 LEU N N 15 118.020 0.10 . 1 . . . . . . . . 5480 1 1373 . 1 1 112 112 LEU H H 1 7.707 0.050 . 1 . . . . . . . . 5480 1 1374 . 1 1 112 112 LEU CA C 13 55.700 0.10 . 1 . . . . . . . . 5480 1 1375 . 1 1 112 112 LEU HA H 1 4.137 0.050 . 1 . . . . . . . . 5480 1 1376 . 1 1 112 112 LEU CB C 13 42.660 0.10 . 1 . . . . . . . . 5480 1 1377 . 1 1 112 112 LEU HB3 H 1 1.600 0.050 . 2 . . . . . . . . 5480 1 1378 . 1 1 112 112 LEU HB2 H 1 1.895 0.050 . 2 . . . . . . . . 5480 1 1379 . 1 1 112 112 LEU CG C 13 26.570 0.10 . 1 . . . . . . . . 5480 1 1380 . 1 1 112 112 LEU HG H 1 1.288 0.050 . 1 . . . . . . . . 5480 1 1381 . 1 1 112 112 LEU CD1 C 13 23.930 0.10 . 1 . . . . . . . . 5480 1 1382 . 1 1 112 112 LEU HD11 H 1 0.746 0.050 . 2 . . . . . . . . 5480 1 1383 . 1 1 112 112 LEU HD12 H 1 0.746 0.050 . 2 . . . . . . . . 5480 1 1384 . 1 1 112 112 LEU HD13 H 1 0.746 0.050 . 2 . . . . . . . . 5480 1 1385 . 1 1 112 112 LEU CD2 C 13 26.100 0.10 . 1 . . . . . . . . 5480 1 1386 . 1 1 112 112 LEU HD21 H 1 0.785 0.050 . 2 . . . . . . . . 5480 1 1387 . 1 1 112 112 LEU HD22 H 1 0.785 0.050 . 2 . . . . . . . . 5480 1 1388 . 1 1 112 112 LEU HD23 H 1 0.785 0.050 . 2 . . . . . . . . 5480 1 1389 . 1 1 112 112 LEU C C 13 176.400 0.10 . 1 . . . . . . . . 5480 1 1390 . 1 1 113 113 GLY N N 15 104.580 0.10 . 1 . . . . . . . . 5480 1 1391 . 1 1 113 113 GLY H H 1 7.614 0.050 . 1 . . . . . . . . 5480 1 1392 . 1 1 113 113 GLY CA C 13 44.900 0.10 . 1 . . . . . . . . 5480 1 1393 . 1 1 113 113 GLY HA3 H 1 3.610 0.050 . 2 . . . . . . . . 5480 1 1394 . 1 1 113 113 GLY HA2 H 1 4.210 0.050 . 2 . . . . . . . . 5480 1 1395 . 1 1 113 113 GLY C C 13 174.580 0.10 . 1 . . . . . . . . 5480 1 1396 . 1 1 114 114 GLU N N 15 120.340 0.10 . 1 . . . . . . . . 5480 1 1397 . 1 1 114 114 GLU H H 1 7.860 0.050 . 1 . . . . . . . . 5480 1 1398 . 1 1 114 114 GLU CA C 13 55.000 0.10 . 1 . . . . . . . . 5480 1 1399 . 1 1 114 114 GLU HA H 1 4.340 0.050 . 1 . . . . . . . . 5480 1 1400 . 1 1 114 114 GLU CB C 13 30.750 0.10 . 1 . . . . . . . . 5480 1 1401 . 1 1 114 114 GLU HB3 H 1 1.626 0.050 . 2 . . . . . . . . 5480 1 1402 . 1 1 114 114 GLU HB2 H 1 1.799 0.050 . 2 . . . . . . . . 5480 1 1403 . 1 1 114 114 GLU CG C 13 35.550 0.10 . 1 . . . . . . . . 5480 1 1404 . 1 1 114 114 GLU HG3 H 1 1.936 0.050 . 2 . . . . . . . . 5480 1 1405 . 1 1 114 114 GLU HG2 H 1 2.036 0.050 . 2 . . . . . . . . 5480 1 1406 . 1 1 114 114 GLU CD C 13 182.500 0.10 . 1 . . . . . . . . 5480 1 1407 . 1 1 114 114 GLU C C 13 175.200 0.10 . 1 . . . . . . . . 5480 1 1408 . 1 1 115 115 LYS N N 15 124.620 0.10 . 1 . . . . . . . . 5480 1 1409 . 1 1 115 115 LYS H H 1 8.424 0.050 . 1 . . . . . . . . 5480 1 1410 . 1 1 115 115 LYS CA C 13 55.450 0.10 . 1 . . . . . . . . 5480 1 1411 . 1 1 115 115 LYS HA H 1 4.320 0.050 . 1 . . . . . . . . 5480 1 1412 . 1 1 115 115 LYS CB C 13 31.890 0.10 . 1 . . . . . . . . 5480 1 1413 . 1 1 115 115 LYS HB3 H 1 1.626 0.050 . 2 . . . . . . . . 5480 1 1414 . 1 1 115 115 LYS HB2 H 1 1.694 0.050 . 2 . . . . . . . . 5480 1 1415 . 1 1 115 115 LYS CG C 13 24.510 0.10 . 1 . . . . . . . . 5480 1 1416 . 1 1 115 115 LYS HG3 H 1 1.249 0.050 . 2 . . . . . . . . 5480 1 1417 . 1 1 115 115 LYS HG2 H 1 1.334 0.050 . 2 . . . . . . . . 5480 1 1418 . 1 1 115 115 LYS CD C 13 28.880 0.10 . 1 . . . . . . . . 5480 1 1419 . 1 1 115 115 LYS HD3 H 1 1.599 0.050 . 1 . . . . . . . . 5480 1 1420 . 1 1 115 115 LYS HD2 H 1 1.599 0.050 . 1 . . . . . . . . 5480 1 1421 . 1 1 115 115 LYS CE C 13 41.930 0.10 . 1 . . . . . . . . 5480 1 1422 . 1 1 115 115 LYS HE3 H 1 2.920 0.050 . 1 . . . . . . . . 5480 1 1423 . 1 1 115 115 LYS HE2 H 1 2.920 0.050 . 1 . . . . . . . . 5480 1 1424 . 1 1 115 115 LYS C C 13 175.400 0.10 . 1 . . . . . . . . 5480 1 1425 . 1 1 116 116 LEU N N 15 124.263 0.10 . 1 . . . . . . . . 5480 1 1426 . 1 1 116 116 LEU H H 1 7.915 0.050 . 1 . . . . . . . . 5480 1 1427 . 1 1 116 116 LEU CA C 13 53.800 0.10 . 1 . . . . . . . . 5480 1 1428 . 1 1 116 116 LEU HA H 1 4.750 0.050 . 1 . . . . . . . . 5480 1 1429 . 1 1 116 116 LEU CB C 13 44.900 0.10 . 1 . . . . . . . . 5480 1 1430 . 1 1 116 116 LEU HB3 H 1 1.530 0.050 . 2 . . . . . . . . 5480 1 1431 . 1 1 116 116 LEU HB2 H 1 1.390 0.050 . 2 . . . . . . . . 5480 1 1432 . 1 1 116 116 LEU CG C 13 27.480 0.10 . 1 . . . . . . . . 5480 1 1433 . 1 1 116 116 LEU HG H 1 1.481 0.050 . 1 . . . . . . . . 5480 1 1434 . 1 1 116 116 LEU CD1 C 13 27.204 0.10 . 1 . . . . . . . . 5480 1 1435 . 1 1 116 116 LEU HD11 H 1 0.705 0.050 . 2 . . . . . . . . 5480 1 1436 . 1 1 116 116 LEU HD12 H 1 0.705 0.050 . 2 . . . . . . . . 5480 1 1437 . 1 1 116 116 LEU HD13 H 1 0.705 0.050 . 2 . . . . . . . . 5480 1 1438 . 1 1 116 116 LEU CD2 C 13 24.130 0.10 . 1 . . . . . . . . 5480 1 1439 . 1 1 116 116 LEU HD21 H 1 0.725 0.050 . 2 . . . . . . . . 5480 1 1440 . 1 1 116 116 LEU HD22 H 1 0.725 0.050 . 2 . . . . . . . . 5480 1 1441 . 1 1 116 116 LEU HD23 H 1 0.725 0.050 . 2 . . . . . . . . 5480 1 1442 . 1 1 116 116 LEU C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 1443 . 1 1 117 117 THR N N 15 113.610 0.10 . 1 . . . . . . . . 5480 1 1444 . 1 1 117 117 THR H H 1 9.010 0.050 . 1 . . . . . . . . 5480 1 1445 . 1 1 117 117 THR CA C 13 60.490 0.10 . 1 . . . . . . . . 5480 1 1446 . 1 1 117 117 THR HA H 1 4.430 0.050 . 1 . . . . . . . . 5480 1 1447 . 1 1 117 117 THR CB C 13 71.090 0.10 . 1 . . . . . . . . 5480 1 1448 . 1 1 117 117 THR HB H 1 4.678 0.050 . 1 . . . . . . . . 5480 1 1449 . 1 1 117 117 THR HG21 H 1 1.240 0.050 . 1 . . . . . . . . 5480 1 1450 . 1 1 117 117 THR HG22 H 1 1.240 0.050 . 1 . . . . . . . . 5480 1 1451 . 1 1 117 117 THR HG23 H 1 1.240 0.050 . 1 . . . . . . . . 5480 1 1452 . 1 1 117 117 THR C C 13 175.600 0.10 . 1 . . . . . . . . 5480 1 1453 . 1 1 118 118 ASP N N 15 120.650 0.10 . 1 . . . . . . . . 5480 1 1454 . 1 1 118 118 ASP H H 1 8.772 0.050 . 1 . . . . . . . . 5480 1 1455 . 1 1 118 118 ASP CA C 13 57.800 0.10 . 1 . . . . . . . . 5480 1 1456 . 1 1 118 118 ASP HA H 1 4.150 0.050 . 1 . . . . . . . . 5480 1 1457 . 1 1 118 118 ASP CB C 13 39.700 0.10 . 1 . . . . . . . . 5480 1 1458 . 1 1 118 118 ASP HB3 H 1 2.520 0.050 . 2 . . . . . . . . 5480 1 1459 . 1 1 118 118 ASP HB2 H 1 2.700 0.050 . 2 . . . . . . . . 5480 1 1460 . 1 1 118 118 ASP CG C 13 179.700 0.10 . 1 . . . . . . . . 5480 1 1461 . 1 1 118 118 ASP C C 13 178.700 0.10 . 1 . . . . . . . . 5480 1 1462 . 1 1 119 119 GLU N N 15 118.790 0.10 . 1 . . . . . . . . 5480 1 1463 . 1 1 119 119 GLU H H 1 8.556 0.050 . 1 . . . . . . . . 5480 1 1464 . 1 1 119 119 GLU CA C 13 59.870 0.10 . 1 . . . . . . . . 5480 1 1465 . 1 1 119 119 GLU HA H 1 4.045 0.050 . 1 . . . . . . . . 5480 1 1466 . 1 1 119 119 GLU CB C 13 29.220 0.10 . 1 . . . . . . . . 5480 1 1467 . 1 1 119 119 GLU HB3 H 1 1.870 0.050 . 2 . . . . . . . . 5480 1 1468 . 1 1 119 119 GLU HB2 H 1 2.010 0.050 . 2 . . . . . . . . 5480 1 1469 . 1 1 119 119 GLU CG C 13 36.830 0.10 . 1 . . . . . . . . 5480 1 1470 . 1 1 119 119 GLU HG3 H 1 2.255 0.050 . 2 . . . . . . . . 5480 1 1471 . 1 1 119 119 GLU HG2 H 1 2.335 0.050 . 2 . . . . . . . . 5480 1 1472 . 1 1 119 119 GLU C C 13 179.100 0.10 . 1 . . . . . . . . 5480 1 1473 . 1 1 120 120 GLU N N 15 119.730 0.10 . 1 . . . . . . . . 5480 1 1474 . 1 1 120 120 GLU H H 1 7.614 0.050 . 1 . . . . . . . . 5480 1 1475 . 1 1 120 120 GLU CA C 13 59.188 0.10 . 1 . . . . . . . . 5480 1 1476 . 1 1 120 120 GLU HA H 1 3.947 0.050 . 1 . . . . . . . . 5480 1 1477 . 1 1 120 120 GLU CB C 13 30.560 0.10 . 1 . . . . . . . . 5480 1 1478 . 1 1 120 120 GLU HB3 H 1 2.340 0.050 . 2 . . . . . . . . 5480 1 1479 . 1 1 120 120 GLU HB2 H 1 1.850 0.050 . 2 . . . . . . . . 5480 1 1480 . 1 1 120 120 GLU CG C 13 38.080 0.10 . 1 . . . . . . . . 5480 1 1481 . 1 1 120 120 GLU HG3 H 1 2.191 0.050 . 2 . . . . . . . . 5480 1 1482 . 1 1 120 120 GLU HG2 H 1 2.317 0.050 . 2 . . . . . . . . 5480 1 1483 . 1 1 120 120 GLU CD C 13 183.500 0.10 . 1 . . . . . . . . 5480 1 1484 . 1 1 120 120 GLU C C 13 179.800 0.10 . 1 . . . . . . . . 5480 1 1485 . 1 1 121 121 VAL N N 15 120.100 0.10 . 1 . . . . . . . . 5480 1 1486 . 1 1 121 121 VAL H H 1 7.893 0.050 . 1 . . . . . . . . 5480 1 1487 . 1 1 121 121 VAL CA C 13 66.700 0.10 . 1 . . . . . . . . 5480 1 1488 . 1 1 121 121 VAL HA H 1 3.487 0.050 . 1 . . . . . . . . 5480 1 1489 . 1 1 121 121 VAL CB C 13 31.500 0.10 . 1 . . . . . . . . 5480 1 1490 . 1 1 121 121 VAL HB H 1 2.120 0.050 . 1 . . . . . . . . 5480 1 1491 . 1 1 121 121 VAL CG2 C 13 22.490 0.10 . 1 . . . . . . . . 5480 1 1492 . 1 1 121 121 VAL HG21 H 1 0.932 0.050 . 2 . . . . . . . . 5480 1 1493 . 1 1 121 121 VAL HG22 H 1 0.932 0.050 . 2 . . . . . . . . 5480 1 1494 . 1 1 121 121 VAL HG23 H 1 0.932 0.050 . 2 . . . . . . . . 5480 1 1495 . 1 1 121 121 VAL CG1 C 13 23.670 0.10 . 1 . . . . . . . . 5480 1 1496 . 1 1 121 121 VAL HG11 H 1 0.869 0.050 . 2 . . . . . . . . 5480 1 1497 . 1 1 121 121 VAL HG12 H 1 0.869 0.050 . 2 . . . . . . . . 5480 1 1498 . 1 1 121 121 VAL HG13 H 1 0.869 0.050 . 2 . . . . . . . . 5480 1 1499 . 1 1 121 121 VAL C C 13 177.500 0.10 . 1 . . . . . . . . 5480 1 1500 . 1 1 122 122 ASP N N 15 119.600 0.10 . 1 . . . . . . . . 5480 1 1501 . 1 1 122 122 ASP H H 1 7.985 0.050 . 1 . . . . . . . . 5480 1 1502 . 1 1 122 122 ASP CA C 13 57.625 0.10 . 1 . . . . . . . . 5480 1 1503 . 1 1 122 122 ASP HA H 1 4.267 0.050 . 1 . . . . . . . . 5480 1 1504 . 1 1 122 122 ASP CB C 13 40.495 0.10 . 1 . . . . . . . . 5480 1 1505 . 1 1 122 122 ASP HB3 H 1 2.560 0.050 . 2 . . . . . . . . 5480 1 1506 . 1 1 122 122 ASP HB2 H 1 2.713 0.050 . 2 . . . . . . . . 5480 1 1507 . 1 1 122 122 ASP CG C 13 179.300 0.10 . 1 . . . . . . . . 5480 1 1508 . 1 1 122 122 ASP C C 13 179.100 0.10 . 1 . . . . . . . . 5480 1 1509 . 1 1 123 123 GLU N N 15 118.660 0.10 . 1 . . . . . . . . 5480 1 1510 . 1 1 123 123 GLU H H 1 7.902 0.050 . 1 . . . . . . . . 5480 1 1511 . 1 1 123 123 GLU CA C 13 59.260 0.10 . 1 . . . . . . . . 5480 1 1512 . 1 1 123 123 GLU HA H 1 3.955 0.050 . 1 . . . . . . . . 5480 1 1513 . 1 1 123 123 GLU CB C 13 29.300 0.10 . 1 . . . . . . . . 5480 1 1514 . 1 1 123 123 GLU HB3 H 1 1.997 0.050 . 2 . . . . . . . . 5480 1 1515 . 1 1 123 123 GLU HB2 H 1 2.090 0.050 . 2 . . . . . . . . 5480 1 1516 . 1 1 123 123 GLU CG C 13 36.000 0.10 . 1 . . . . . . . . 5480 1 1517 . 1 1 123 123 GLU HG2 H 1 2.320 0.050 . 2 . . . . . . . . 5480 1 1518 . 1 1 123 123 GLU C C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 1519 . 1 1 124 124 MET N N 15 118.660 0.10 . 1 . . . . . . . . 5480 1 1520 . 1 1 124 124 MET H H 1 7.589 0.050 . 1 . . . . . . . . 5480 1 1521 . 1 1 124 124 MET CA C 13 59.510 0.10 . 1 . . . . . . . . 5480 1 1522 . 1 1 124 124 MET HA H 1 4.298 0.050 . 1 . . . . . . . . 5480 1 1523 . 1 1 124 124 MET CB C 13 33.800 0.10 . 1 . . . . . . . . 5480 1 1524 . 1 1 124 124 MET HB3 H 1 1.718 0.050 . 2 . . . . . . . . 5480 1 1525 . 1 1 124 124 MET HB2 H 1 2.272 0.050 . 2 . . . . . . . . 5480 1 1526 . 1 1 124 124 MET CG C 13 33.390 0.10 . 1 . . . . . . . . 5480 1 1527 . 1 1 124 124 MET HG3 H 1 2.414 0.050 . 2 . . . . . . . . 5480 1 1528 . 1 1 124 124 MET HG2 H 1 2.873 0.050 . 2 . . . . . . . . 5480 1 1529 . 1 1 124 124 MET CE C 13 17.310 0.10 . 1 . . . . . . . . 5480 1 1530 . 1 1 124 124 MET HE1 H 1 1.886 0.050 . 1 . . . . . . . . 5480 1 1531 . 1 1 124 124 MET HE2 H 1 1.886 0.050 . 1 . . . . . . . . 5480 1 1532 . 1 1 124 124 MET HE3 H 1 1.886 0.050 . 1 . . . . . . . . 5480 1 1533 . 1 1 124 124 MET C C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 1534 . 1 1 125 125 ILE N N 15 117.770 0.10 . 1 . . . . . . . . 5480 1 1535 . 1 1 125 125 ILE H H 1 7.710 0.050 . 1 . . . . . . . . 5480 1 1536 . 1 1 125 125 ILE CA C 13 62.700 0.10 . 1 . . . . . . . . 5480 1 1537 . 1 1 125 125 ILE HA H 1 3.560 0.050 . 1 . . . . . . . . 5480 1 1538 . 1 1 125 125 ILE CB C 13 36.000 0.10 . 1 . . . . . . . . 5480 1 1539 . 1 1 125 125 ILE HB H 1 2.200 0.050 . 1 . . . . . . . . 5480 1 1540 . 1 1 125 125 ILE CG1 C 13 27.620 0.10 . 2 . . . . . . . . 5480 1 1541 . 1 1 125 125 ILE HG13 H 1 1.377 0.050 . 1 . . . . . . . . 5480 1 1542 . 1 1 125 125 ILE HG12 H 1 1.325 0.050 . 1 . . . . . . . . 5480 1 1543 . 1 1 125 125 ILE CD1 C 13 9.770 0.10 . 1 . . . . . . . . 5480 1 1544 . 1 1 125 125 ILE HD11 H 1 0.520 0.050 . 1 . . . . . . . . 5480 1 1545 . 1 1 125 125 ILE HD12 H 1 0.520 0.050 . 1 . . . . . . . . 5480 1 1546 . 1 1 125 125 ILE HD13 H 1 0.520 0.050 . 1 . . . . . . . . 5480 1 1547 . 1 1 125 125 ILE CG2 C 13 16.550 0.10 . 1 . . . . . . . . 5480 1 1548 . 1 1 125 125 ILE HG21 H 1 0.694 0.050 . 1 . . . . . . . . 5480 1 1549 . 1 1 125 125 ILE HG22 H 1 0.694 0.050 . 1 . . . . . . . . 5480 1 1550 . 1 1 125 125 ILE HG23 H 1 0.694 0.050 . 1 . . . . . . . . 5480 1 1551 . 1 1 125 125 ILE C C 13 178.600 0.10 . 1 . . . . . . . . 5480 1 1552 . 1 1 126 126 ARG N N 15 118.150 0.10 . 1 . . . . . . . . 5480 1 1553 . 1 1 126 126 ARG H H 1 8.128 0.050 . 1 . . . . . . . . 5480 1 1554 . 1 1 126 126 ARG CA C 13 59.300 0.10 . 1 . . . . . . . . 5480 1 1555 . 1 1 126 126 ARG HA H 1 3.980 0.050 . 1 . . . . . . . . 5480 1 1556 . 1 1 126 126 ARG CB C 13 30.280 0.10 . 1 . . . . . . . . 5480 1 1557 . 1 1 126 126 ARG HB3 H 1 1.909 0.050 . 1 . . . . . . . . 5480 1 1558 . 1 1 126 126 ARG HB2 H 1 1.909 0.050 . 1 . . . . . . . . 5480 1 1559 . 1 1 126 126 ARG CG C 13 28.420 0.10 . 1 . . . . . . . . 5480 1 1560 . 1 1 126 126 ARG HG3 H 1 1.659 0.050 . 2 . . . . . . . . 5480 1 1561 . 1 1 126 126 ARG HG2 H 1 1.824 0.050 . 2 . . . . . . . . 5480 1 1562 . 1 1 126 126 ARG CD C 13 43.510 0.10 . 1 . . . . . . . . 5480 1 1563 . 1 1 126 126 ARG HD3 H 1 3.129 0.050 . 2 . . . . . . . . 5480 1 1564 . 1 1 126 126 ARG HD2 H 1 3.203 0.050 . 2 . . . . . . . . 5480 1 1565 . 1 1 126 126 ARG C C 13 178.100 0.10 . 1 . . . . . . . . 5480 1 1566 . 1 1 127 127 GLU N N 15 116.840 0.10 . 1 . . . . . . . . 5480 1 1567 . 1 1 127 127 GLU H H 1 7.678 0.050 . 1 . . . . . . . . 5480 1 1568 . 1 1 127 127 GLU CA C 13 59.130 0.10 . 1 . . . . . . . . 5480 1 1569 . 1 1 127 127 GLU HA H 1 3.950 0.050 . 1 . . . . . . . . 5480 1 1570 . 1 1 127 127 GLU CB C 13 30.400 0.10 . 1 . . . . . . . . 5480 1 1571 . 1 1 127 127 GLU HB3 H 1 2.100 0.050 . 2 . . . . . . . . 5480 1 1572 . 1 1 127 127 GLU HB2 H 1 2.290 0.050 . 2 . . . . . . . . 5480 1 1573 . 1 1 127 127 GLU CG C 13 37.240 0.10 . 1 . . . . . . . . 5480 1 1574 . 1 1 127 127 GLU HG3 H 1 2.218 0.050 . 2 . . . . . . . . 5480 1 1575 . 1 1 127 127 GLU HG2 H 1 2.630 0.050 . 2 . . . . . . . . 5480 1 1576 . 1 1 127 127 GLU CD C 13 183.800 0.10 . 1 . . . . . . . . 5480 1 1577 . 1 1 127 127 GLU C C 13 177.100 0.10 . 1 . . . . . . . . 5480 1 1578 . 1 1 128 128 ALA N N 15 116.840 0.10 . 1 . . . . . . . . 5480 1 1579 . 1 1 128 128 ALA H H 1 7.232 0.050 . 1 . . . . . . . . 5480 1 1580 . 1 1 128 128 ALA CA C 13 50.900 0.10 . 1 . . . . . . . . 5480 1 1581 . 1 1 128 128 ALA HA H 1 4.570 0.050 . 1 . . . . . . . . 5480 1 1582 . 1 1 128 128 ALA CB C 13 22.830 0.10 . 1 . . . . . . . . 5480 1 1583 . 1 1 128 128 ALA HB1 H 1 1.440 0.050 . 1 . . . . . . . . 5480 1 1584 . 1 1 128 128 ALA HB2 H 1 1.440 0.050 . 1 . . . . . . . . 5480 1 1585 . 1 1 128 128 ALA HB3 H 1 1.440 0.050 . 1 . . . . . . . . 5480 1 1586 . 1 1 128 128 ALA C C 13 177.100 0.10 . 1 . . . . . . . . 5480 1 1587 . 1 1 129 129 ASP N N 15 117.920 0.10 . 1 . . . . . . . . 5480 1 1588 . 1 1 129 129 ASP H H 1 7.900 0.050 . 1 . . . . . . . . 5480 1 1589 . 1 1 129 129 ASP CA C 13 54.500 0.10 . 1 . . . . . . . . 5480 1 1590 . 1 1 129 129 ASP HA H 1 4.430 0.050 . 1 . . . . . . . . 5480 1 1591 . 1 1 129 129 ASP CB C 13 41.000 0.10 . 1 . . . . . . . . 5480 1 1592 . 1 1 129 129 ASP HB3 H 1 2.370 0.050 . 2 . . . . . . . . 5480 1 1593 . 1 1 129 129 ASP HB2 H 1 2.710 0.050 . 2 . . . . . . . . 5480 1 1594 . 1 1 129 129 ASP CG C 13 179.200 0.10 . 1 . . . . . . . . 5480 1 1595 . 1 1 129 129 ASP C C 13 175.800 0.10 . 1 . . . . . . . . 5480 1 1596 . 1 1 130 130 ILE N N 15 127.438 0.10 . 1 . . . . . . . . 5480 1 1597 . 1 1 130 130 ILE H H 1 8.222 0.050 . 1 . . . . . . . . 5480 1 1598 . 1 1 130 130 ILE CA C 13 63.100 0.10 . 1 . . . . . . . . 5480 1 1599 . 1 1 130 130 ILE HA H 1 3.936 0.050 . 1 . . . . . . . . 5480 1 1600 . 1 1 130 130 ILE CB C 13 38.900 0.10 . 1 . . . . . . . . 5480 1 1601 . 1 1 130 130 ILE HB H 1 1.940 0.050 . 1 . . . . . . . . 5480 1 1602 . 1 1 130 130 ILE CG1 C 13 27.700 0.10 . 2 . . . . . . . . 5480 1 1603 . 1 1 130 130 ILE HG13 H 1 1.230 0.050 . 1 . . . . . . . . 5480 1 1604 . 1 1 130 130 ILE HG12 H 1 1.640 0.050 . 1 . . . . . . . . 5480 1 1605 . 1 1 130 130 ILE CD1 C 13 12.500 0.10 . 1 . . . . . . . . 5480 1 1606 . 1 1 130 130 ILE HD11 H 1 0.830 0.050 . 1 . . . . . . . . 5480 1 1607 . 1 1 130 130 ILE HD12 H 1 0.830 0.050 . 1 . . . . . . . . 5480 1 1608 . 1 1 130 130 ILE HD13 H 1 0.830 0.050 . 1 . . . . . . . . 5480 1 1609 . 1 1 130 130 ILE CG2 C 13 17.240 0.10 . 1 . . . . . . . . 5480 1 1610 . 1 1 130 130 ILE HG21 H 1 0.870 0.050 . 1 . . . . . . . . 5480 1 1611 . 1 1 130 130 ILE HG22 H 1 0.870 0.050 . 1 . . . . . . . . 5480 1 1612 . 1 1 130 130 ILE HG23 H 1 0.870 0.050 . 1 . . . . . . . . 5480 1 1613 . 1 1 130 130 ILE C C 13 177.800 0.10 . 1 . . . . . . . . 5480 1 1614 . 1 1 131 131 ASP N N 15 116.600 0.10 . 1 . . . . . . . . 5480 1 1615 . 1 1 131 131 ASP H H 1 8.278 0.050 . 1 . . . . . . . . 5480 1 1616 . 1 1 131 131 ASP CA C 13 53.900 0.10 . 1 . . . . . . . . 5480 1 1617 . 1 1 131 131 ASP HA H 1 4.450 0.050 . 1 . . . . . . . . 5480 1 1618 . 1 1 131 131 ASP CB C 13 39.837 0.10 . 1 . . . . . . . . 5480 1 1619 . 1 1 131 131 ASP HB3 H 1 2.600 0.050 . 2 . . . . . . . . 5480 1 1620 . 1 1 131 131 ASP HB2 H 1 3.020 0.050 . 2 . . . . . . . . 5480 1 1621 . 1 1 131 131 ASP CG C 13 180.600 0.10 . 1 . . . . . . . . 5480 1 1622 . 1 1 131 131 ASP C C 13 178.300 0.10 . 1 . . . . . . . . 5480 1 1623 . 1 1 132 132 GLY N N 15 108.080 0.10 . 1 . . . . . . . . 5480 1 1624 . 1 1 132 132 GLY H H 1 7.603 0.050 . 1 . . . . . . . . 5480 1 1625 . 1 1 132 132 GLY CA C 13 47.280 0.10 . 1 . . . . . . . . 5480 1 1626 . 1 1 132 132 GLY HA3 H 1 3.940 0.050 . 2 . . . . . . . . 5480 1 1627 . 1 1 132 132 GLY HA2 H 1 3.770 0.050 . 2 . . . . . . . . 5480 1 1628 . 1 1 132 132 GLY C C 13 175.350 0.10 . 1 . . . . . . . . 5480 1 1629 . 1 1 133 133 ASP N N 15 120.147 0.10 . 1 . . . . . . . . 5480 1 1630 . 1 1 133 133 ASP H H 1 8.283 0.050 . 1 . . . . . . . . 5480 1 1631 . 1 1 133 133 ASP CA C 13 53.600 0.10 . 1 . . . . . . . . 5480 1 1632 . 1 1 133 133 ASP HA H 1 4.410 0.050 . 1 . . . . . . . . 5480 1 1633 . 1 1 133 133 ASP CB C 13 40.100 0.10 . 1 . . . . . . . . 5480 1 1634 . 1 1 133 133 ASP HB3 H 1 2.940 0.050 . 2 . . . . . . . . 5480 1 1635 . 1 1 133 133 ASP HB2 H 1 2.470 0.050 . 2 . . . . . . . . 5480 1 1636 . 1 1 133 133 ASP CG C 13 182.500 0.10 . 1 . . . . . . . . 5480 1 1637 . 1 1 133 133 ASP C C 13 177.600 0.10 . 1 . . . . . . . . 5480 1 1638 . 1 1 134 134 GLY N N 15 111.930 0.10 . 1 . . . . . . . . 5480 1 1639 . 1 1 134 134 GLY H H 1 10.008 0.050 . 1 . . . . . . . . 5480 1 1640 . 1 1 134 134 GLY CA C 13 45.700 0.10 . 1 . . . . . . . . 5480 1 1641 . 1 1 134 134 GLY HA3 H 1 4.030 0.050 . 2 . . . . . . . . 5480 1 1642 . 1 1 134 134 GLY HA2 H 1 3.370 0.050 . 2 . . . . . . . . 5480 1 1643 . 1 1 134 134 GLY C C 13 172.900 0.10 . 1 . . . . . . . . 5480 1 1644 . 1 1 135 135 GLN N N 15 115.090 0.10 . 1 . . . . . . . . 5480 1 1645 . 1 1 135 135 GLN H H 1 7.951 0.050 . 1 . . . . . . . . 5480 1 1646 . 1 1 135 135 GLN CA C 13 53.100 0.10 . 1 . . . . . . . . 5480 1 1647 . 1 1 135 135 GLN HA H 1 4.912 0.050 . 1 . . . . . . . . 5480 1 1648 . 1 1 135 135 GLN CB C 13 32.650 0.10 . 1 . . . . . . . . 5480 1 1649 . 1 1 135 135 GLN HB3 H 1 1.960 0.050 . 2 . . . . . . . . 5480 1 1650 . 1 1 135 135 GLN HB2 H 1 1.780 0.050 . 2 . . . . . . . . 5480 1 1651 . 1 1 135 135 GLN CG C 13 33.320 0.10 . 1 . . . . . . . . 5480 1 1652 . 1 1 135 135 GLN HG3 H 1 1.921 0.050 . 2 . . . . . . . . 5480 1 1653 . 1 1 135 135 GLN HG2 H 1 1.982 0.050 . 2 . . . . . . . . 5480 1 1654 . 1 1 135 135 GLN CD C 13 179.000 0.10 . 1 . . . . . . . . 5480 1 1655 . 1 1 135 135 GLN NE2 N 15 108.090 0.10 . 1 . . . . . . . . 5480 1 1656 . 1 1 135 135 GLN HE21 H 1 6.479 0.050 . 2 . . . . . . . . 5480 1 1657 . 1 1 135 135 GLN HE22 H 1 5.854 0.050 . 2 . . . . . . . . 5480 1 1658 . 1 1 135 135 GLN C C 13 175.300 0.10 . 1 . . . . . . . . 5480 1 1659 . 1 1 136 136 VAL N N 15 125.150 0.10 . 1 . . . . . . . . 5480 1 1660 . 1 1 136 136 VAL H H 1 9.117 0.050 . 1 . . . . . . . . 5480 1 1661 . 1 1 136 136 VAL CA C 13 61.480 0.10 . 1 . . . . . . . . 5480 1 1662 . 1 1 136 136 VAL HA H 1 5.170 0.050 . 1 . . . . . . . . 5480 1 1663 . 1 1 136 136 VAL CB C 13 34.023 0.10 . 1 . . . . . . . . 5480 1 1664 . 1 1 136 136 VAL HB H 1 2.297 0.050 . 1 . . . . . . . . 5480 1 1665 . 1 1 136 136 VAL CG2 C 13 23.140 0.10 . 1 . . . . . . . . 5480 1 1666 . 1 1 136 136 VAL HG21 H 1 1.054 0.050 . 2 . . . . . . . . 5480 1 1667 . 1 1 136 136 VAL HG22 H 1 1.054 0.050 . 2 . . . . . . . . 5480 1 1668 . 1 1 136 136 VAL HG23 H 1 1.054 0.050 . 2 . . . . . . . . 5480 1 1669 . 1 1 136 136 VAL CG1 C 13 21.890 0.10 . 1 . . . . . . . . 5480 1 1670 . 1 1 136 136 VAL HG11 H 1 1.270 0.050 . 2 . . . . . . . . 5480 1 1671 . 1 1 136 136 VAL HG12 H 1 1.270 0.050 . 2 . . . . . . . . 5480 1 1672 . 1 1 136 136 VAL HG13 H 1 1.270 0.050 . 2 . . . . . . . . 5480 1 1673 . 1 1 136 136 VAL C C 13 175.900 0.10 . 1 . . . . . . . . 5480 1 1674 . 1 1 137 137 ASN N N 15 128.713 0.10 . 1 . . . . . . . . 5480 1 1675 . 1 1 137 137 ASN H H 1 9.518 0.050 . 1 . . . . . . . . 5480 1 1676 . 1 1 137 137 ASN CA C 13 50.900 0.10 . 1 . . . . . . . . 5480 1 1677 . 1 1 137 137 ASN HA H 1 5.301 0.050 . 1 . . . . . . . . 5480 1 1678 . 1 1 137 137 ASN CB C 13 38.500 0.10 . 1 . . . . . . . . 5480 1 1679 . 1 1 137 137 ASN HB3 H 1 2.960 0.050 . 2 . . . . . . . . 5480 1 1680 . 1 1 137 137 ASN HB2 H 1 3.120 0.050 . 2 . . . . . . . . 5480 1 1681 . 1 1 137 137 ASN CG C 13 175.300 0.10 . 1 . . . . . . . . 5480 1 1682 . 1 1 137 137 ASN ND2 N 15 108.430 0.10 . 1 . . . . . . . . 5480 1 1683 . 1 1 137 137 ASN HD21 H 1 7.110 0.050 . 2 . . . . . . . . 5480 1 1684 . 1 1 137 137 ASN HD22 H 1 6.820 0.050 . 2 . . . . . . . . 5480 1 1685 . 1 1 137 137 ASN C C 13 175.000 0.10 . 1 . . . . . . . . 5480 1 1686 . 1 1 138 138 TYR N N 15 118.100 0.10 . 1 . . . . . . . . 5480 1 1687 . 1 1 138 138 TYR H H 1 8.201 0.050 . 1 . . . . . . . . 5480 1 1688 . 1 1 138 138 TYR CA C 13 62.400 0.10 . 1 . . . . . . . . 5480 1 1689 . 1 1 138 138 TYR HA H 1 3.380 0.050 . 1 . . . . . . . . 5480 1 1690 . 1 1 138 138 TYR CB C 13 37.780 0.10 . 1 . . . . . . . . 5480 1 1691 . 1 1 138 138 TYR HB3 H 1 2.095 0.050 . 2 . . . . . . . . 5480 1 1692 . 1 1 138 138 TYR HB2 H 1 2.387 0.050 . 2 . . . . . . . . 5480 1 1693 . 1 1 138 138 TYR CD1 C 13 132.180 0.10 . 1 . . . . . . . . 5480 1 1694 . 1 1 138 138 TYR HD1 H 1 6.177 0.050 . 1 . . . . . . . . 5480 1 1695 . 1 1 138 138 TYR CE1 C 13 117.860 0.10 . 1 . . . . . . . . 5480 1 1696 . 1 1 138 138 TYR HE1 H 1 6.460 0.050 . 1 . . . . . . . . 5480 1 1697 . 1 1 138 138 TYR CE2 C 13 117.860 0.10 . 1 . . . . . . . . 5480 1 1698 . 1 1 138 138 TYR HE2 H 1 6.460 0.050 . 1 . . . . . . . . 5480 1 1699 . 1 1 138 138 TYR CD2 C 13 132.180 0.10 . 1 . . . . . . . . 5480 1 1700 . 1 1 138 138 TYR HD2 H 1 6.177 0.050 . 1 . . . . . . . . 5480 1 1701 . 1 1 138 138 TYR C C 13 176.300 0.10 . 1 . . . . . . . . 5480 1 1702 . 1 1 139 139 GLU N N 15 118.160 0.10 . 1 . . . . . . . . 5480 1 1703 . 1 1 139 139 GLU H H 1 8.020 0.050 . 1 . . . . . . . . 5480 1 1704 . 1 1 139 139 GLU CA C 13 60.300 0.10 . 1 . . . . . . . . 5480 1 1705 . 1 1 139 139 GLU HA H 1 3.600 0.050 . 1 . . . . . . . . 5480 1 1706 . 1 1 139 139 GLU CB C 13 28.850 0.10 . 1 . . . . . . . . 5480 1 1707 . 1 1 139 139 GLU HB3 H 1 1.912 0.050 . 2 . . . . . . . . 5480 1 1708 . 1 1 139 139 GLU HB2 H 1 2.020 0.050 . 2 . . . . . . . . 5480 1 1709 . 1 1 139 139 GLU CG C 13 37.120 0.10 . 1 . . . . . . . . 5480 1 1710 . 1 1 139 139 GLU HG3 H 1 2.280 0.050 . 2 . . . . . . . . 5480 1 1711 . 1 1 139 139 GLU HG2 H 1 2.218 0.050 . 2 . . . . . . . . 5480 1 1712 . 1 1 139 139 GLU C C 13 180.500 0.10 . 1 . . . . . . . . 5480 1 1713 . 1 1 140 140 GLU N N 15 119.520 0.10 . 1 . . . . . . . . 5480 1 1714 . 1 1 140 140 GLU H H 1 8.725 0.050 . 1 . . . . . . . . 5480 1 1715 . 1 1 140 140 GLU CA C 13 58.700 0.10 . 1 . . . . . . . . 5480 1 1716 . 1 1 140 140 GLU HA H 1 3.860 0.050 . 1 . . . . . . . . 5480 1 1717 . 1 1 140 140 GLU CB C 13 29.800 0.10 . 1 . . . . . . . . 5480 1 1718 . 1 1 140 140 GLU HB3 H 1 1.890 0.050 . 2 . . . . . . . . 5480 1 1719 . 1 1 140 140 GLU HB2 H 1 2.010 0.050 . 2 . . . . . . . . 5480 1 1720 . 1 1 140 140 GLU CG C 13 37.080 0.10 . 1 . . . . . . . . 5480 1 1721 . 1 1 140 140 GLU HG3 H 1 2.510 0.050 . 2 . . . . . . . . 5480 1 1722 . 1 1 140 140 GLU HG2 H 1 2.280 0.050 . 2 . . . . . . . . 5480 1 1723 . 1 1 140 140 GLU C C 13 179.500 0.10 . 1 . . . . . . . . 5480 1 1724 . 1 1 141 141 PHE N N 15 124.020 0.10 . 1 . . . . . . . . 5480 1 1725 . 1 1 141 141 PHE H H 1 8.602 0.050 . 1 . . . . . . . . 5480 1 1726 . 1 1 141 141 PHE CA C 13 62.190 0.10 . 1 . . . . . . . . 5480 1 1727 . 1 1 141 141 PHE HA H 1 3.734 0.050 . 1 . . . . . . . . 5480 1 1728 . 1 1 141 141 PHE CB C 13 40.250 0.10 . 1 . . . . . . . . 5480 1 1729 . 1 1 141 141 PHE HB3 H 1 3.086 0.050 . 2 . . . . . . . . 5480 1 1730 . 1 1 141 141 PHE HB2 H 1 3.301 0.050 . 2 . . . . . . . . 5480 1 1731 . 1 1 141 141 PHE HD1 H 1 6.760 0.050 . 1 . . . . . . . . 5480 1 1732 . 1 1 141 141 PHE HE1 H 1 6.989 0.050 . 1 . . . . . . . . 5480 1 1733 . 1 1 141 141 PHE HE2 H 1 6.989 0.050 . 1 . . . . . . . . 5480 1 1734 . 1 1 141 141 PHE HD2 H 1 6.760 0.050 . 1 . . . . . . . . 5480 1 1735 . 1 1 141 141 PHE C C 13 176.700 0.10 . 1 . . . . . . . . 5480 1 1736 . 1 1 142 142 VAL N N 15 119.150 0.10 . 1 . . . . . . . . 5480 1 1737 . 1 1 142 142 VAL H H 1 8.716 0.050 . 1 . . . . . . . . 5480 1 1738 . 1 1 142 142 VAL CA C 13 67.160 0.10 . 1 . . . . . . . . 5480 1 1739 . 1 1 142 142 VAL HA H 1 3.095 0.050 . 1 . . . . . . . . 5480 1 1740 . 1 1 142 142 VAL CB C 13 31.500 0.10 . 1 . . . . . . . . 5480 1 1741 . 1 1 142 142 VAL HB H 1 1.800 0.050 . 1 . . . . . . . . 5480 1 1742 . 1 1 142 142 VAL CG2 C 13 21.330 0.10 . 1 . . . . . . . . 5480 1 1743 . 1 1 142 142 VAL HG21 H 1 0.696 0.050 . 2 . . . . . . . . 5480 1 1744 . 1 1 142 142 VAL HG22 H 1 0.696 0.050 . 2 . . . . . . . . 5480 1 1745 . 1 1 142 142 VAL HG23 H 1 0.696 0.050 . 2 . . . . . . . . 5480 1 1746 . 1 1 142 142 VAL CG1 C 13 23.140 0.10 . 1 . . . . . . . . 5480 1 1747 . 1 1 142 142 VAL HG11 H 1 0.417 0.050 . 2 . . . . . . . . 5480 1 1748 . 1 1 142 142 VAL HG12 H 1 0.417 0.050 . 2 . . . . . . . . 5480 1 1749 . 1 1 142 142 VAL HG13 H 1 0.417 0.050 . 2 . . . . . . . . 5480 1 1750 . 1 1 142 142 VAL C C 13 179.400 0.10 . 1 . . . . . . . . 5480 1 1751 . 1 1 143 143 GLN N N 15 119.180 0.10 . 1 . . . . . . . . 5480 1 1752 . 1 1 143 143 GLN H H 1 7.755 0.050 . 1 . . . . . . . . 5480 1 1753 . 1 1 143 143 GLN CA C 13 59.100 0.10 . 1 . . . . . . . . 5480 1 1754 . 1 1 143 143 GLN HA H 1 3.740 0.050 . 1 . . . . . . . . 5480 1 1755 . 1 1 143 143 GLN CB C 13 27.920 0.10 . 1 . . . . . . . . 5480 1 1756 . 1 1 143 143 GLN HB3 H 1 2.045 0.050 . 1 . . . . . . . . 5480 1 1757 . 1 1 143 143 GLN HB2 H 1 2.045 0.050 . 1 . . . . . . . . 5480 1 1758 . 1 1 143 143 GLN CG C 13 33.960 0.10 . 1 . . . . . . . . 5480 1 1759 . 1 1 143 143 GLN HG3 H 1 2.314 0.050 . 2 . . . . . . . . 5480 1 1760 . 1 1 143 143 GLN HG2 H 1 2.356 0.050 . 2 . . . . . . . . 5480 1 1761 . 1 1 143 143 GLN CD C 13 179.700 0.10 . 1 . . . . . . . . 5480 1 1762 . 1 1 143 143 GLN NE2 N 15 110.940 0.10 . 1 . . . . . . . . 5480 1 1763 . 1 1 143 143 GLN HE21 H 1 7.241 0.050 . 2 . . . . . . . . 5480 1 1764 . 1 1 143 143 GLN HE22 H 1 6.644 0.050 . 2 . . . . . . . . 5480 1 1765 . 1 1 143 143 GLN C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 1766 . 1 1 144 144 MET N N 15 118.340 0.10 . 1 . . . . . . . . 5480 1 1767 . 1 1 144 144 MET H H 1 7.532 0.050 . 1 . . . . . . . . 5480 1 1768 . 1 1 144 144 MET CA C 13 58.360 0.10 . 1 . . . . . . . . 5480 1 1769 . 1 1 144 144 MET HA H 1 3.984 0.050 . 1 . . . . . . . . 5480 1 1770 . 1 1 144 144 MET CB C 13 31.700 0.10 . 1 . . . . . . . . 5480 1 1771 . 1 1 144 144 MET HB3 H 1 1.880 0.050 . 2 . . . . . . . . 5480 1 1772 . 1 1 144 144 MET HB2 H 1 1.950 0.050 . 2 . . . . . . . . 5480 1 1773 . 1 1 144 144 MET CG C 13 31.216 0.10 . 1 . . . . . . . . 5480 1 1774 . 1 1 144 144 MET HG3 H 1 1.871 0.050 . 2 . . . . . . . . 5480 1 1775 . 1 1 144 144 MET HG2 H 1 2.286 0.050 . 2 . . . . . . . . 5480 1 1776 . 1 1 144 144 MET CE C 13 16.140 0.10 . 1 . . . . . . . . 5480 1 1777 . 1 1 144 144 MET HE1 H 1 0.536 0.050 . 1 . . . . . . . . 5480 1 1778 . 1 1 144 144 MET HE2 H 1 0.536 0.050 . 1 . . . . . . . . 5480 1 1779 . 1 1 144 144 MET HE3 H 1 0.536 0.050 . 1 . . . . . . . . 5480 1 1780 . 1 1 144 144 MET C C 13 178.200 0.10 . 1 . . . . . . . . 5480 1 1781 . 1 1 145 145 MET N N 15 114.790 0.10 . 1 . . . . . . . . 5480 1 1782 . 1 1 145 145 MET H H 1 7.740 0.050 . 1 . . . . . . . . 5480 1 1783 . 1 1 145 145 MET CA C 13 56.300 0.10 . 1 . . . . . . . . 5480 1 1784 . 1 1 145 145 MET HA H 1 3.990 0.050 . 1 . . . . . . . . 5480 1 1785 . 1 1 145 145 MET CB C 13 32.080 0.10 . 1 . . . . . . . . 5480 1 1786 . 1 1 145 145 MET HB3 H 1 1.720 0.050 . 2 . . . . . . . . 5480 1 1787 . 1 1 145 145 MET HB2 H 1 1.750 0.050 . 2 . . . . . . . . 5480 1 1788 . 1 1 145 145 MET CG C 13 32.600 0.10 . 1 . . . . . . . . 5480 1 1789 . 1 1 145 145 MET HG3 H 1 1.750 0.050 . 2 . . . . . . . . 5480 1 1790 . 1 1 145 145 MET HG2 H 1 2.461 0.050 . 2 . . . . . . . . 5480 1 1791 . 1 1 145 145 MET CE C 13 16.010 0.10 . 1 . . . . . . . . 5480 1 1792 . 1 1 145 145 MET HE1 H 1 0.938 0.050 . 1 . . . . . . . . 5480 1 1793 . 1 1 145 145 MET HE2 H 1 0.938 0.050 . 1 . . . . . . . . 5480 1 1794 . 1 1 145 145 MET HE3 H 1 0.938 0.050 . 1 . . . . . . . . 5480 1 1795 . 1 1 145 145 MET C C 13 177.900 0.10 . 1 . . . . . . . . 5480 1 1796 . 1 1 146 146 THR N N 15 108.270 0.10 . 1 . . . . . . . . 5480 1 1797 . 1 1 146 146 THR H H 1 7.658 0.050 . 1 . . . . . . . . 5480 1 1798 . 1 1 146 146 THR CA C 13 61.800 0.10 . 1 . . . . . . . . 5480 1 1799 . 1 1 146 146 THR HA H 1 4.280 0.050 . 1 . . . . . . . . 5480 1 1800 . 1 1 146 146 THR CB C 13 70.303 0.10 . 1 . . . . . . . . 5480 1 1801 . 1 1 146 146 THR HB H 1 4.239 0.050 . 1 . . . . . . . . 5480 1 1802 . 1 1 146 146 THR CG2 C 13 21.330 0.10 . 1 . . . . . . . . 5480 1 1803 . 1 1 146 146 THR HG21 H 1 1.086 0.050 . 1 . . . . . . . . 5480 1 1804 . 1 1 146 146 THR HG22 H 1 1.086 0.050 . 1 . . . . . . . . 5480 1 1805 . 1 1 146 146 THR HG23 H 1 1.086 0.050 . 1 . . . . . . . . 5480 1 1806 . 1 1 146 146 THR C C 13 174.400 0.10 . 1 . . . . . . . . 5480 1 1807 . 1 1 147 147 ALA N N 15 126.062 0.10 . 1 . . . . . . . . 5480 1 1808 . 1 1 147 147 ALA H H 1 7.312 0.050 . 1 . . . . . . . . 5480 1 1809 . 1 1 147 147 ALA CA C 13 52.900 0.10 . 1 . . . . . . . . 5480 1 1810 . 1 1 147 147 ALA HA H 1 4.174 0.050 . 1 . . . . . . . . 5480 1 1811 . 1 1 147 147 ALA CB C 13 18.900 0.10 . 1 . . . . . . . . 5480 1 1812 . 1 1 147 147 ALA HB1 H 1 1.340 0.050 . 1 . . . . . . . . 5480 1 1813 . 1 1 147 147 ALA HB2 H 1 1.340 0.050 . 1 . . . . . . . . 5480 1 1814 . 1 1 147 147 ALA HB3 H 1 1.340 0.050 . 1 . . . . . . . . 5480 1 1815 . 1 1 147 147 ALA C C 13 176.800 0.10 . 1 . . . . . . . . 5480 1 1816 . 1 1 148 148 LYS N N 15 125.770 0.10 . 1 . . . . . . . . 5480 1 1817 . 1 1 148 148 LYS H H 1 7.840 0.050 . 1 . . . . . . . . 5480 1 1818 . 1 1 148 148 LYS CA C 13 57.400 0.10 . 1 . . . . . . . . 5480 1 1819 . 1 1 148 148 LYS HA H 1 4.050 0.050 . 1 . . . . . . . . 5480 1 1820 . 1 1 148 148 LYS CB C 13 33.710 0.10 . 1 . . . . . . . . 5480 1 1821 . 1 1 148 148 LYS HB3 H 1 1.621 0.050 . 2 . . . . . . . . 5480 1 1822 . 1 1 148 148 LYS HB2 H 1 1.757 0.050 . 2 . . . . . . . . 5480 1 1823 . 1 1 148 148 LYS CG C 13 24.680 0.10 . 1 . . . . . . . . 5480 1 1824 . 1 1 148 148 LYS HG3 H 1 1.350 0.050 . 1 . . . . . . . . 5480 1 1825 . 1 1 148 148 LYS HG2 H 1 1.350 0.050 . 1 . . . . . . . . 5480 1 1826 . 1 1 148 148 LYS CD C 13 28.950 0.10 . 1 . . . . . . . . 5480 1 1827 . 1 1 148 148 LYS HD3 H 1 1.596 0.050 . 1 . . . . . . . . 5480 1 1828 . 1 1 148 148 LYS HD2 H 1 1.596 0.050 . 1 . . . . . . . . 5480 1 1829 . 1 1 148 148 LYS CE C 13 42.000 0.10 . 1 . . . . . . . . 5480 1 1830 . 1 1 148 148 LYS HE3 H 1 2.934 0.050 . 1 . . . . . . . . 5480 1 1831 . 1 1 148 148 LYS HE2 H 1 2.934 0.050 . 1 . . . . . . . . 5480 1 1832 . 1 1 148 148 LYS C C 13 181.400 0.10 . 1 . . . . . . . . 5480 1 stop_ save_ save_chemical_shift_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_2 _Assigned_chem_shift_list.Entry_ID 5480 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Exp-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 5480 2 . . 2 $sample_2 . 5480 2 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 . 2 2 1 1 GLN H H 1 8.225 0.050 . 1 . . . . . . . . 5480 2 2 . 2 2 1 1 GLN HA H 1 4.180 0.050 . 1 . . . . . . . . 5480 2 3 . 2 2 1 1 GLN HB3 H 1 1.859 0.050 . 2 . . . . . . . . 5480 2 4 . 2 2 1 1 GLN HB2 H 1 1.981 0.050 . 2 . . . . . . . . 5480 2 5 . 2 2 1 1 GLN HG3 H 1 2.258 0.050 . 1 . . . . . . . . 5480 2 6 . 2 2 1 1 GLN HG2 H 1 2.258 0.050 . 1 . . . . . . . . 5480 2 7 . 2 2 2 2 GLN H H 1 8.449 0.050 . 1 . . . . . . . . 5480 2 8 . 2 2 2 2 GLN HA H 1 4.220 0.050 . 1 . . . . . . . . 5480 2 9 . 2 2 2 2 GLN HB3 H 1 1.991 0.050 . 2 . . . . . . . . 5480 2 10 . 2 2 2 2 GLN HB2 H 1 1.899 0.050 . 2 . . . . . . . . 5480 2 11 . 2 2 2 2 GLN HG3 H 1 2.269 0.050 . 1 . . . . . . . . 5480 2 12 . 2 2 2 2 GLN HG2 H 1 2.269 0.050 . 1 . . . . . . . . 5480 2 13 . 2 2 3 3 ARG H H 1 8.349 0.050 . 1 . . . . . . . . 5480 2 14 . 2 2 3 3 ARG HA H 1 4.245 0.050 . 1 . . . . . . . . 5480 2 15 . 2 2 3 3 ARG HB3 H 1 1.678 0.050 . 2 . . . . . . . . 5480 2 16 . 2 2 3 3 ARG HB2 H 1 1.771 0.050 . 2 . . . . . . . . 5480 2 17 . 2 2 3 3 ARG HG2 H 1 1.536 0.050 . 2 . . . . . . . . 5480 2 18 . 2 2 4 4 ARG H H 1 8.285 0.050 . 1 . . . . . . . . 5480 2 19 . 2 2 4 4 ARG HA H 1 4.311 0.050 . 1 . . . . . . . . 5480 2 20 . 2 2 4 4 ARG HB3 H 1 1.720 0.050 . 2 . . . . . . . . 5480 2 21 . 2 2 4 4 ARG HB2 H 1 1.800 0.050 . 2 . . . . . . . . 5480 2 22 . 2 2 4 4 ARG HG2 H 1 1.560 0.050 . 2 . . . . . . . . 5480 2 23 . 2 2 5 5 GLY H H 1 9.029 0.050 . 1 . . . . . . . . 5480 2 24 . 2 2 5 5 GLY HA3 H 1 3.899 0.050 . 2 . . . . . . . . 5480 2 25 . 2 2 5 5 GLY HA2 H 1 3.991 0.050 . 2 . . . . . . . . 5480 2 26 . 2 2 6 6 GLY H H 1 8.472 0.050 . 1 . . . . . . . . 5480 2 27 . 2 2 6 6 GLY HA3 H 1 3.776 0.050 . 2 . . . . . . . . 5480 2 28 . 2 2 6 6 GLY HA2 H 1 3.945 0.050 . 2 . . . . . . . . 5480 2 29 . 2 2 7 7 PHE H H 1 9.520 0.050 . 1 . . . . . . . . 5480 2 30 . 2 2 7 7 PHE HA H 1 4.580 0.050 . 1 . . . . . . . . 5480 2 31 . 2 2 7 7 PHE HB3 H 1 3.071 0.050 . 2 . . . . . . . . 5480 2 32 . 2 2 7 7 PHE HB2 H 1 3.361 0.050 . 2 . . . . . . . . 5480 2 33 . 2 2 7 7 PHE HD1 H 1 7.227 0.050 . 1 . . . . . . . . 5480 2 34 . 2 2 7 7 PHE HE1 H 1 6.402 0.050 . 1 . . . . . . . . 5480 2 35 . 2 2 7 7 PHE HZ H 1 6.748 0.050 . 1 . . . . . . . . 5480 2 36 . 2 2 7 7 PHE HE2 H 1 6.402 0.050 . 1 . . . . . . . . 5480 2 37 . 2 2 7 7 PHE HD2 H 1 7.227 0.050 . 1 . . . . . . . . 5480 2 38 . 2 2 8 8 ARG H H 1 8.501 0.050 . 1 . . . . . . . . 5480 2 39 . 2 2 8 8 ARG HA H 1 3.510 0.050 . 1 . . . . . . . . 5480 2 40 . 2 2 8 8 ARG HB3 H 1 1.703 0.050 . 2 . . . . . . . . 5480 2 41 . 2 2 8 8 ARG HB2 H 1 1.615 0.050 . 2 . . . . . . . . 5480 2 42 . 2 2 9 9 ARG H H 1 7.712 0.050 . 1 . . . . . . . . 5480 2 43 . 2 2 10 10 ILE H H 1 8.379 0.050 . 1 . . . . . . . . 5480 2 44 . 2 2 10 10 ILE HA H 1 3.979 0.050 . 1 . . . . . . . . 5480 2 45 . 2 2 10 10 ILE HB H 1 1.910 0.050 . 1 . . . . . . . . 5480 2 46 . 2 2 10 10 ILE HG21 H 1 1.153 0.050 . 1 . . . . . . . . 5480 2 47 . 2 2 10 10 ILE HG22 H 1 1.153 0.050 . 1 . . . . . . . . 5480 2 48 . 2 2 10 10 ILE HG23 H 1 1.153 0.050 . 1 . . . . . . . . 5480 2 49 . 2 2 11 11 ALA H H 1 8.882 0.050 . 1 . . . . . . . . 5480 2 50 . 2 2 11 11 ALA HA H 1 4.323 0.050 . 1 . . . . . . . . 5480 2 51 . 2 2 11 11 ALA HB1 H 1 1.365 0.050 . 1 . . . . . . . . 5480 2 52 . 2 2 11 11 ALA HB2 H 1 1.365 0.050 . 1 . . . . . . . . 5480 2 53 . 2 2 11 11 ALA HB3 H 1 1.365 0.050 . 1 . . . . . . . . 5480 2 54 . 2 2 12 12 ARG H H 1 7.913 0.050 . 1 . . . . . . . . 5480 2 55 . 2 2 12 12 ARG HA H 1 4.092 0.050 . 1 . . . . . . . . 5480 2 56 . 2 2 13 13 LEU H H 1 7.706 0.050 . 1 . . . . . . . . 5480 2 57 . 2 2 14 14 VAL H H 1 8.412 0.050 . 1 . . . . . . . . 5480 2 58 . 2 2 14 14 VAL HA H 1 3.535 0.050 . 1 . . . . . . . . 5480 2 59 . 2 2 14 14 VAL HB H 1 2.381 0.050 . 1 . . . . . . . . 5480 2 60 . 2 2 14 14 VAL HG21 H 1 0.894 0.050 . 2 . . . . . . . . 5480 2 61 . 2 2 14 14 VAL HG22 H 1 0.894 0.050 . 2 . . . . . . . . 5480 2 62 . 2 2 14 14 VAL HG23 H 1 0.894 0.050 . 2 . . . . . . . . 5480 2 63 . 2 2 14 14 VAL HG11 H 1 1.087 0.050 . 2 . . . . . . . . 5480 2 64 . 2 2 14 14 VAL HG12 H 1 1.087 0.050 . 2 . . . . . . . . 5480 2 65 . 2 2 14 14 VAL HG13 H 1 1.087 0.050 . 2 . . . . . . . . 5480 2 66 . 2 2 15 15 GLY H H 1 8.142 0.050 . 1 . . . . . . . . 5480 2 67 . 2 2 15 15 GLY HA3 H 1 3.784 0.050 . 2 . . . . . . . . 5480 2 68 . 2 2 15 15 GLY HA2 H 1 3.981 0.050 . 2 . . . . . . . . 5480 2 69 . 2 2 16 16 VAL H H 1 7.978 0.050 . 1 . . . . . . . . 5480 2 70 . 2 2 16 16 VAL HA H 1 3.675 0.050 . 1 . . . . . . . . 5480 2 71 . 2 2 16 16 VAL HB H 1 2.270 0.050 . 1 . . . . . . . . 5480 2 72 . 2 2 16 16 VAL HG21 H 1 1.008 0.050 . 2 . . . . . . . . 5480 2 73 . 2 2 16 16 VAL HG22 H 1 1.008 0.050 . 2 . . . . . . . . 5480 2 74 . 2 2 16 16 VAL HG23 H 1 1.008 0.050 . 2 . . . . . . . . 5480 2 75 . 2 2 16 16 VAL HG11 H 1 0.861 0.050 . 2 . . . . . . . . 5480 2 76 . 2 2 16 16 VAL HG12 H 1 0.861 0.050 . 2 . . . . . . . . 5480 2 77 . 2 2 16 16 VAL HG13 H 1 0.861 0.050 . 2 . . . . . . . . 5480 2 78 . 2 2 17 17 LEU H H 1 8.496 0.050 . 1 . . . . . . . . 5480 2 79 . 2 2 17 17 LEU HA H 1 4.236 0.050 . 1 . . . . . . . . 5480 2 80 . 2 2 17 17 LEU HD11 H 1 1.011 0.050 . 2 . . . . . . . . 5480 2 81 . 2 2 17 17 LEU HD12 H 1 1.011 0.050 . 2 . . . . . . . . 5480 2 82 . 2 2 17 17 LEU HD13 H 1 1.011 0.050 . 2 . . . . . . . . 5480 2 83 . 2 2 17 17 LEU HD21 H 1 0.874 0.050 . 2 . . . . . . . . 5480 2 84 . 2 2 17 17 LEU HD22 H 1 0.874 0.050 . 2 . . . . . . . . 5480 2 85 . 2 2 17 17 LEU HD23 H 1 0.874 0.050 . 2 . . . . . . . . 5480 2 86 . 2 2 18 18 ARG H H 1 8.334 0.050 . 1 . . . . . . . . 5480 2 87 . 2 2 18 18 ARG HA H 1 3.871 0.050 . 1 . . . . . . . . 5480 2 88 . 2 2 19 19 GLU H H 1 7.872 0.050 . 1 . . . . . . . . 5480 2 89 . 2 2 19 19 GLU HA H 1 4.047 0.050 . 1 . . . . . . . . 5480 2 90 . 2 2 19 19 GLU HB3 H 1 1.902 0.050 . 2 . . . . . . . . 5480 2 91 . 2 2 19 19 GLU HB2 H 1 2.116 0.050 . 2 . . . . . . . . 5480 2 92 . 2 2 19 19 GLU HG2 H 1 2.397 0.050 . 2 . . . . . . . . 5480 2 93 . 2 2 20 20 TRP H H 1 8.392 0.050 . 1 . . . . . . . . 5480 2 94 . 2 2 20 20 TRP HA H 1 4.218 0.050 . 1 . . . . . . . . 5480 2 95 . 2 2 20 20 TRP HB3 H 1 3.208 0.050 . 2 . . . . . . . . 5480 2 96 . 2 2 20 20 TRP HB2 H 1 3.480 0.050 . 2 . . . . . . . . 5480 2 97 . 2 2 20 20 TRP HD1 H 1 7.233 0.050 . 1 . . . . . . . . 5480 2 98 . 2 2 20 20 TRP HE1 H 1 9.742 0.050 . 3 . . . . . . . . 5480 2 99 . 2 2 20 20 TRP HZ2 H 1 7.004 0.050 . 3 . . . . . . . . 5480 2 100 . 2 2 20 20 TRP HH2 H 1 6.620 0.050 . 1 . . . . . . . . 5480 2 101 . 2 2 20 20 TRP HZ3 H 1 6.500 0.050 . 3 . . . . . . . . 5480 2 102 . 2 2 20 20 TRP HE3 H 1 7.173 0.050 . 3 . . . . . . . . 5480 2 103 . 2 2 21 21 ALA H H 1 8.010 0.050 . 1 . . . . . . . . 5480 2 104 . 2 2 21 21 ALA HA H 1 3.875 0.050 . 1 . . . . . . . . 5480 2 105 . 2 2 21 21 ALA HB1 H 1 1.169 0.050 . 1 . . . . . . . . 5480 2 106 . 2 2 21 21 ALA HB2 H 1 1.169 0.050 . 1 . . . . . . . . 5480 2 107 . 2 2 21 21 ALA HB3 H 1 1.169 0.050 . 1 . . . . . . . . 5480 2 108 . 2 2 22 22 TYR H H 1 7.847 0.050 . 1 . . . . . . . . 5480 2 109 . 2 2 22 22 TYR HA H 1 4.204 0.050 . 1 . . . . . . . . 5480 2 110 . 2 2 22 22 TYR HB3 H 1 3.002 0.050 . 2 . . . . . . . . 5480 2 111 . 2 2 22 22 TYR HB2 H 1 3.067 0.050 . 2 . . . . . . . . 5480 2 112 . 2 2 22 22 TYR HD1 H 1 7.058 0.050 . 1 . . . . . . . . 5480 2 113 . 2 2 22 22 TYR HE1 H 1 6.695 0.050 . 1 . . . . . . . . 5480 2 114 . 2 2 22 22 TYR HE2 H 1 6.695 0.050 . 1 . . . . . . . . 5480 2 115 . 2 2 22 22 TYR HD2 H 1 7.058 0.050 . 1 . . . . . . . . 5480 2 116 . 2 2 24 24 ASN H H 1 7.816 0.050 . 1 . . . . . . . . 5480 2 117 . 2 2 24 24 ASN HA H 1 4.603 0.050 . 1 . . . . . . . . 5480 2 118 . 2 2 24 24 ASN HB3 H 1 2.324 0.050 . 2 . . . . . . . . 5480 2 119 . 2 2 24 24 ASN HB2 H 1 2.577 0.050 . 2 . . . . . . . . 5480 2 120 . 2 2 25 25 PHE H H 1 7.745 0.050 . 1 . . . . . . . . 5480 2 121 . 2 2 25 25 PHE HA H 1 4.565 0.050 . 1 . . . . . . . . 5480 2 122 . 2 2 25 25 PHE HB3 H 1 2.934 0.050 . 2 . . . . . . . . 5480 2 123 . 2 2 25 25 PHE HB2 H 1 3.105 0.050 . 2 . . . . . . . . 5480 2 124 . 2 2 25 25 PHE HD1 H 1 6.857 0.050 . 3 . . . . . . . . 5480 2 125 . 2 2 26 26 ARG H H 1 7.835 0.050 . 1 . . . . . . . . 5480 2 126 . 2 2 26 26 ARG HA H 1 4.049 0.050 . 1 . . . . . . . . 5480 2 127 . 2 2 26 26 ARG HB3 H 1 1.594 0.050 . 2 . . . . . . . . 5480 2 128 . 2 2 26 26 ARG HB2 H 1 1.735 0.050 . 2 . . . . . . . . 5480 2 129 . 2 2 26 26 ARG HG3 H 1 1.329 0.050 . 2 . . . . . . . . 5480 2 130 . 2 2 26 26 ARG HG2 H 1 1.461 0.050 . 2 . . . . . . . . 5480 2 stop_ save_