data_4978 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4978 _Entry.Title ; NMR assignments for the Ca2+-bound B0 isoform of the C-terminal globular domain of agrin (agrin-G3) ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-03-25 _Entry.Accession_date 2001-03-25 _Entry.Last_release_date 2001-07-30 _Entry.Original_release_date 2001-07-30 _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 Andrei Alexandrescu . T. . 4978 2 Mark Maciejewski . W. . 4978 3 Markus Ruegg . A. . 4978 4 Jurgen Engel . . . 4978 5 Richard Kammerer . A. . 4978 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4978 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 532 4978 '13C chemical shifts' 548 4978 '15N chemical shifts' 193 4978 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-07-30 2001-03-21 original author . 4978 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4978 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 20 _Citation.Journal_issue 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 295 _Citation.Page_last 296 _Citation.Year 2001 _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 Andrei Alexandrescu . T. . 4978 1 2 Mark Maciejewski . W. . 4978 1 3 Markus Ruegg . A. . 4978 1 4 Jurgen Engel . . . 4978 1 5 Richard Kammerer . A. . 4978 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'synapse development' 4978 1 'neuromuscular junction' 4978 1 'AChR clustering' 4978 1 'sequence isoforms' 4978 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4978 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10202544 _Citation.Full_citation ; Sanes, J.R. & Lichtman, J.W. (1999) Development of the vertebrate neuromuscular junction. Annu. Rev. Neurosci 22: 389-442. ; _Citation.Title 'Development of the vertebrate neuromuscular junction.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Annu. Rev. Neurosci.' _Citation.Journal_name_full 'Annual review of neuroscience' _Citation.Journal_volume 22 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN 0147-006X _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 389 _Citation.Page_last 442 _Citation.Year 1999 _Citation.Details ; We describe the formation, maturation, elimination, maintenance, and regeneration of vertebrate neuromuscular junctions (NMJs), the best studied of all synapses. The NMJ forms in a series of steps that involve the exchange of signals among its three cellular components--nerve terminal, muscle fiber, and Schwann cell. Although essentially any motor axon can form NMJs with any muscle fiber, an additional set of cues biases synapse formation in favor of appropriate partners. The NMJ is functional at birth but undergoes numerous alterations postnatally. One step in maturation is the elimination of excess inputs, a competitive process in which the muscle is an intermediary. Once elimination is complete, the NMJ is maintained stably in a dynamic equilibrium that can be perturbed to initiate remodeling. NMJs regenerate following damage to nerve or muscle, but this process differs in fundamental ways from embryonic synaptogenesis. Finally, we consider the extent to which the NMJ is a suitable model for development of neuron-neuron synapses. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 J.R. Sanes J. R. . 4978 2 2 J.W. Lichtman J. W. . 4978 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4978 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1333640 _Citation.Full_citation ; Marx, J. (1992) Getting it together at the synapse. Science 258: 1304-1306. ; _Citation.Title 'Getting it together at the synapse.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Science _Citation.Journal_name_full 'Science (New York, N.Y.)' _Citation.Journal_volume 258 _Citation.Journal_issue 5086 _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 1304 _Citation.Page_last 1306 _Citation.Year 1992 _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 J. Marx J. . . 4978 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4978 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10491152 _Citation.Full_citation ; Hoch, W. (1999) Formation of the neuromuscular junction: agrin and its unusual receptors. Eur. J. Biochem. 265: 1-10. ; _Citation.Title 'Formation of the neuromuscular junction. Agrin and its unusual receptors.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 265 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1 _Citation.Page_last 10 _Citation.Year 1999 _Citation.Details ; Synapses are essential relay stations for the transmission of information between neurones and other cells. An ordered and tightly regulated formation of these structures is crucial for the functioning of the nervous system. The induction of the intensively studied synapse between nerve and muscle is initiated by the binding of neurone-specific isoforms of the basal membrane protein agrin to receptors on the surface of myotubes. Agrin activates a receptor complex that includes the muscle-specific kinase and most likely additional, yet to be identified, components. Receptor activation leads to the aggregation of acetylcholine receptors (AChR) and other proteins of the postsynaptic apparatus. This activation process has unique features which distinguish it from other receptor tyrosine kinases. In particular, the autophosphorylation of the kinase domain, which usually induces the recruitment of adaptor and signalling molecules, is not sufficient for AChR aggregation. Apparently, interactions of the extracellular domain with unknown components are also required for this process. Agrin binds to a second protein complex on the muscle surface known as the dystrophin-associated glycoprotein complex. This binding forms one end of a molecular link between the extracellular matrix and the cytoskeleton. While many components of the machinery triggering postsynaptic differentiation have now been identified, our picture of the molecular pathway causing the redistribution of synaptic proteins is still incomplete. ; 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. Hoch W. . . 4978 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4978 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1329871 _Citation.Full_citation ; McMahan, U.J.Horton, S.E., Werle, M.J., Honig, L.S., Kroger, S., Ruegg, M.A. & Escher, G. (1992) Agrin isoforms and their roles in synaptogenesis. Curr. Opin. Cell Biol. 4: 869-874. ; _Citation.Title 'Agrin isoforms and their role in synaptogenesis.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Curr. Opin. Cell Biol.' _Citation.Journal_name_full 'Current opinion in cell biology' _Citation.Journal_volume 4 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0955-0674 _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 869 _Citation.Page_last 874 _Citation.Year 1992 _Citation.Details ; Agrin is thought to mediate the motor neuron-induced aggregation of synaptic proteins on the surface of muscle fibers at neuromuscular junctions. Recent experiments provide direct evidence in support of this hypothesis, reveal the nature of agrin immunoreactivity at sites other than neuromuscular junctions, and have resulted in findings that are consistent with the possibility that agrin plays a role in synaptogenesis throughout the nervous system. ; 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 U.J. McMahan U. J. . 4978 5 2 S.E. Horton S. E. . 4978 5 3 M.J. Werle M. J. . 4978 5 4 L.S. Honig L. S. . 4978 5 5 S. Kroger S. . . 4978 5 6 M.A. Ruegg M. A. . 4978 5 7 G. Escher G. . . 4978 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4978 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8653788 _Citation.Full_citation ; Gautam, M., Noakes, P.G., Moscoso, L., Rupp, F., Scheller, R.H., & Hall, Z. (1996) Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell 85: 525-535. ; _Citation.Title 'Defective neuromuscular synaptogenesis in agrin-deficient mutant mice.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Cell _Citation.Journal_name_full Cell _Citation.Journal_volume 85 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0092-8674 _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 525 _Citation.Page_last 535 _Citation.Year 1996 _Citation.Details ; During neuromuscular synapse formation, motor axons induce clustering of acetylcholine receptors (AChRs) in the muscle fiber membrane. The protein agrin, originally isolated from the basal lamina of the synaptic cleft, is synthesized and secreted by motoneurons and triggers formation of AChR clusters on cultured myotubes. We show here postsynaptic AChR aggregates are markedly reduced in number, size, and density in muscles of agrin-deficient mutant mice. These results support the hypothesis that agrin is a critical organizer of postsynaptic differentiation does occur in the mutant, suggesting the existence of a second-nerve-derived synaptic organizing signal. In addition, we show that intramuscular nerve branching and presynaptic differentiation are abnormal in the mutant, phenotypes which may reflect either a distinct effect of agrin or impaired retrograde signaling from a defective postsynaptic apparatus. ; 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. Gautam M. . . 4978 6 2 P.G. Noakes P. G. . 4978 6 3 L. Moscoso L. . . 4978 6 4 F. Rupp F. . . 4978 6 5 R.H. Scheller R. H. . 4978 6 6 J.P. Merlie J. P. . 4978 6 7 J.R. Sanes J. R. . 4978 6 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 4978 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9425009 _Citation.Full_citation ; Megeath, L.J. & Fallon, J.R. (1998) Intracellular calcium regulates agrin-induced acetylcholine receptor clustering. J. Neurosci. 18: 672-678. ; _Citation.Title 'Intracellular calcium regulates agrin-induced acetylcholine receptor clustering.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Neurosci.' _Citation.Journal_name_full 'The Journal of neuroscience : the official journal of the Society for Neuroscience' _Citation.Journal_volume 18 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0270-6474 _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 672 _Citation.Page_last 678 _Citation.Year 1998 _Citation.Details ; Agrin is an extracellular matrix protein that directs neuromuscular junction formation. Early signal transduction events in agrin-mediated postsynaptic differentiation include activation of a receptor tyrosine kinase and phosphorylation of acetylcholine receptors (AChRs), but later steps in this pathway are unknown. Here, we have investigated the role of intracellular calcium in agrin-induced AChR clustering on cultured myotubes. Clamping intracellular calcium levels by loading with the fast chelator BAPTA inhibited agrin-induced AChR aggregation. In addition, preexisting AChR aggregates dispersed under these conditions, indicating that the maintenance of AChR clusters is similarly dependent on intracellular calcium fluxes. The decrease in AChR clusters in BAPTA-loaded cells was dose-dependent and reversible, and no change in the number or mobility of AChRs was observed. Clamping intracellular calcium did not block agrin-induced tyrosine phosphorylation of the AChR beta-subunit, indicating that intracellular calcium fluxes are likely to act downstream from or parallel to AChR phosphorylation. Finally, the targets of the intracellular calcium are likely to be close to the calcium source, since agrin-induced AChR clustering was unaffected in cells loaded with EGTA, a slower-binding calcium chelator. These findings distinguish a novel step in the signal transduction mechanism of agrin and raise the possibility that the pathways mediating agrin- and activity-driven changes in synaptic architecture could intersect at the level of intracellular calcium fluxes. ; 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 L.J. Megeath L. J. . 4978 7 2 J.R. Fallon J. R. . 4978 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 4978 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10339611 _Citation.Full_citation ; Donahue, J.E., Berzin, T.M., Rafii, M.S., Glass, D.J., Yancopoulos, G.D., Fallon, J.R., & Stopa, E.G. (1999) Agrin in alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma. Proc. Natl. Acad. Sci. USA 96: 6468-6472. ; _Citation.Title 'Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 96 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 6468 _Citation.Page_last 6472 _Citation.Year 1999 _Citation.Details ; Agrin is a heparan sulfate proteoglycan that is widely expressed in neurons and microvascular basal lamina in the rodent and avian central nervous system. Agrin induces the differentiation of nerve-muscle synapses, but its function in either normal or diseased brains is not known. Alzheimer's disease (AD) is characterized by loss of synapses, changes in microvascular architecture, and formation of neurofibrillary tangles and senile plaques. Here we have asked whether AD causes changes in the distribution and biochemical properties of agrin. Immunostaining of normal, aged human central nervous system revealed that agrin is expressed in neurons in multiple brain areas. Robust agrin immunoreactivity was observed uniformly in the microvascular basal lamina. In AD brains, agrin is highly concentrated in both diffuse and neuritic plaques as well as neurofibrillary tangles; neuronal expression of agrin also was observed. Furthermore, patients with AD had microvascular alterations characterized by thinning and fragmentation of the basal lamina. Detergent extraction and Western blotting showed that virtually all the agrin in normal brain is soluble in 1% SDS. In contrast, a large fraction of the agrin in AD brains is insoluble under these conditions, suggesting that it is tightly associated with beta-amyloid. Together, these data indicate that the agrin abnormalities observed in AD are closely linked to beta-amyloid deposition. These observations suggest that altered agrin expression in the microvasculature and the brain parenchyma contribute to the pathogenesis of AD. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 J.E. Donahue J. E. . 4978 8 2 T.M. Berzin T. M. . 4978 8 3 M.S. Rafii M. S. . 4978 8 4 D.J. Glass D. J. . 4978 8 5 G.D. Yancopoulos G. D. . 4978 8 6 J.R. Fallon J. R. . 4978 8 7 E.G. Stopa E. G. . 4978 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 4978 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10673326 _Citation.Full_citation ; Cotman, S.L., Halfter, W., & Cole G.J. (2000) Agrin binds to b-amyloid (Ab), accelerates Ab fibril formation, and is localized to Ab deposits in Alzheimer's disease brain . Molec. Cell. Neurosci. 15: 183-198. ; _Citation.Title 'Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Cell. Neurosci.' _Citation.Journal_name_full 'Molecular and cellular neurosciences' _Citation.Journal_volume 15 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1044-7431 _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 183 _Citation.Page_last 198 _Citation.Year 2000 _Citation.Details ; Agrin is an extracellular matrix heparan sulfate proteoglycan (HSPG) well known for its role in modulation of the neuromuscular junction during development. Although agrin is one of the major HSPGs of the brain, its function there remains elusive. Here we provide evidence suggesting a possible function for agrin in Alzheimer's disease brain. Agrin protein binds the amyloidogenic peptide Abeta (1-40) in its fibrillar state via a mechanism that involves the heparan sulfate glycosaminoglycan chains of agrin. Furthermore, agrin is able to accelerate Abeta fibril formation and protect Abeta (1-40) from proteolysis, in vitro. Supporting a biological significance for these in vitro data, immunocytochemical studies demonstrate agrin's presence within senile plaques and cerebrovascular amyloid deposits, and agrin immunostained capillaries exhibit pathological alterations in AD brain. These data therefore suggest that agrin may be an important factor in the progression of Abeta peptide aggregation and/or its persistence in Alzheimer's disease brain. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 S.L. Cotman S. L. . 4978 9 2 W. Halfter W. . . 4978 9 3 G.J. Cole G. J. . 4978 9 stop_ save_ save_ref_9 _Citation.Sf_category citations _Citation.Sf_framecode ref_9 _Citation.Entry_ID 4978 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9480764 _Citation.Full_citation ; Beckmann,G., Hanke, J., Bork, P. & Reich, J.G. (1998). Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins. J. Mol. Biol. 275: 725-730. ; _Citation.Title 'Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 275 _Citation.Journal_issue 5 _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 725 _Citation.Page_last 730 _Citation.Year 1998 _Citation.Details ; Using a new method for construction and database searches of sequence consensus strings, we have identified a new superfamily of protein modules comprising laminin G, thrombospondin N and the pentraxin families. The conserved patterns correspond mainly to hydrophobic core residues located in central beta strands of the known three-dimensional structures of two pentraxins, the human C-reactive protein and the serum amyloid P-component. Thus, we predict a similar jellyroll fold for all members of this superfamily. In addition, the conservation of two exposed aspartate residues in the majority of superfamily members suggests hitherto unrecognised functional sites. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 G. Beckmann G. . . 4978 10 2 J. Hanke J. . . 4978 10 3 P. Bork P. . . 4978 10 4 J.G. Reich J. G. . 4978 10 stop_ save_ save_ref_10 _Citation.Sf_category citations _Citation.Sf_framecode ref_10 _Citation.Entry_ID 4978 _Citation.ID 11 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9430625 _Citation.Full_citation ; Denzer, A.J., Schulthess, T., Fauser, C., Schumacher, B., Kammerer, R.A., Engel, J. & Ruegg, M.A. (1998) Electron microscopic structure of agrin and mapping of its binding site in laminin-1. EMBO J 17: 335-343. ; _Citation.Title 'Electron microscopic structure of agrin and mapping of its binding site in laminin-1.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'EMBO J.' _Citation.Journal_name_full 'The EMBO journal' _Citation.Journal_volume 17 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0261-4189 _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 335 _Citation.Page_last 343 _Citation.Year 1998 _Citation.Details ; Agrin is a large, multidomain heparan sulfate proteoglycan that is associated with basement membranes of several tissues. Particular splice variants of agrin are essential for the formation of synaptic structures at the neuromuscular junction. The binding of agrin to laminin appears to be required for its localization to synaptic basal lamina and other basement membranes. Here, electron microscopy was used to determine the structure of agrin and to localize its binding site in laminin-1. Agrin appears as an approximately 95 nm long particle that consists of a globular, N-terminal laminin-binding domain, a central rod predominantly formed by the follistatin-like domains and three globular, C-terminal laminin G-like domains. In a few cases, heparan sulfate glycosaminoglycan chains were seen emerging from the central portion of the core protein. Moreover, we show that agrin binds to the central region of the three-stranded, coiled-coil oligomerization domain in the long arm of laminin-1, which mediates subunit assembly of the native laminin molecule. In summary, our data show for the first time a protein-protein interaction of the extracellular matrix that involves a coiled-coil domain, and they assign a novel role to this domain of laminin-1. Based on this, we propose that agrin associates with basal lamina in a polarized way. ; 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 A.J. Denzer A. J. . 4978 11 2 T. Schulthess T. . . 4978 11 3 C. Fauser C. . . 4978 11 4 B. Schumacher B. . . 4978 11 5 R.A. Kammerer R. A. . 4978 11 6 J. Engel J. . . 4978 11 7 M.A. Ruegg M. A. . 4978 11 stop_ save_ save_ref_11 _Citation.Sf_category citations _Citation.Sf_framecode ref_11 _Citation.Entry_ID 4978 _Citation.ID 12 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8654359 _Citation.Full_citation ; Meier, T., Gessemann, M., Cavalli, V., Ruegg, M.A. & Wallace, B.G. (1996) AChR phophorylation and aggregation induced by an agrin fragment that lacks the binding domain for a-dystroglycan. J. Cell Sci. 112: 1213-1223. ; _Citation.Title 'AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycan.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'EMBO J.' _Citation.Journal_name_full 'The EMBO journal' _Citation.Journal_volume 15 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0261-4189 _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 2625 _Citation.Page_last 2631 _Citation.Year 1996 _Citation.Details ; Agrin induces both phosphorylation and aggregation of nicotinic acetylcholine receptors (AChRs) when added to myotubes in culture, apparently by binding to a specific receptor on the myotube surface. One such agrin receptor is alpha-dystroglycan, although binding to alpha-dystroglycan appears not to mediate AChR aggregation. To determine whether agrin-induced AChR phosphorylation is mediated by alpha-dystroglycan or by a different agrin receptor, fragments of recombinant agrin that differ in affinity for alpha-dystroglycan were examined for their ability to induce AChR phosphorylation and aggregation in mouse C2 myotubes. The carboxy-terminal 95 kDa agrin fragment agrin-c95(A0B0), which binds to alpha-dystroglycan with high affinity, failed to induce AChR phosphorylation and aggregation. In contrast, agrin-c95(A4B8) which binds less strongly to alpha-dystroglycan, induced both phosphorylation and aggregation, as did a small 21 kDa fragment of agrin, agrin-c21(B8), that completely lacks the binding domain for alpha-dystroglycan. We conclude that agrin-induced AChR phosphorylation and aggregation are triggered by an agrin receptor that is distinct from alpha-dystroglycan. ; 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 T. Meier T. . . 4978 12 2 M. Gesemann M. . . 4978 12 3 V. Cavalli V. . . 4978 12 4 M.A. Ruegg M. A. . 4978 12 5 B.G. Wallace B. G. . 4978 12 stop_ save_ save_ref_12 _Citation.Sf_category citations _Citation.Sf_framecode ref_12 _Citation.Entry_ID 4978 _Citation.ID 13 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10619025 _Citation.Full_citation ; Hohenester, E., Tisi, D., Talts, J.F., & Timpl, R. (1999) The crystal structure of a laminin G-like module reveals the molecular basis of a-dystroglycan binding to laminins, perlecan, and agrin. Molecular Cell 4: 783-792. ; _Citation.Title 'The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Cell' _Citation.Journal_name_full 'Molecular cell' _Citation.Journal_volume 4 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1097-2765 _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 783 _Citation.Page_last 792 _Citation.Year 1999 _Citation.Details ; Laminin G-like (LG) modules in the extracellular matrix glycoproteins laminin, perlecan, and agrin mediate the binding to heparin and the cell surface receptor alpha-dystroglycan (alpha-DG). These interactions are crucial to basement membrane assembly, as well as muscle and nerve cell function. The crystal structure of the laminin alpha 2 chain LG5 module reveals a 14-stranded beta sandwich. A calcium ion is bound to one edge of the sandwich by conserved acidic residues and is surrounded by residues implicated in heparin and alpha-DG binding. A calcium-coordinated sulfate ion is suggested to mimic the binding of anionic oligosaccharides. The structure demonstrates a conserved function of the LG module in calcium-dependent lectin-like alpha-DG binding. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 E. Hohenester E. . . 4978 13 2 D. Tisi D. . . 4978 13 3 J.F. Talts J. F. . 4978 13 4 R. Timpl R. . . 4978 13 stop_ save_ save_ref_13 _Citation.Sf_category citations _Citation.Sf_framecode ref_13 _Citation.Entry_ID 4978 _Citation.ID 14 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 2839519 _Citation.Full_citation ; Wallace, B.G. (1988) Regulation of agrin-induced acetylcholine receptor aggregation by Ca++ and phorbol ester, J. Cell Biol. 107: 267-278. ; _Citation.Title 'Regulation of agrin-induced acetylcholine receptor aggregation by Ca++ and phorbol ester.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Cell Biol.' _Citation.Journal_name_full 'The Journal of cell biology' _Citation.Journal_volume 107 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9525 _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 267 _Citation.Page_last 278 _Citation.Year 1988 _Citation.Details ; Agrin, a protein extracted from the electric organ of Torpedo californica, induces the formation of specializations on cultured chick myotubes that resemble the postsynaptic apparatus at the neuromuscular junction. The aim of the studies reported here was to characterize the effects of agrin on the distribution of acetylcholine receptors (AChRs) and cholinesterase as a step toward determining agrin's mechanism of action. When agrin was added to the medium bathing chick myotubes small (less than 4 micron 2) aggregates of AChRs began to appear within 2 h and increased rapidly in number until 4 h. Over the next 12-20 h the number of aggregates per myotube decreased as the mean size of each aggregate increased to approximately 15 micron 2. The accumulation of AChRs into agrin-induced aggregates occurred primarily by lateral migration of AChRs already in the myotube plasma membrane at the time agrin was added to the cultures. Aggregates of AChRs and cholinesterase remained as long as agrin was present in the medium; if agrin was removed the number of aggregates declined slowly. The formation and maintenance of agrin-induced AChR aggregates required Ca++, Co++ and Mn++ inhibited agrin-induced AChR aggregation and increased the rate of aggregate dispersal. Mg++ and Sr++ could not substitute for Ca++. Agrin-induced receptor aggregation also was inhibited by phorbol 12-myristate 13-acetate, an activator of protein kinase C, and by inhibitors of energy metabolism. The similarities between agrin's effects on cultured myotubes and events that occur during formation of neuromuscular junctions support the hypothesis that axon terminals release molecules similar to agrin that induce the differentiation of the postsynaptic apparatus. ; 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.G. Wallace B. G. . 4978 14 stop_ save_ save_ref_14 _Citation.Sf_category citations _Citation.Sf_framecode ref_14 _Citation.Entry_ID 4978 _Citation.ID 15 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8587694 _Citation.Full_citation ; Deyst, K.A., Ma, J. & Fallon, J.R. (1995) Agrin: toward a molecular understanding of synapse regeneration. Neurosurgery 37: 71-77. ; _Citation.Title 'Agrin: toward a molecular understanding of synapse regeneration.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Neurosurgery _Citation.Journal_name_full Neurosurgery _Citation.Journal_volume 37 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0148-396X _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 71 _Citation.Page_last 77 _Citation.Year 1995 _Citation.Details ; One of the foremost challenges to repairing damage after stroke, trauma, or disease is the regeneration of synaptic connections between neurons. Here, we consider recent strides in our understanding of the molecular basis of synapse formation and regeneration. We will focus on the protein agrin, a key player in synaptogenesis at neuromuscular junctions and perhaps at central nervous system synapses as well. Insights into agrin and its receptor could guide the development of rational therapies to combat neuronal degeneration. We will also consider recent surprising and provocative data linking the mechanisms of synapse formation and the cellular pathology in Duchenne muscular dystrophy. ; 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 K.A. Deyst K. A. . 4978 15 2 J. Ma J. . . 4978 15 3 J.R. Fallon J. R. . 4978 15 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_agrin-G3 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_agrin-G3 _Assembly.Entry_ID 4978 _Assembly.ID 1 _Assembly.Name 'B0 isoform of the 3rd(C-terminal) globular domain of agrin' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'oligomeric state was determined by by analytical ultracentrifugation' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4978 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 agrin-G3 1 $agrin_G3_monomer . . . native . . . . . 4978 1 2 'Ca 2+' 2 $CA . . . native . . . . . 4978 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . . CYS 166 166 SG . 1 . 1 CYS 192 192 SG . . . . . . . . . . 4978 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 1QU0 . . . . . ; non-homologus predicted to belong to same fold family as agrin-G3 For the purposes of structural genomics lumping, the agrin G3 domain is predicted to belong to a b-jellyroll fold family that includes laminin G, thrombospondin N, and the pentraxin family. Although sequence homologies within this superfamily are below the 'twilight' threshold, the fold assignment is based on the alignment of hydrophobic consensus strings with conserved hydrophobic residues in the b-strands of the known structures of two pentraxins [1] The closest structural siblings to agrin-G3 are beleived to be the laminin G domains (PDB:1QU0, 1DYK) and the ligand binding domain of neurexin 1-beta (PDB:1C4R) [1] Beckmann,G., Hanke, J., Bork, P. & Reich, J.G. (1998). Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins. J. Mol. Biol. 275: 725-730. ; 4978 1 . PDB 1DYK . . . . . . 4978 1 . PDB 1C4R . . . . . . 4978 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'B0 isoform of the 3rd(C-terminal) globular domain of agrin' system 4978 1 agrin-G3 abbreviation 4978 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'domain acts as a signal to induce aggregation (clustering) of acetylcholine receptors on the postynaptic membrane (muscle) of neuromuscular junctions.' 4978 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_agrin_G3_monomer _Entity.Sf_category entity _Entity.Sf_framecode agrin_G3_monomer _Entity.Entry_ID 4978 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name agrin-G3 _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 ; GSEKVIIEKAAGDAEAIAFD GRTYMEYHNAVTKSEKALQS NHFELSIKTEATQGLILWSG KGLERSDYIALAIVDGFVQM MYDLGSKPVVLRSTVPINTN HWTHIKAYRVQREGSLQVGN EAPITGSSPLGATQLDTDGA LWLGGMERLSVAHKLPKAYS TGFIGCIRDVIVDRQELHLV EDALNNPTILHCSAK ; _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 195 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 21310 _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 1Q56 . "Nmr Structure Of The B0 Isoform Of The Agrin G3 Domain In Its Ca2+ Bound State" . . . . . 100.00 195 100.00 100.00 2.22e-141 . . . . 4978 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID agrin-G3 common 4978 1 agrin-G3 abbreviation 4978 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 . GLY . 4978 1 2 . SER . 4978 1 3 1748 GLU . 4978 1 4 1749 LYS . 4978 1 5 1750 VAL . 4978 1 6 1751 ILE . 4978 1 7 1752 ILE . 4978 1 8 1753 GLU . 4978 1 9 1754 LYS . 4978 1 10 1755 ALA . 4978 1 11 1756 ALA . 4978 1 12 1757 GLY . 4978 1 13 1758 ASP . 4978 1 14 1759 ALA . 4978 1 15 1760 GLU . 4978 1 16 1761 ALA . 4978 1 17 1762 ILE . 4978 1 18 1763 ALA . 4978 1 19 1764 PHE . 4978 1 20 1765 ASP . 4978 1 21 1766 GLY . 4978 1 22 1767 ARG . 4978 1 23 1768 THR . 4978 1 24 1769 TYR . 4978 1 25 1770 MET . 4978 1 26 1771 GLU . 4978 1 27 1772 TYR . 4978 1 28 1773 HIS . 4978 1 29 1774 ASN . 4978 1 30 1775 ALA . 4978 1 31 1776 VAL . 4978 1 32 1777 THR . 4978 1 33 1778 LYS . 4978 1 34 1779 SER . 4978 1 35 1780 GLU . 4978 1 36 1781 LYS . 4978 1 37 1782 ALA . 4978 1 38 1783 LEU . 4978 1 39 1784 GLN . 4978 1 40 1785 SER . 4978 1 41 1786 ASN . 4978 1 42 1787 HIS . 4978 1 43 1788 PHE . 4978 1 44 1789 GLU . 4978 1 45 1790 LEU . 4978 1 46 1791 SER . 4978 1 47 1792 ILE . 4978 1 48 1793 LYS . 4978 1 49 1794 THR . 4978 1 50 1795 GLU . 4978 1 51 1796 ALA . 4978 1 52 1797 THR . 4978 1 53 1798 GLN . 4978 1 54 1799 GLY . 4978 1 55 1800 LEU . 4978 1 56 1801 ILE . 4978 1 57 1802 LEU . 4978 1 58 1803 TRP . 4978 1 59 1804 SER . 4978 1 60 1805 GLY . 4978 1 61 1806 LYS . 4978 1 62 1807 GLY . 4978 1 63 1808 LEU . 4978 1 64 1809 GLU . 4978 1 65 1810 ARG . 4978 1 66 1811 SER . 4978 1 67 1812 ASP . 4978 1 68 1813 TYR . 4978 1 69 1814 ILE . 4978 1 70 1815 ALA . 4978 1 71 1816 LEU . 4978 1 72 1817 ALA . 4978 1 73 1818 ILE . 4978 1 74 1819 VAL . 4978 1 75 1820 ASP . 4978 1 76 1821 GLY . 4978 1 77 1822 PHE . 4978 1 78 1823 VAL . 4978 1 79 1824 GLN . 4978 1 80 1825 MET . 4978 1 81 1826 MET . 4978 1 82 1827 TYR . 4978 1 83 1828 ASP . 4978 1 84 1829 LEU . 4978 1 85 1830 GLY . 4978 1 86 1831 SER . 4978 1 87 1832 LYS . 4978 1 88 1833 PRO . 4978 1 89 1834 VAL . 4978 1 90 1835 VAL . 4978 1 91 1836 LEU . 4978 1 92 1837 ARG . 4978 1 93 1838 SER . 4978 1 94 1839 THR . 4978 1 95 1840 VAL . 4978 1 96 1841 PRO . 4978 1 97 1842 ILE . 4978 1 98 1843 ASN . 4978 1 99 1844 THR . 4978 1 100 1845 ASN . 4978 1 101 1846 HIS . 4978 1 102 1847 TRP . 4978 1 103 1848 THR . 4978 1 104 1849 HIS . 4978 1 105 1850 ILE . 4978 1 106 1851 LYS . 4978 1 107 1852 ALA . 4978 1 108 1853 TYR . 4978 1 109 1854 ARG . 4978 1 110 1855 VAL . 4978 1 111 1856 GLN . 4978 1 112 1857 ARG . 4978 1 113 1858 GLU . 4978 1 114 1859 GLY . 4978 1 115 1860 SER . 4978 1 116 1861 LEU . 4978 1 117 1862 GLN . 4978 1 118 1863 VAL . 4978 1 119 1864 GLY . 4978 1 120 1865 ASN . 4978 1 121 1866 GLU . 4978 1 122 1867 ALA . 4978 1 123 1868 PRO . 4978 1 124 1869 ILE . 4978 1 125 1870 THR . 4978 1 126 1871 GLY . 4978 1 127 1872 SER . 4978 1 128 1873 SER . 4978 1 129 1874 PRO . 4978 1 130 1875 LEU . 4978 1 131 1876 GLY . 4978 1 132 1877 ALA . 4978 1 133 1878 THR . 4978 1 134 1879 GLN . 4978 1 135 1880 LEU . 4978 1 136 1881 ASP . 4978 1 137 1882 THR . 4978 1 138 1883 ASP . 4978 1 139 1884 GLY . 4978 1 140 1885 ALA . 4978 1 141 1886 LEU . 4978 1 142 1887 TRP . 4978 1 143 1888 LEU . 4978 1 144 1889 GLY . 4978 1 145 1890 GLY . 4978 1 146 1891 MET . 4978 1 147 1892 GLU . 4978 1 148 1893 ARG . 4978 1 149 1894 LEU . 4978 1 150 1895 SER . 4978 1 151 1896 VAL . 4978 1 152 1897 ALA . 4978 1 153 1898 HIS . 4978 1 154 1899 LYS . 4978 1 155 1900 LEU . 4978 1 156 1901 PRO . 4978 1 157 1902 LYS . 4978 1 158 1903 ALA . 4978 1 159 1904 TYR . 4978 1 160 1905 SER . 4978 1 161 1906 THR . 4978 1 162 1907 GLY . 4978 1 163 1908 PHE . 4978 1 164 1909 ILE . 4978 1 165 1910 GLY . 4978 1 166 1911 CYS . 4978 1 167 1912 ILE . 4978 1 168 1913 ARG . 4978 1 169 1914 ASP . 4978 1 170 1915 VAL . 4978 1 171 1916 ILE . 4978 1 172 1917 VAL . 4978 1 173 1918 ASP . 4978 1 174 1919 ARG . 4978 1 175 1920 GLN . 4978 1 176 1921 GLU . 4978 1 177 1922 LEU . 4978 1 178 1923 HIS . 4978 1 179 1924 LEU . 4978 1 180 1925 VAL . 4978 1 181 1926 GLU . 4978 1 182 1927 ASP . 4978 1 183 1928 ALA . 4978 1 184 1929 LEU . 4978 1 185 1930 ASN . 4978 1 186 1931 ASN . 4978 1 187 1932 PRO . 4978 1 188 1933 THR . 4978 1 189 1934 ILE . 4978 1 190 1935 LEU . 4978 1 191 1936 HIS . 4978 1 192 1937 CYS . 4978 1 193 1938 SER . 4978 1 194 1939 ALA . 4978 1 195 1940 LYS . 4978 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 . GLY 1 1 4978 1 . SER 2 2 4978 1 . GLU 3 3 4978 1 . LYS 4 4 4978 1 . VAL 5 5 4978 1 . ILE 6 6 4978 1 . ILE 7 7 4978 1 . GLU 8 8 4978 1 . LYS 9 9 4978 1 . ALA 10 10 4978 1 . ALA 11 11 4978 1 . GLY 12 12 4978 1 . ASP 13 13 4978 1 . ALA 14 14 4978 1 . GLU 15 15 4978 1 . ALA 16 16 4978 1 . ILE 17 17 4978 1 . ALA 18 18 4978 1 . PHE 19 19 4978 1 . ASP 20 20 4978 1 . GLY 21 21 4978 1 . ARG 22 22 4978 1 . THR 23 23 4978 1 . TYR 24 24 4978 1 . MET 25 25 4978 1 . GLU 26 26 4978 1 . TYR 27 27 4978 1 . HIS 28 28 4978 1 . ASN 29 29 4978 1 . ALA 30 30 4978 1 . VAL 31 31 4978 1 . THR 32 32 4978 1 . LYS 33 33 4978 1 . SER 34 34 4978 1 . GLU 35 35 4978 1 . LYS 36 36 4978 1 . ALA 37 37 4978 1 . LEU 38 38 4978 1 . GLN 39 39 4978 1 . SER 40 40 4978 1 . ASN 41 41 4978 1 . HIS 42 42 4978 1 . PHE 43 43 4978 1 . GLU 44 44 4978 1 . LEU 45 45 4978 1 . SER 46 46 4978 1 . ILE 47 47 4978 1 . LYS 48 48 4978 1 . THR 49 49 4978 1 . GLU 50 50 4978 1 . ALA 51 51 4978 1 . THR 52 52 4978 1 . GLN 53 53 4978 1 . GLY 54 54 4978 1 . LEU 55 55 4978 1 . ILE 56 56 4978 1 . LEU 57 57 4978 1 . TRP 58 58 4978 1 . SER 59 59 4978 1 . GLY 60 60 4978 1 . LYS 61 61 4978 1 . GLY 62 62 4978 1 . LEU 63 63 4978 1 . GLU 64 64 4978 1 . ARG 65 65 4978 1 . SER 66 66 4978 1 . ASP 67 67 4978 1 . TYR 68 68 4978 1 . ILE 69 69 4978 1 . ALA 70 70 4978 1 . LEU 71 71 4978 1 . ALA 72 72 4978 1 . ILE 73 73 4978 1 . VAL 74 74 4978 1 . ASP 75 75 4978 1 . GLY 76 76 4978 1 . PHE 77 77 4978 1 . VAL 78 78 4978 1 . GLN 79 79 4978 1 . MET 80 80 4978 1 . MET 81 81 4978 1 . TYR 82 82 4978 1 . ASP 83 83 4978 1 . LEU 84 84 4978 1 . GLY 85 85 4978 1 . SER 86 86 4978 1 . LYS 87 87 4978 1 . PRO 88 88 4978 1 . VAL 89 89 4978 1 . VAL 90 90 4978 1 . LEU 91 91 4978 1 . ARG 92 92 4978 1 . SER 93 93 4978 1 . THR 94 94 4978 1 . VAL 95 95 4978 1 . PRO 96 96 4978 1 . ILE 97 97 4978 1 . ASN 98 98 4978 1 . THR 99 99 4978 1 . ASN 100 100 4978 1 . HIS 101 101 4978 1 . TRP 102 102 4978 1 . THR 103 103 4978 1 . HIS 104 104 4978 1 . ILE 105 105 4978 1 . LYS 106 106 4978 1 . ALA 107 107 4978 1 . TYR 108 108 4978 1 . ARG 109 109 4978 1 . VAL 110 110 4978 1 . GLN 111 111 4978 1 . ARG 112 112 4978 1 . GLU 113 113 4978 1 . GLY 114 114 4978 1 . SER 115 115 4978 1 . LEU 116 116 4978 1 . GLN 117 117 4978 1 . VAL 118 118 4978 1 . GLY 119 119 4978 1 . ASN 120 120 4978 1 . GLU 121 121 4978 1 . ALA 122 122 4978 1 . PRO 123 123 4978 1 . ILE 124 124 4978 1 . THR 125 125 4978 1 . GLY 126 126 4978 1 . SER 127 127 4978 1 . SER 128 128 4978 1 . PRO 129 129 4978 1 . LEU 130 130 4978 1 . GLY 131 131 4978 1 . ALA 132 132 4978 1 . THR 133 133 4978 1 . GLN 134 134 4978 1 . LEU 135 135 4978 1 . ASP 136 136 4978 1 . THR 137 137 4978 1 . ASP 138 138 4978 1 . GLY 139 139 4978 1 . ALA 140 140 4978 1 . LEU 141 141 4978 1 . TRP 142 142 4978 1 . LEU 143 143 4978 1 . GLY 144 144 4978 1 . GLY 145 145 4978 1 . MET 146 146 4978 1 . GLU 147 147 4978 1 . ARG 148 148 4978 1 . LEU 149 149 4978 1 . SER 150 150 4978 1 . VAL 151 151 4978 1 . ALA 152 152 4978 1 . HIS 153 153 4978 1 . LYS 154 154 4978 1 . LEU 155 155 4978 1 . PRO 156 156 4978 1 . LYS 157 157 4978 1 . ALA 158 158 4978 1 . TYR 159 159 4978 1 . SER 160 160 4978 1 . THR 161 161 4978 1 . GLY 162 162 4978 1 . PHE 163 163 4978 1 . ILE 164 164 4978 1 . GLY 165 165 4978 1 . CYS 166 166 4978 1 . ILE 167 167 4978 1 . ARG 168 168 4978 1 . ASP 169 169 4978 1 . VAL 170 170 4978 1 . ILE 171 171 4978 1 . VAL 172 172 4978 1 . ASP 173 173 4978 1 . ARG 174 174 4978 1 . GLN 175 175 4978 1 . GLU 176 176 4978 1 . LEU 177 177 4978 1 . HIS 178 178 4978 1 . LEU 179 179 4978 1 . VAL 180 180 4978 1 . GLU 181 181 4978 1 . ASP 182 182 4978 1 . ALA 183 183 4978 1 . LEU 184 184 4978 1 . ASN 185 185 4978 1 . ASN 186 186 4978 1 . PRO 187 187 4978 1 . THR 188 188 4978 1 . ILE 189 189 4978 1 . LEU 190 190 4978 1 . HIS 191 191 4978 1 . CYS 192 192 4978 1 . SER 193 193 4978 1 . ALA 194 194 4978 1 . LYS 195 195 4978 1 stop_ save_ save_CA _Entity.Sf_category entity _Entity.Sf_framecode CA _Entity.Entry_ID 4978 _Entity.ID 2 _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 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . CA . 4978 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4978 _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 $agrin_G3_monomer . 9031 organism . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 4978 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 4978 _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 $agrin_G3_monomer . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli JM109 . . . . . . . . . . . . plasmid . . 'pGSTHis: a derivative of pGEX-1 (Amersham Pharmacia Biotech) that contains a 6xHis tag followed by a thrombin cleavage site between the gluthathione S-transferase (GST) carrier protein and the agrin-G3 domain.' . . . ; The recombinant agrin-G3 domain corresponds to residues 1748-1940 of the B0 mRNA alternative splice variant of the C-terminal globular domain of chicken agrin. The sequence is given in SWISS-PROT under accession number P31696. This sequence corresponds to the "B11" isoform of the agrin G3 domain. To obtain the sequence of the BO isoform of agrin-G3 for which NMR assignments are reported -> follow the hyperlink "Agrin related protein 2" under "VARSPLIC 1783 1793" Residues 1748-1940 of the sequence you arrive at from this hyperlink correspond to residues 3-195 of the agrin-G3 domain studied by NMR. The first two residues of the agrin-G3 domain for which NMR assignments are reported, GS, are a cloning artifact (part of a thrombin cleavage site used to separate agrin-G3 from the GST carrier protein used in the recombinant fusion protein). ; . . 4978 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 4978 _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 4978 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 4978 CA [Ca++] SMILES CACTVS 3.341 4978 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4978 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 4978 CA InChI=1S/Ca/q+2 InChI InChI 1.03 4978 CA BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 4978 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 4978 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4978 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 . 4978 CA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4978 _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 agrin-G3 '[U-13C; U-15N; U-90% 2H]' . . 1 $agrin_G3_monomer . . 1.0 . . mM . . . . 4978 1 2 CaCl2 . . . . . . . 4 . . mM . . . . 4978 1 3 immidazole . . . . . . . 10 . . mM . . . . 4978 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4978 _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 agrin-G3 [U-15N] . . 1 $agrin_G3_monomer . . 1.0 . . mM . . . . 4978 2 2 CaCl2 . . . . . . . 4 . . mM . . . . 4978 2 3 immidazole . . . . . . . 10 . . mM . . . . 4978 2 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-Cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-Cond_1 _Sample_condition_list.Entry_ID 4978 _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 6.5 0.1 n/a 4978 1 temperature 298 1 K 4978 1 pressure 1 . atm 4978 1 stop_ save_ save_Ex-Cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-Cond_2 _Sample_condition_list.Entry_ID 4978 _Sample_condition_list.ID 2 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.1 0.1 n/a 4978 2 temperature 298 1 K 4978 2 pressure 1 . atm 4978 2 stop_ 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 4978 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4978 _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 Varian INOVA . 600 . . . 4978 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 4978 _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 '3D HSQC-NOESY-HSQC (200 ms mix time)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 1 2 'deuterium-decoupled TROSY versions of:' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 1 3 '3D HNCACB' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 1 4 HNCO . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 1 5 HN(CA)CO . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 1 6 '3D 15N TOCSY-HSQC (39 ms mix time)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 1 7 '3D 15N NOESY-HSQC (100 mix time)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4978 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 4978 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '3D HSQC-NOESY-HSQC (200 ms mix time)' _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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name 'deuterium-decoupled TROSY versions of:' _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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D HNCACB' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _NMR_spec_expt.ID 4 _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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HN(CA)CO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '3D 15N TOCSY-HSQC (39 ms mix time)' _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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '3D 15N NOESY-HSQC (100 mix time)' _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 'NMR spectrometer of UCONN Health Center @ Farmington' 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 4978 _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 . . . . . . . . . 4978 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4978 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4978 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_agrin_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode agrin_shifts _Assigned_chem_shift_list.Entry_ID 4978 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-Cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; All aliphatic proton chemical shifts were obtained from a 15N labeled sample. All other chemical shifts were obtained from a 2H/13C/15N labled sample and the values reported are not corrected for 2H isotope effects. ; _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 . 4978 1 . . 2 $sample_2 . 4978 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 SER C C 13 174.31 0.15 . 1 . . . . . . . . 4978 1 2 . 1 1 2 2 SER CA C 13 57.66 0.25 . 1 . . . . . . . . 4978 1 3 . 1 1 2 2 SER CB C 13 62.81 0.25 . 1 . . . . . . . . 4978 1 4 . 1 1 3 3 GLU H H 1 8.66 0.03 . 1 . . . . . . . . 4978 1 5 . 1 1 3 3 GLU HA H 1 4.25 0.07 . 1 . . . . . . . . 4978 1 6 . 1 1 3 3 GLU HB2 H 1 1.91 0.07 . 2 . . . . . . . . 4978 1 7 . 1 1 3 3 GLU C C 13 176.28 0.15 . 1 . . . . . . . . 4978 1 8 . 1 1 3 3 GLU CA C 13 56.02 0.25 . 1 . . . . . . . . 4978 1 9 . 1 1 3 3 GLU CB C 13 28.59 0.25 . 1 . . . . . . . . 4978 1 10 . 1 1 3 3 GLU N N 15 123.75 0.10 . 1 . . . . . . . . 4978 1 11 . 1 1 4 4 LYS H H 1 8.27 0.03 . 1 . . . . . . . . 4978 1 12 . 1 1 4 4 LYS HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 13 . 1 1 4 4 LYS HB2 H 1 1.65 0.07 . 2 . . . . . . . . 4978 1 14 . 1 1 4 4 LYS C C 13 176.14 0.15 . 1 . . . . . . . . 4978 1 15 . 1 1 4 4 LYS CA C 13 55.55 0.25 . 1 . . . . . . . . 4978 1 16 . 1 1 4 4 LYS CB C 13 31.63 0.25 . 1 . . . . . . . . 4978 1 17 . 1 1 4 4 LYS N N 15 123.22 0.10 . 1 . . . . . . . . 4978 1 18 . 1 1 5 5 VAL H H 1 8.10 0.03 . 1 . . . . . . . . 4978 1 19 . 1 1 5 5 VAL HA H 1 4.05 0.07 . 1 . . . . . . . . 4978 1 20 . 1 1 5 5 VAL HB H 1 1.90 0.07 . 1 . . . . . . . . 4978 1 21 . 1 1 5 5 VAL HG11 H 1 0.80 0.07 . 2 . . . . . . . . 4978 1 22 . 1 1 5 5 VAL HG12 H 1 0.80 0.07 . 2 . . . . . . . . 4978 1 23 . 1 1 5 5 VAL HG13 H 1 0.80 0.07 . 2 . . . . . . . . 4978 1 24 . 1 1 5 5 VAL C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 25 . 1 1 5 5 VAL CA C 13 61.64 0.25 . 1 . . . . . . . . 4978 1 26 . 1 1 5 5 VAL CB C 13 31.63 0.25 . 1 . . . . . . . . 4978 1 27 . 1 1 5 5 VAL N N 15 123.47 0.10 . 1 . . . . . . . . 4978 1 28 . 1 1 6 6 ILE H H 1 8.25 0.03 . 1 . . . . . . . . 4978 1 29 . 1 1 6 6 ILE HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 30 . 1 1 6 6 ILE HB H 1 1.75 0.07 . 1 . . . . . . . . 4978 1 31 . 1 1 6 6 ILE C C 13 175.86 0.15 . 1 . . . . . . . . 4978 1 32 . 1 1 6 6 ILE CA C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 33 . 1 1 6 6 ILE CB C 13 37.26 0.25 . 1 . . . . . . . . 4978 1 34 . 1 1 6 6 ILE N N 15 126.83 0.10 . 1 . . . . . . . . 4978 1 35 . 1 1 7 7 ILE H H 1 8.20 0.03 . 1 . . . . . . . . 4978 1 36 . 1 1 7 7 ILE HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 37 . 1 1 7 7 ILE HB H 1 1.83 0.07 . 1 . . . . . . . . 4978 1 38 . 1 1 7 7 ILE C C 13 175.86 0.15 . 1 . . . . . . . . 4978 1 39 . 1 1 7 7 ILE CA C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 40 . 1 1 7 7 ILE CB C 13 37.26 0.25 . 1 . . . . . . . . 4978 1 41 . 1 1 7 7 ILE N N 15 127.01 0.10 . 1 . . . . . . . . 4978 1 42 . 1 1 8 8 GLU H H 1 8.42 0.03 . 1 . . . . . . . . 4978 1 43 . 1 1 8 8 GLU C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 44 . 1 1 8 8 GLU CA C 13 55.78 0.25 . 1 . . . . . . . . 4978 1 45 . 1 1 8 8 GLU CB C 13 29.30 0.25 . 1 . . . . . . . . 4978 1 46 . 1 1 8 8 GLU N N 15 126.70 0.10 . 1 . . . . . . . . 4978 1 47 . 1 1 9 9 LYS H H 1 8.30 0.03 . 1 . . . . . . . . 4978 1 48 . 1 1 9 9 LYS HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 49 . 1 1 9 9 LYS C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 50 . 1 1 9 9 LYS CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 51 . 1 1 9 9 LYS CB C 13 31.87 0.25 . 1 . . . . . . . . 4978 1 52 . 1 1 9 9 LYS N N 15 123.93 0.10 . 1 . . . . . . . . 4978 1 53 . 1 1 10 10 ALA H H 1 8.36 0.03 . 1 . . . . . . . . 4978 1 54 . 1 1 10 10 ALA HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 55 . 1 1 10 10 ALA HB1 H 1 1.35 0.07 . 1 . . . . . . . . 4978 1 56 . 1 1 10 10 ALA HB2 H 1 1.35 0.07 . 1 . . . . . . . . 4978 1 57 . 1 1 10 10 ALA HB3 H 1 1.35 0.07 . 1 . . . . . . . . 4978 1 58 . 1 1 10 10 ALA C C 13 177.55 0.15 . 1 . . . . . . . . 4978 1 59 . 1 1 10 10 ALA CA C 13 51.56 0.25 . 1 . . . . . . . . 4978 1 60 . 1 1 10 10 ALA CB C 13 18.04 0.25 . 1 . . . . . . . . 4978 1 61 . 1 1 10 10 ALA N N 15 126.77 0.10 . 1 . . . . . . . . 4978 1 62 . 1 1 11 11 ALA H H 1 8.29 0.03 . 1 . . . . . . . . 4978 1 63 . 1 1 11 11 ALA HA H 1 4.31 0.07 . 1 . . . . . . . . 4978 1 64 . 1 1 11 11 ALA HB1 H 1 1.29 0.07 . 1 . . . . . . . . 4978 1 65 . 1 1 11 11 ALA HB2 H 1 1.29 0.07 . 1 . . . . . . . . 4978 1 66 . 1 1 11 11 ALA HB3 H 1 1.29 0.07 . 1 . . . . . . . . 4978 1 67 . 1 1 11 11 ALA C C 13 178.39 0.15 . 1 . . . . . . . . 4978 1 68 . 1 1 11 11 ALA CA C 13 51.80 0.25 . 1 . . . . . . . . 4978 1 69 . 1 1 11 11 ALA CB C 13 18.04 0.25 . 1 . . . . . . . . 4978 1 70 . 1 1 11 11 ALA N N 15 124.48 0.10 . 1 . . . . . . . . 4978 1 71 . 1 1 12 12 GLY H H 1 8.27 0.03 . 1 . . . . . . . . 4978 1 72 . 1 1 12 12 GLY HA2 H 1 3.91 0.07 . 2 . . . . . . . . 4978 1 73 . 1 1 12 12 GLY C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 74 . 1 1 12 12 GLY CA C 13 44.53 0.25 . 1 . . . . . . . . 4978 1 75 . 1 1 12 12 GLY N N 15 108.63 0.10 . 1 . . . . . . . . 4978 1 76 . 1 1 13 13 ASP H H 1 8.20 0.03 . 1 . . . . . . . . 4978 1 77 . 1 1 13 13 ASP HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 78 . 1 1 13 13 ASP HB2 H 1 2.55 0.07 . 2 . . . . . . . . 4978 1 79 . 1 1 13 13 ASP C C 13 176.28 0.15 . 1 . . . . . . . . 4978 1 80 . 1 1 13 13 ASP CA C 13 54.14 0.25 . 1 . . . . . . . . 4978 1 81 . 1 1 13 13 ASP CB C 13 40.31 0.25 . 1 . . . . . . . . 4978 1 82 . 1 1 13 13 ASP N N 15 121.52 0.10 . 1 . . . . . . . . 4978 1 83 . 1 1 14 14 ALA H H 1 8.17 0.03 . 1 . . . . . . . . 4978 1 84 . 1 1 14 14 ALA HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 85 . 1 1 14 14 ALA HB1 H 1 1.30 0.07 . 1 . . . . . . . . 4978 1 86 . 1 1 14 14 ALA HB2 H 1 1.30 0.07 . 1 . . . . . . . . 4978 1 87 . 1 1 14 14 ALA HB3 H 1 1.30 0.07 . 1 . . . . . . . . 4978 1 88 . 1 1 14 14 ALA C C 13 177.69 0.15 . 1 . . . . . . . . 4978 1 89 . 1 1 14 14 ALA CA C 13 51.79 0.25 . 1 . . . . . . . . 4978 1 90 . 1 1 14 14 ALA CB C 13 18.04 0.25 . 1 . . . . . . . . 4978 1 91 . 1 1 14 14 ALA N N 15 124.21 0.10 . 1 . . . . . . . . 4978 1 92 . 1 1 15 15 GLU H H 1 8.22 0.03 . 1 . . . . . . . . 4978 1 93 . 1 1 15 15 GLU HA H 1 4.26 0.07 . 1 . . . . . . . . 4978 1 94 . 1 1 15 15 GLU HB2 H 1 1.93 0.07 . 2 . . . . . . . . 4978 1 95 . 1 1 15 15 GLU C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 96 . 1 1 15 15 GLU CA C 13 56.02 0.25 . 1 . . . . . . . . 4978 1 97 . 1 1 15 15 GLU CB C 13 29.06 0.25 . 1 . . . . . . . . 4978 1 98 . 1 1 15 15 GLU N N 15 119.60 0.10 . 1 . . . . . . . . 4978 1 99 . 1 1 16 16 ALA H H 1 8.22 0.03 . 1 . . . . . . . . 4978 1 100 . 1 1 16 16 ALA HA H 1 4.99 0.07 . 1 . . . . . . . . 4978 1 101 . 1 1 16 16 ALA HB1 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 102 . 1 1 16 16 ALA HB2 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 103 . 1 1 16 16 ALA HB3 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 104 . 1 1 16 16 ALA C C 13 176.56 0.15 . 1 . . . . . . . . 4978 1 105 . 1 1 16 16 ALA CA C 13 50.39 0.25 . 1 . . . . . . . . 4978 1 106 . 1 1 16 16 ALA CB C 13 20.62 0.25 . 1 . . . . . . . . 4978 1 107 . 1 1 16 16 ALA N N 15 124.77 0.10 . 1 . . . . . . . . 4978 1 108 . 1 1 17 17 ILE H H 1 8.55 0.03 . 1 . . . . . . . . 4978 1 109 . 1 1 17 17 ILE HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 110 . 1 1 17 17 ILE C C 13 174.60 0.15 . 1 . . . . . . . . 4978 1 111 . 1 1 17 17 ILE CA C 13 57.89 0.25 . 1 . . . . . . . . 4978 1 112 . 1 1 17 17 ILE CB C 13 37.49 0.25 . 1 . . . . . . . . 4978 1 113 . 1 1 17 17 ILE N N 15 123.89 0.10 . 1 . . . . . . . . 4978 1 114 . 1 1 18 18 ALA H H 1 8.33 0.03 . 1 . . . . . . . . 4978 1 115 . 1 1 18 18 ALA HA H 1 5.17 0.07 . 1 . . . . . . . . 4978 1 116 . 1 1 18 18 ALA HB1 H 1 1.11 0.07 . 1 . . . . . . . . 4978 1 117 . 1 1 18 18 ALA HB2 H 1 1.11 0.07 . 1 . . . . . . . . 4978 1 118 . 1 1 18 18 ALA HB3 H 1 1.11 0.07 . 1 . . . . . . . . 4978 1 119 . 1 1 18 18 ALA C C 13 175.16 0.15 . 1 . . . . . . . . 4978 1 120 . 1 1 18 18 ALA CA C 13 50.16 0.25 . 1 . . . . . . . . 4978 1 121 . 1 1 18 18 ALA CB C 13 20.39 0.25 . 1 . . . . . . . . 4978 1 122 . 1 1 18 18 ALA N N 15 127.51 0.10 . 1 . . . . . . . . 4978 1 123 . 1 1 19 19 PHE H H 1 8.95 0.03 . 1 . . . . . . . . 4978 1 124 . 1 1 19 19 PHE HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 125 . 1 1 19 19 PHE HB2 H 1 2.77 0.07 . 2 . . . . . . . . 4978 1 126 . 1 1 19 19 PHE C C 13 176.71 0.15 . 1 . . . . . . . . 4978 1 127 . 1 1 19 19 PHE CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 128 . 1 1 19 19 PHE CB C 13 40.31 0.25 . 1 . . . . . . . . 4978 1 129 . 1 1 19 19 PHE N N 15 118.73 0.10 . 1 . . . . . . . . 4978 1 130 . 1 1 20 20 ASP H H 1 8.03 0.03 . 1 . . . . . . . . 4978 1 131 . 1 1 20 20 ASP HA H 1 4.53 0.07 . 1 . . . . . . . . 4978 1 132 . 1 1 20 20 ASP HB2 H 1 3.19 0.07 . 2 . . . . . . . . 4978 1 133 . 1 1 20 20 ASP C C 13 176.42 0.15 . 1 . . . . . . . . 4978 1 134 . 1 1 20 20 ASP CA C 13 52.50 0.25 . 1 . . . . . . . . 4978 1 135 . 1 1 20 20 ASP CB C 13 40.31 0.25 . 1 . . . . . . . . 4978 1 136 . 1 1 20 20 ASP N N 15 123.29 0.10 . 1 . . . . . . . . 4978 1 137 . 1 1 21 21 GLY H H 1 7.83 0.03 . 1 . . . . . . . . 4978 1 138 . 1 1 21 21 GLY HA2 H 1 3.11 0.07 . 2 . . . . . . . . 4978 1 139 . 1 1 21 21 GLY HA3 H 1 4.24 0.07 . 2 . . . . . . . . 4978 1 140 . 1 1 21 21 GLY C C 13 173.47 0.15 . 1 . . . . . . . . 4978 1 141 . 1 1 21 21 GLY CA C 13 45.23 0.25 . 1 . . . . . . . . 4978 1 142 . 1 1 21 21 GLY N N 15 112.98 0.10 . 1 . . . . . . . . 4978 1 143 . 1 1 22 22 ARG H H 1 8.07 0.03 . 1 . . . . . . . . 4978 1 144 . 1 1 22 22 ARG HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 145 . 1 1 22 22 ARG HB2 H 1 1.47 0.07 . 2 . . . . . . . . 4978 1 146 . 1 1 22 22 ARG C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 147 . 1 1 22 22 ARG CA C 13 53.44 0.25 . 1 . . . . . . . . 4978 1 148 . 1 1 22 22 ARG CB C 13 29.06 0.25 . 1 . . . . . . . . 4978 1 149 . 1 1 22 22 ARG N N 15 120.12 0.10 . 1 . . . . . . . . 4978 1 150 . 1 1 23 23 THR H H 1 7.79 0.03 . 1 . . . . . . . . 4978 1 151 . 1 1 23 23 THR HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 152 . 1 1 23 23 THR HB H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 153 . 1 1 23 23 THR HG21 H 1 1.04 0.07 . 1 . . . . . . . . 4978 1 154 . 1 1 23 23 THR HG22 H 1 1.04 0.07 . 1 . . . . . . . . 4978 1 155 . 1 1 23 23 THR HG23 H 1 1.04 0.07 . 1 . . . . . . . . 4978 1 156 . 1 1 23 23 THR C C 13 171.22 0.15 . 1 . . . . . . . . 4978 1 157 . 1 1 23 23 THR CA C 13 61.87 0.25 . 1 . . . . . . . . 4978 1 158 . 1 1 23 23 THR CB C 13 69.61 0.25 . 1 . . . . . . . . 4978 1 159 . 1 1 23 23 THR N N 15 119.47 0.10 . 1 . . . . . . . . 4978 1 160 . 1 1 24 24 TYR H H 1 7.89 0.03 . 1 . . . . . . . . 4978 1 161 . 1 1 24 24 TYR HA H 1 5.62 0.07 . 1 . . . . . . . . 4978 1 162 . 1 1 24 24 TYR C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 163 . 1 1 24 24 TYR CA C 13 52.97 0.25 . 1 . . . . . . . . 4978 1 164 . 1 1 24 24 TYR CB C 13 37.73 0.25 . 1 . . . . . . . . 4978 1 165 . 1 1 24 24 TYR N N 15 127.09 0.10 . 1 . . . . . . . . 4978 1 166 . 1 1 25 25 MET H H 1 8.94 0.03 . 1 . . . . . . . . 4978 1 167 . 1 1 25 25 MET C C 13 176.42 0.15 . 1 . . . . . . . . 4978 1 168 . 1 1 25 25 MET CB C 13 33.28 0.25 . 1 . . . . . . . . 4978 1 169 . 1 1 25 25 MET N N 15 115.43 0.10 . 1 . . . . . . . . 4978 1 170 . 1 1 26 26 GLU H H 1 8.71 0.03 . 1 . . . . . . . . 4978 1 171 . 1 1 26 26 GLU HA H 1 4.73 0.07 . 1 . . . . . . . . 4978 1 172 . 1 1 26 26 GLU C C 13 173.05 0.15 . 1 . . . . . . . . 4978 1 173 . 1 1 26 26 GLU CA C 13 53.90 0.25 . 1 . . . . . . . . 4978 1 174 . 1 1 26 26 GLU CB C 13 29.76 0.25 . 1 . . . . . . . . 4978 1 175 . 1 1 26 26 GLU N N 15 120.52 0.10 . 1 . . . . . . . . 4978 1 176 . 1 1 27 27 TYR H H 1 8.85 0.03 . 1 . . . . . . . . 4978 1 177 . 1 1 27 27 TYR HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 178 . 1 1 27 27 TYR HB2 H 1 2.37 0.07 . 2 . . . . . . . . 4978 1 179 . 1 1 27 27 TYR C C 13 177.41 0.15 . 1 . . . . . . . . 4978 1 180 . 1 1 27 27 TYR CA C 13 55.78 0.25 . 1 . . . . . . . . 4978 1 181 . 1 1 27 27 TYR CB C 13 40.55 0.25 . 1 . . . . . . . . 4978 1 182 . 1 1 27 27 TYR N N 15 123.05 0.10 . 1 . . . . . . . . 4978 1 183 . 1 1 28 28 HIS H H 1 9.62 0.03 . 1 . . . . . . . . 4978 1 184 . 1 1 28 28 HIS HA H 1 5.53 0.07 . 1 . . . . . . . . 4978 1 185 . 1 1 28 28 HIS C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 186 . 1 1 28 28 HIS CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 187 . 1 1 28 28 HIS CB C 13 28.12 0.25 . 1 . . . . . . . . 4978 1 188 . 1 1 28 28 HIS N N 15 121.23 0.10 . 1 . . . . . . . . 4978 1 189 . 1 1 29 29 ASN H H 1 8.87 0.03 . 1 . . . . . . . . 4978 1 190 . 1 1 29 29 ASN HA H 1 5.71 0.07 . 1 . . . . . . . . 4978 1 191 . 1 1 29 29 ASN HB2 H 1 2.57 0.07 . 2 . . . . . . . . 4978 1 192 . 1 1 29 29 ASN HB3 H 1 2.93 0.07 . 2 . . . . . . . . 4978 1 193 . 1 1 29 29 ASN HD21 H 1 6.71 0.03 . 2 . . . . . . . . 4978 1 194 . 1 1 29 29 ASN HD22 H 1 7.51 0.03 . 2 . . . . . . . . 4978 1 195 . 1 1 29 29 ASN C C 13 174.31 0.15 . 1 . . . . . . . . 4978 1 196 . 1 1 29 29 ASN CA C 13 52.97 0.25 . 1 . . . . . . . . 4978 1 197 . 1 1 29 29 ASN CB C 13 36.56 0.25 . 1 . . . . . . . . 4978 1 198 . 1 1 29 29 ASN CG C 13 178.53 0.15 . 1 . . . . . . . . 4978 1 199 . 1 1 29 29 ASN N N 15 127.14 0.10 . 1 . . . . . . . . 4978 1 200 . 1 1 29 29 ASN ND2 N 15 112.87 0.10 . 1 . . . . . . . . 4978 1 201 . 1 1 30 30 ALA H H 1 8.21 0.03 . 1 . . . . . . . . 4978 1 202 . 1 1 30 30 ALA HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 203 . 1 1 30 30 ALA HB1 H 1 1.20 0.07 . 1 . . . . . . . . 4978 1 204 . 1 1 30 30 ALA HB2 H 1 1.20 0.07 . 1 . . . . . . . . 4978 1 205 . 1 1 30 30 ALA HB3 H 1 1.20 0.07 . 1 . . . . . . . . 4978 1 206 . 1 1 30 30 ALA C C 13 172.62 0.15 . 1 . . . . . . . . 4978 1 207 . 1 1 30 30 ALA CA C 13 50.39 0.25 . 1 . . . . . . . . 4978 1 208 . 1 1 30 30 ALA CB C 13 19.92 0.25 . 1 . . . . . . . . 4978 1 209 . 1 1 30 30 ALA N N 15 123.24 0.10 . 1 . . . . . . . . 4978 1 210 . 1 1 31 31 VAL H H 1 9.70 0.03 . 1 . . . . . . . . 4978 1 211 . 1 1 31 31 VAL C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 212 . 1 1 31 31 VAL CA C 13 60.47 0.25 . 1 . . . . . . . . 4978 1 213 . 1 1 31 31 VAL CB C 13 35.62 0.25 . 1 . . . . . . . . 4978 1 214 . 1 1 31 31 VAL N N 15 128.84 0.10 . 1 . . . . . . . . 4978 1 215 . 1 1 32 32 THR H H 1 9.15 0.03 . 1 . . . . . . . . 4978 1 216 . 1 1 32 32 THR C C 13 170.80 0.15 . 1 . . . . . . . . 4978 1 217 . 1 1 32 32 THR CA C 13 58.59 0.25 . 1 . . . . . . . . 4978 1 218 . 1 1 32 32 THR CB C 13 67.03 0.25 . 1 . . . . . . . . 4978 1 219 . 1 1 32 32 THR N N 15 113.16 0.10 . 1 . . . . . . . . 4978 1 220 . 1 1 34 34 SER H H 1 8.35 0.03 . 1 . . . . . . . . 4978 1 221 . 1 1 34 34 SER HA H 1 4.70 0.07 . 1 . . . . . . . . 4978 1 222 . 1 1 34 34 SER HB2 H 1 3.94 0.07 . 2 . . . . . . . . 4978 1 223 . 1 1 34 34 SER C C 13 176.46 0.15 . 1 . . . . . . . . 4978 1 224 . 1 1 34 34 SER N N 15 112.62 0.10 . 1 . . . . . . . . 4978 1 225 . 1 1 35 35 GLU H H 1 8.11 0.00 . 1 . . . . . . . . 4978 1 226 . 1 1 35 35 GLU HA H 1 4.21 0.07 . 1 . . . . . . . . 4978 1 227 . 1 1 35 35 GLU N N 15 120.58 0.10 . 1 . . . . . . . . 4978 1 228 . 1 1 36 36 LYS C C 13 175.86 0.15 . 1 . . . . . . . . 4978 1 229 . 1 1 36 36 LYS CA C 13 53.20 0.25 . 1 . . . . . . . . 4978 1 230 . 1 1 37 37 ALA H H 1 8.52 0.03 . 1 . . . . . . . . 4978 1 231 . 1 1 37 37 ALA HA H 1 5.08 0.07 . 1 . . . . . . . . 4978 1 232 . 1 1 37 37 ALA C C 13 176.56 0.15 . 1 . . . . . . . . 4978 1 233 . 1 1 37 37 ALA CA C 13 46.87 0.25 . 1 . . . . . . . . 4978 1 234 . 1 1 37 37 ALA CB C 13 18.04 0.25 . 1 . . . . . . . . 4978 1 235 . 1 1 37 37 ALA N N 15 127.04 0.10 . 1 . . . . . . . . 4978 1 236 . 1 1 38 38 LEU H H 1 7.79 0.03 . 1 . . . . . . . . 4978 1 237 . 1 1 38 38 LEU HA H 1 5.41 0.07 . 1 . . . . . . . . 4978 1 238 . 1 1 38 38 LEU C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 239 . 1 1 38 38 LEU CA C 13 53.20 0.25 . 1 . . . . . . . . 4978 1 240 . 1 1 38 38 LEU CB C 13 45.47 0.25 . 1 . . . . . . . . 4978 1 241 . 1 1 38 38 LEU N N 15 118.52 0.10 . 1 . . . . . . . . 4978 1 242 . 1 1 39 39 GLN H H 1 9.31 0.03 . 1 . . . . . . . . 4978 1 243 . 1 1 39 39 GLN HA H 1 5.17 0.07 . 1 . . . . . . . . 4978 1 244 . 1 1 39 39 GLN C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 245 . 1 1 39 39 GLN CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 246 . 1 1 39 39 GLN CB C 13 33.05 0.25 . 1 . . . . . . . . 4978 1 247 . 1 1 39 39 GLN N N 15 125.85 0.10 . 1 . . . . . . . . 4978 1 248 . 1 1 40 40 SER H H 1 8.16 0.03 . 1 . . . . . . . . 4978 1 249 . 1 1 40 40 SER HA H 1 5.49 0.07 . 1 . . . . . . . . 4978 1 250 . 1 1 40 40 SER C C 13 173.61 0.15 . 1 . . . . . . . . 4978 1 251 . 1 1 40 40 SER CA C 13 56.48 0.25 . 1 . . . . . . . . 4978 1 252 . 1 1 40 40 SER CB C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 253 . 1 1 40 40 SER N N 15 116.00 0.10 . 1 . . . . . . . . 4978 1 254 . 1 1 41 41 ASN H H 1 8.96 0.03 . 1 . . . . . . . . 4978 1 255 . 1 1 41 41 ASN HA H 1 5.62 0.07 . 1 . . . . . . . . 4978 1 256 . 1 1 41 41 ASN C C 13 173.33 0.15 . 1 . . . . . . . . 4978 1 257 . 1 1 41 41 ASN CA C 13 52.73 0.25 . 1 . . . . . . . . 4978 1 258 . 1 1 41 41 ASN CB C 13 36.56 0.25 . 1 . . . . . . . . 4978 1 259 . 1 1 41 41 ASN N N 15 122.30 0.10 . 1 . . . . . . . . 4978 1 260 . 1 1 42 42 HIS H H 1 7.35 0.03 . 1 . . . . . . . . 4978 1 261 . 1 1 42 42 HIS HA H 1 4.82 0.07 . 1 . . . . . . . . 4978 1 262 . 1 1 42 42 HIS C C 13 173.33 0.15 . 1 . . . . . . . . 4978 1 263 . 1 1 42 42 HIS CB C 13 30.23 0.25 . 1 . . . . . . . . 4978 1 264 . 1 1 42 42 HIS N N 15 116.32 0.10 . 1 . . . . . . . . 4978 1 265 . 1 1 43 43 PHE H H 1 9.22 0.03 . 1 . . . . . . . . 4978 1 266 . 1 1 43 43 PHE HA H 1 5.62 0.07 . 1 . . . . . . . . 4978 1 267 . 1 1 43 43 PHE HB2 H 1 2.80 0.07 . 2 . . . . . . . . 4978 1 268 . 1 1 43 43 PHE C C 13 174.46 0.15 . 1 . . . . . . . . 4978 1 269 . 1 1 43 43 PHE CA C 13 55.08 0.25 . 1 . . . . . . . . 4978 1 270 . 1 1 43 43 PHE CB C 13 41.72 0.25 . 1 . . . . . . . . 4978 1 271 . 1 1 43 43 PHE N N 15 124.38 0.10 . 1 . . . . . . . . 4978 1 272 . 1 1 44 44 GLU H H 1 8.92 0.03 . 1 . . . . . . . . 4978 1 273 . 1 1 44 44 GLU HA H 1 5.44 0.07 . 1 . . . . . . . . 4978 1 274 . 1 1 44 44 GLU HB2 H 1 1.95 0.07 . 2 . . . . . . . . 4978 1 275 . 1 1 44 44 GLU C C 13 174.32 0.15 . 1 . . . . . . . . 4978 1 276 . 1 1 44 44 GLU CA C 13 54.61 0.25 . 1 . . . . . . . . 4978 1 277 . 1 1 44 44 GLU CB C 13 32.81 0.25 . 1 . . . . . . . . 4978 1 278 . 1 1 44 44 GLU N N 15 121.23 0.10 . 1 . . . . . . . . 4978 1 279 . 1 1 45 45 LEU H H 1 8.42 0.03 . 1 . . . . . . . . 4978 1 280 . 1 1 45 45 LEU HA H 1 5.08 0.07 . 1 . . . . . . . . 4978 1 281 . 1 1 45 45 LEU C C 13 174.32 0.15 . 1 . . . . . . . . 4978 1 282 . 1 1 45 45 LEU CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 283 . 1 1 45 45 LEU CB C 13 42.19 0.25 . 1 . . . . . . . . 4978 1 284 . 1 1 45 45 LEU N N 15 116.57 0.10 . 1 . . . . . . . . 4978 1 285 . 1 1 46 46 SER H H 1 8.26 0.03 . 1 . . . . . . . . 4978 1 286 . 1 1 46 46 SER HA H 1 5.89 0.07 . 1 . . . . . . . . 4978 1 287 . 1 1 46 46 SER HB2 H 1 3.73 0.07 . 2 . . . . . . . . 4978 1 288 . 1 1 46 46 SER C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 289 . 1 1 46 46 SER CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 290 . 1 1 46 46 SER CB C 13 64.45 0.25 . 1 . . . . . . . . 4978 1 291 . 1 1 46 46 SER N N 15 115.80 0.10 . 1 . . . . . . . . 4978 1 292 . 1 1 47 47 ILE H H 1 8.97 0.03 . 1 . . . . . . . . 4978 1 293 . 1 1 47 47 ILE HA H 1 5.73 0.07 . 1 . . . . . . . . 4978 1 294 . 1 1 47 47 ILE C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 295 . 1 1 47 47 ILE CA C 13 58.12 0.25 . 1 . . . . . . . . 4978 1 296 . 1 1 47 47 ILE CB C 13 41.95 0.25 . 1 . . . . . . . . 4978 1 297 . 1 1 47 47 ILE N N 15 117.76 0.10 . 1 . . . . . . . . 4978 1 298 . 1 1 48 48 LYS H H 1 8.01 0.03 . 1 . . . . . . . . 4978 1 299 . 1 1 48 48 LYS HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 300 . 1 1 48 48 LYS C C 13 175.30 0.15 . 1 . . . . . . . . 4978 1 301 . 1 1 48 48 LYS CA C 13 54.37 0.25 . 1 . . . . . . . . 4978 1 302 . 1 1 48 48 LYS CB C 13 33.24 0.25 . 1 . . . . . . . . 4978 1 303 . 1 1 48 48 LYS N N 15 123.46 0.10 . 1 . . . . . . . . 4978 1 304 . 1 1 49 49 THR H H 1 9.70 0.03 . 1 . . . . . . . . 4978 1 305 . 1 1 49 49 THR HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 306 . 1 1 49 49 THR HG21 H 1 1.04 0.07 . 1 . . . . . . . . 4978 1 307 . 1 1 49 49 THR HG22 H 1 1.04 0.07 . 1 . . . . . . . . 4978 1 308 . 1 1 49 49 THR HG23 H 1 1.04 0.07 . 1 . . . . . . . . 4978 1 309 . 1 1 49 49 THR C C 13 170.80 0.15 . 1 . . . . . . . . 4978 1 310 . 1 1 49 49 THR CA C 13 60.94 0.25 . 1 . . . . . . . . 4978 1 311 . 1 1 49 49 THR CB C 13 68.90 0.25 . 1 . . . . . . . . 4978 1 312 . 1 1 49 49 THR N N 15 123.86 0.10 . 1 . . . . . . . . 4978 1 313 . 1 1 50 50 GLU H H 1 8.52 0.03 . 1 . . . . . . . . 4978 1 314 . 1 1 50 50 GLU HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 315 . 1 1 50 50 GLU C C 13 175.30 0.15 . 1 . . . . . . . . 4978 1 316 . 1 1 50 50 GLU CA C 13 54.37 0.25 . 1 . . . . . . . . 4978 1 317 . 1 1 50 50 GLU CB C 13 30.23 0.25 . 1 . . . . . . . . 4978 1 318 . 1 1 50 50 GLU N N 15 123.02 0.10 . 1 . . . . . . . . 4978 1 319 . 1 1 51 51 ALA H H 1 9.04 0.03 . 1 . . . . . . . . 4978 1 320 . 1 1 51 51 ALA HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 321 . 1 1 51 51 ALA HB1 H 1 1.65 0.07 . 1 . . . . . . . . 4978 1 322 . 1 1 51 51 ALA HB2 H 1 1.65 0.07 . 1 . . . . . . . . 4978 1 323 . 1 1 51 51 ALA HB3 H 1 1.65 0.07 . 1 . . . . . . . . 4978 1 324 . 1 1 51 51 ALA C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 325 . 1 1 51 51 ALA CA C 13 52.26 0.25 . 1 . . . . . . . . 4978 1 326 . 1 1 51 51 ALA CB C 13 18.75 0.25 . 1 . . . . . . . . 4978 1 327 . 1 1 51 51 ALA N N 15 129.67 0.10 . 1 . . . . . . . . 4978 1 328 . 1 1 52 52 THR H H 1 8.14 0.03 . 1 . . . . . . . . 4978 1 329 . 1 1 52 52 THR HA H 1 3.91 0.07 . 1 . . . . . . . . 4978 1 330 . 1 1 52 52 THR HB H 1 3.81 0.07 . 1 . . . . . . . . 4978 1 331 . 1 1 52 52 THR HG21 H 1 1.74 0.07 . 1 . . . . . . . . 4978 1 332 . 1 1 52 52 THR HG22 H 1 1.74 0.07 . 1 . . . . . . . . 4978 1 333 . 1 1 52 52 THR HG23 H 1 1.74 0.07 . 1 . . . . . . . . 4978 1 334 . 1 1 52 52 THR C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 335 . 1 1 52 52 THR CA C 13 60.70 0.25 . 1 . . . . . . . . 4978 1 336 . 1 1 52 52 THR CB C 13 68.90 0.25 . 1 . . . . . . . . 4978 1 337 . 1 1 52 52 THR N N 15 105.12 0.10 . 1 . . . . . . . . 4978 1 338 . 1 1 53 53 GLN H H 1 7.45 0.03 . 1 . . . . . . . . 4978 1 339 . 1 1 53 53 GLN HA H 1 5.26 0.07 . 1 . . . . . . . . 4978 1 340 . 1 1 53 53 GLN HB2 H 1 1.65 0.07 . 2 . . . . . . . . 4978 1 341 . 1 1 53 53 GLN C C 13 176.99 0.15 . 1 . . . . . . . . 4978 1 342 . 1 1 53 53 GLN CA C 13 52.26 0.25 . 1 . . . . . . . . 4978 1 343 . 1 1 53 53 GLN CB C 13 29.76 0.25 . 1 . . . . . . . . 4978 1 344 . 1 1 53 53 GLN N N 15 118.43 0.10 . 1 . . . . . . . . 4978 1 345 . 1 1 54 54 GLY H H 1 8.37 0.03 . 1 . . . . . . . . 4978 1 346 . 1 1 54 54 GLY HA2 H 1 3.91 0.07 . 2 . . . . . . . . 4978 1 347 . 1 1 54 54 GLY HA3 H 1 4.72 0.07 . 2 . . . . . . . . 4978 1 348 . 1 1 54 54 GLY C C 13 170.24 0.15 . 1 . . . . . . . . 4978 1 349 . 1 1 54 54 GLY CA C 13 45.23 0.25 . 1 . . . . . . . . 4978 1 350 . 1 1 54 54 GLY N N 15 108.53 0.10 . 1 . . . . . . . . 4978 1 351 . 1 1 55 55 LEU H H 1 8.30 0.03 . 1 . . . . . . . . 4978 1 352 . 1 1 55 55 LEU HA H 1 5.39 0.07 . 1 . . . . . . . . 4978 1 353 . 1 1 55 55 LEU C C 13 174.46 0.15 . 1 . . . . . . . . 4978 1 354 . 1 1 55 55 LEU CA C 13 55.14 0.25 . 1 . . . . . . . . 4978 1 355 . 1 1 55 55 LEU CB C 13 40.78 0.25 . 1 . . . . . . . . 4978 1 356 . 1 1 55 55 LEU N N 15 128.05 0.10 . 1 . . . . . . . . 4978 1 357 . 1 1 56 56 ILE H H 1 9.15 0.03 . 1 . . . . . . . . 4978 1 358 . 1 1 56 56 ILE HA H 1 5.18 0.07 . 1 . . . . . . . . 4978 1 359 . 1 1 56 56 ILE C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 360 . 1 1 56 56 ILE CA C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 361 . 1 1 56 56 ILE CB C 13 40.78 0.25 . 1 . . . . . . . . 4978 1 362 . 1 1 56 56 ILE N N 15 120.50 0.10 . 1 . . . . . . . . 4978 1 363 . 1 1 57 57 LEU H H 1 8.30 0.03 . 1 . . . . . . . . 4978 1 364 . 1 1 57 57 LEU C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 365 . 1 1 57 57 LEU CA C 13 51.79 0.25 . 1 . . . . . . . . 4978 1 366 . 1 1 57 57 LEU CB C 13 37.73 0.25 . 1 . . . . . . . . 4978 1 367 . 1 1 57 57 LEU N N 15 127.76 0.10 . 1 . . . . . . . . 4978 1 368 . 1 1 58 58 TRP H H 1 7.60 0.03 . 1 . . . . . . . . 4978 1 369 . 1 1 58 58 TRP HE1 H 1 7.32 0.07 . 1 . . . . . . . . 4978 1 370 . 1 1 58 58 TRP C C 13 174.32 0.15 . 1 . . . . . . . . 4978 1 371 . 1 1 58 58 TRP CA C 13 58.59 0.25 . 1 . . . . . . . . 4978 1 372 . 1 1 58 58 TRP CB C 13 28.12 0.25 . 1 . . . . . . . . 4978 1 373 . 1 1 58 58 TRP N N 15 112.45 0.10 . 1 . . . . . . . . 4978 1 374 . 1 1 58 58 TRP NE1 N 15 130.63 0.10 . 1 . . . . . . . . 4978 1 375 . 1 1 59 59 SER H H 1 7.48 0.03 . 1 . . . . . . . . 4978 1 376 . 1 1 59 59 SER C C 13 172.20 0.15 . 1 . . . . . . . . 4978 1 377 . 1 1 59 59 SER CA C 13 56.01 0.25 . 1 . . . . . . . . 4978 1 378 . 1 1 59 59 SER CB C 13 65.62 0.25 . 1 . . . . . . . . 4978 1 379 . 1 1 59 59 SER N N 15 112.66 0.10 . 1 . . . . . . . . 4978 1 380 . 1 1 60 60 GLY H H 1 9.60 0.03 . 1 . . . . . . . . 4978 1 381 . 1 1 60 60 GLY CA C 13 45.47 0.25 . 1 . . . . . . . . 4978 1 382 . 1 1 60 60 GLY N N 15 106.56 0.10 . 1 . . . . . . . . 4978 1 383 . 1 1 61 61 LYS H H 1 7.95 0.03 . 1 . . . . . . . . 4978 1 384 . 1 1 61 61 LYS C C 13 177.83 0.15 . 1 . . . . . . . . 4978 1 385 . 1 1 61 61 LYS CB C 13 31.87 0.25 . 1 . . . . . . . . 4978 1 386 . 1 1 61 61 LYS N N 15 121.36 0.10 . 1 . . . . . . . . 4978 1 387 . 1 1 62 62 GLY H H 1 9.13 0.03 . 1 . . . . . . . . 4978 1 388 . 1 1 62 62 GLY C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 389 . 1 1 62 62 GLY CA C 13 44.06 0.25 . 1 . . . . . . . . 4978 1 390 . 1 1 62 62 GLY N N 15 112.76 0.10 . 1 . . . . . . . . 4978 1 391 . 1 1 63 63 LEU H H 1 8.19 0.03 . 1 . . . . . . . . 4978 1 392 . 1 1 63 63 LEU HA H 1 5.08 0.07 . 1 . . . . . . . . 4978 1 393 . 1 1 63 63 LEU C C 13 172.91 0.15 . 1 . . . . . . . . 4978 1 394 . 1 1 63 63 LEU CA C 13 53.90 0.25 . 1 . . . . . . . . 4978 1 395 . 1 1 63 63 LEU CB C 13 40.31 0.25 . 1 . . . . . . . . 4978 1 396 . 1 1 63 63 LEU N N 15 122.95 0.10 . 1 . . . . . . . . 4978 1 397 . 1 1 64 64 GLU H H 1 8.63 0.03 . 1 . . . . . . . . 4978 1 398 . 1 1 64 64 GLU HA H 1 4.81 0.07 . 1 . . . . . . . . 4978 1 399 . 1 1 64 64 GLU C C 13 176.71 0.15 . 1 . . . . . . . . 4978 1 400 . 1 1 64 64 GLU CA C 13 55.55 0.25 . 1 . . . . . . . . 4978 1 401 . 1 1 64 64 GLU CB C 13 32.34 0.25 . 1 . . . . . . . . 4978 1 402 . 1 1 64 64 GLU N N 15 123.94 0.10 . 1 . . . . . . . . 4978 1 403 . 1 1 65 65 ARG H H 1 8.65 0.03 . 1 . . . . . . . . 4978 1 404 . 1 1 65 65 ARG HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 405 . 1 1 65 65 ARG C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 406 . 1 1 65 65 ARG CA C 13 57.42 0.25 . 1 . . . . . . . . 4978 1 407 . 1 1 65 65 ARG CB C 13 27.18 0.25 . 1 . . . . . . . . 4978 1 408 . 1 1 65 65 ARG N N 15 117.81 0.10 . 1 . . . . . . . . 4978 1 409 . 1 1 66 66 SER H H 1 7.60 0.03 . 1 . . . . . . . . 4978 1 410 . 1 1 66 66 SER HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 411 . 1 1 66 66 SER C C 13 173.89 0.15 . 1 . . . . . . . . 4978 1 412 . 1 1 66 66 SER CA C 13 57.42 0.25 . 1 . . . . . . . . 4978 1 413 . 1 1 66 66 SER CB C 13 64.22 0.25 . 1 . . . . . . . . 4978 1 414 . 1 1 66 66 SER N N 15 115.38 0.10 . 1 . . . . . . . . 4978 1 415 . 1 1 67 67 ASP H H 1 8.80 0.03 . 1 . . . . . . . . 4978 1 416 . 1 1 67 67 ASP HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 417 . 1 1 67 67 ASP C C 13 177.41 0.15 . 1 . . . . . . . . 4978 1 418 . 1 1 67 67 ASP CA C 13 53.67 0.25 . 1 . . . . . . . . 4978 1 419 . 1 1 67 67 ASP CB C 13 40.31 0.25 . 1 . . . . . . . . 4978 1 420 . 1 1 67 67 ASP N N 15 123.62 0.10 . 1 . . . . . . . . 4978 1 421 . 1 1 68 68 TYR H H 1 7.98 0.03 . 1 . . . . . . . . 4978 1 422 . 1 1 68 68 TYR HA H 1 3.73 0.07 . 4 . . . . . . . . 4978 1 423 . 1 1 68 68 TYR C C 13 173.05 0.15 . 1 . . . . . . . . 4978 1 424 . 1 1 68 68 TYR CA C 13 56.25 0.25 . 1 . . . . . . . . 4978 1 425 . 1 1 68 68 TYR CB C 13 40.55 0.25 . 1 . . . . . . . . 4978 1 426 . 1 1 68 68 TYR N N 15 116.41 0.10 . 1 . . . . . . . . 4978 1 427 . 1 1 69 69 ILE H H 1 8.17 0.03 . 1 . . . . . . . . 4978 1 428 . 1 1 69 69 ILE HA H 1 4.81 0.07 . 1 . . . . . . . . 4978 1 429 . 1 1 69 69 ILE C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 430 . 1 1 69 69 ILE CA C 13 59.30 0.25 . 1 . . . . . . . . 4978 1 431 . 1 1 69 69 ILE CB C 13 40.22 0.25 . 1 . . . . . . . . 4978 1 432 . 1 1 69 69 ILE N N 15 115.81 0.10 . 1 . . . . . . . . 4978 1 433 . 1 1 70 70 ALA H H 1 7.51 0.03 . 1 . . . . . . . . 4978 1 434 . 1 1 70 70 ALA HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 435 . 1 1 70 70 ALA C C 13 174.32 0.15 . 1 . . . . . . . . 4978 1 436 . 1 1 70 70 ALA CB C 13 16.17 0.25 . 1 . . . . . . . . 4978 1 437 . 1 1 70 70 ALA N N 15 123.33 0.10 . 1 . . . . . . . . 4978 1 438 . 1 1 71 71 LEU H H 1 9.47 0.03 . 1 . . . . . . . . 4978 1 439 . 1 1 71 71 LEU HA H 1 5.44 0.07 . 1 . . . . . . . . 4978 1 440 . 1 1 71 71 LEU HD11 H 1 0.21 0.07 . 2 . . . . . . . . 4978 1 441 . 1 1 71 71 LEU HD12 H 1 0.21 0.07 . 2 . . . . . . . . 4978 1 442 . 1 1 71 71 LEU HD13 H 1 0.21 0.07 . 2 . . . . . . . . 4978 1 443 . 1 1 71 71 LEU C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 444 . 1 1 71 71 LEU CA C 13 52.50 0.25 . 1 . . . . . . . . 4978 1 445 . 1 1 71 71 LEU N N 15 122.41 0.10 . 1 . . . . . . . . 4978 1 446 . 1 1 72 72 ALA H H 1 8.94 0.03 . 1 . . . . . . . . 4978 1 447 . 1 1 72 72 ALA HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 448 . 1 1 72 72 ALA HB1 H 1 0.65 0.07 . 1 . . . . . . . . 4978 1 449 . 1 1 72 72 ALA HB2 H 1 0.65 0.07 . 1 . . . . . . . . 4978 1 450 . 1 1 72 72 ALA HB3 H 1 0.65 0.07 . 1 . . . . . . . . 4978 1 451 . 1 1 72 72 ALA C C 13 174.03 0.15 . 1 . . . . . . . . 4978 1 452 . 1 1 72 72 ALA CA C 13 49.68 0.25 . 1 . . . . . . . . 4978 1 453 . 1 1 72 72 ALA CB C 13 21.80 0.25 . 1 . . . . . . . . 4978 1 454 . 1 1 72 72 ALA N N 15 125.23 0.10 . 1 . . . . . . . . 4978 1 455 . 1 1 73 73 ILE H H 1 9.36 0.03 . 1 . . . . . . . . 4978 1 456 . 1 1 73 73 ILE HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 457 . 1 1 73 73 ILE C C 13 174.32 0.15 . 1 . . . . . . . . 4978 1 458 . 1 1 73 73 ILE CA C 13 60.47 0.25 . 1 . . . . . . . . 4978 1 459 . 1 1 73 73 ILE CB C 13 38.20 0.25 . 1 . . . . . . . . 4978 1 460 . 1 1 73 73 ILE N N 15 121.81 0.10 . 1 . . . . . . . . 4978 1 461 . 1 1 74 74 VAL H H 1 8.71 0.03 . 1 . . . . . . . . 4978 1 462 . 1 1 74 74 VAL HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 463 . 1 1 74 74 VAL HB H 1 1.93 0.07 . 1 . . . . . . . . 4978 1 464 . 1 1 74 74 VAL C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 465 . 1 1 74 74 VAL CA C 13 60.70 0.25 . 1 . . . . . . . . 4978 1 466 . 1 1 74 74 VAL CB C 13 33.28 0.25 . 1 . . . . . . . . 4978 1 467 . 1 1 74 74 VAL N N 15 125.76 0.10 . 1 . . . . . . . . 4978 1 468 . 1 1 75 75 ASP H H 1 8.63 0.03 . 1 . . . . . . . . 4978 1 469 . 1 1 75 75 ASP HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 470 . 1 1 75 75 ASP C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 471 . 1 1 75 75 ASP CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 472 . 1 1 75 75 ASP CB C 13 38.90 0.25 . 1 . . . . . . . . 4978 1 473 . 1 1 75 75 ASP N N 15 129.33 0.10 . 1 . . . . . . . . 4978 1 474 . 1 1 76 76 GLY H H 1 8.93 0.03 . 1 . . . . . . . . 4978 1 475 . 1 1 76 76 GLY HA2 H 1 3.91 0.07 . 2 . . . . . . . . 4978 1 476 . 1 1 76 76 GLY HA3 H 1 4.09 0.07 . 2 . . . . . . . . 4978 1 477 . 1 1 76 76 GLY C C 13 171.64 0.15 . 1 . . . . . . . . 4978 1 478 . 1 1 76 76 GLY CA C 13 44.53 0.25 . 1 . . . . . . . . 4978 1 479 . 1 1 76 76 GLY N N 15 101.35 0.10 . 1 . . . . . . . . 4978 1 480 . 1 1 77 77 PHE H H 1 7.56 0.03 . 1 . . . . . . . . 4978 1 481 . 1 1 77 77 PHE HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 482 . 1 1 77 77 PHE HB2 H 1 2.74 0.07 . 2 . . . . . . . . 4978 1 483 . 1 1 77 77 PHE C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 484 . 1 1 77 77 PHE CA C 13 56.02 0.25 . 1 . . . . . . . . 4978 1 485 . 1 1 77 77 PHE CB C 13 41.25 0.00 . 1 . . . . . . . . 4978 1 486 . 1 1 77 77 PHE N N 15 118.61 0.10 . 1 . . . . . . . . 4978 1 487 . 1 1 78 78 VAL H H 1 10.00 0.03 . 1 . . . . . . . . 4978 1 488 . 1 1 78 78 VAL HA H 1 4.41 0.07 . 1 . . . . . . . . 4978 1 489 . 1 1 78 78 VAL C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 490 . 1 1 78 78 VAL CA C 13 62.58 0.25 . 1 . . . . . . . . 4978 1 491 . 1 1 78 78 VAL CB C 13 30.23 0.25 . 1 . . . . . . . . 4978 1 492 . 1 1 78 78 VAL N N 15 126.10 0.10 . 1 . . . . . . . . 4978 1 493 . 1 1 79 79 GLN H H 1 8.05 0.03 . 1 . . . . . . . . 4978 1 494 . 1 1 79 79 GLN HA H 1 4.81 0.07 . 1 . . . . . . . . 4978 1 495 . 1 1 79 79 GLN C C 13 171.92 0.15 . 1 . . . . . . . . 4978 1 496 . 1 1 79 79 GLN CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 497 . 1 1 79 79 GLN CB C 13 29.30 0.25 . 1 . . . . . . . . 4978 1 498 . 1 1 79 79 GLN N N 15 116.55 0.10 . 1 . . . . . . . . 4978 1 499 . 1 1 80 80 MET H H 1 7.69 0.03 . 1 . . . . . . . . 4978 1 500 . 1 1 80 80 MET HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 501 . 1 1 80 80 MET C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 502 . 1 1 80 80 MET CA C 13 53.90 0.25 . 1 . . . . . . . . 4978 1 503 . 1 1 80 80 MET CB C 13 30.00 0.25 . 1 . . . . . . . . 4978 1 504 . 1 1 80 80 MET N N 15 125.48 0.10 . 1 . . . . . . . . 4978 1 505 . 1 1 81 81 MET H H 1 8.63 0.03 . 1 . . . . . . . . 4978 1 506 . 1 1 81 81 MET HA H 1 4.56 0.07 . 1 . . . . . . . . 4978 1 507 . 1 1 81 81 MET C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 508 . 1 1 81 81 MET CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 509 . 1 1 81 81 MET CB C 13 28.59 0.25 . 1 . . . . . . . . 4978 1 510 . 1 1 81 81 MET N N 15 125.58 0.10 . 1 . . . . . . . . 4978 1 511 . 1 1 82 82 TYR H H 1 8.24 0.03 . 1 . . . . . . . . 4978 1 512 . 1 1 82 82 TYR HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 513 . 1 1 82 82 TYR CA C 13 52.97 0.25 . 1 . . . . . . . . 4978 1 514 . 1 1 82 82 TYR CB C 13 42.89 0.25 . 1 . . . . . . . . 4978 1 515 . 1 1 82 82 TYR N N 15 127.98 0.10 . 1 . . . . . . . . 4978 1 516 . 1 1 83 83 ASP H H 1 8.55 0.03 . 1 . . . . . . . . 4978 1 517 . 1 1 83 83 ASP HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 518 . 1 1 83 83 ASP C C 13 172.06 0.15 . 1 . . . . . . . . 4978 1 519 . 1 1 83 83 ASP CA C 13 55.08 0.25 . 1 . . . . . . . . 4978 1 520 . 1 1 83 83 ASP CB C 13 38.90 0.25 . 1 . . . . . . . . 4978 1 521 . 1 1 83 83 ASP N N 15 123.32 0.10 . 1 . . . . . . . . 4978 1 522 . 1 1 84 84 LEU H H 1 7.51 0.03 . 1 . . . . . . . . 4978 1 523 . 1 1 84 84 LEU HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 524 . 1 1 84 84 LEU C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 525 . 1 1 84 84 LEU CA C 13 52.73 0.25 . 1 . . . . . . . . 4978 1 526 . 1 1 84 84 LEU CB C 13 42.66 0.25 . 1 . . . . . . . . 4978 1 527 . 1 1 84 84 LEU N N 15 117.92 0.10 . 1 . . . . . . . . 4978 1 528 . 1 1 85 85 GLY H H 1 9.27 0.03 . 1 . . . . . . . . 4978 1 529 . 1 1 85 85 GLY HA2 H 1 3.82 0.07 . 2 . . . . . . . . 4978 1 530 . 1 1 85 85 GLY CA C 13 43.36 0.25 . 1 . . . . . . . . 4978 1 531 . 1 1 85 85 GLY N N 15 116.00 0.10 . 1 . . . . . . . . 4978 1 532 . 1 1 86 86 SER H H 1 8.34 0.03 . 1 . . . . . . . . 4978 1 533 . 1 1 86 86 SER HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 534 . 1 1 86 86 SER HB2 H 1 3.64 0.07 . 2 . . . . . . . . 4978 1 535 . 1 1 86 86 SER HB3 H 1 3.81 0.07 . 2 . . . . . . . . 4978 1 536 . 1 1 86 86 SER C C 13 175.44 0.15 . 1 . . . . . . . . 4978 1 537 . 1 1 86 86 SER CB C 13 63.98 0.25 . 1 . . . . . . . . 4978 1 538 . 1 1 86 86 SER N N 15 116.40 0.10 . 1 . . . . . . . . 4978 1 539 . 1 1 87 87 LYS H H 1 7.95 0.03 . 1 . . . . . . . . 4978 1 540 . 1 1 87 87 LYS HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 541 . 1 1 87 87 LYS HB2 H 1 1.65 0.07 . 4 . . . . . . . . 4978 1 542 . 1 1 87 87 LYS HB3 H 1 1.75 0.07 . 4 . . . . . . . . 4978 1 543 . 1 1 87 87 LYS CA C 13 54.14 0.25 . 1 . . . . . . . . 4978 1 544 . 1 1 87 87 LYS CB C 13 34.22 0.25 . 1 . . . . . . . . 4978 1 545 . 1 1 87 87 LYS N N 15 127.28 0.10 . 1 . . . . . . . . 4978 1 546 . 1 1 88 88 PRO HA H 1 4.24 0.07 . 1 . . . . . . . . 4978 1 547 . 1 1 88 88 PRO C C 13 171.08 0.15 . 1 . . . . . . . . 4978 1 548 . 1 1 88 88 PRO CA C 13 59.06 0.25 . 1 . . . . . . . . 4978 1 549 . 1 1 88 88 PRO CB C 13 34.45 0.25 . 1 . . . . . . . . 4978 1 550 . 1 1 89 89 VAL H H 1 7.64 0.03 . 1 . . . . . . . . 4978 1 551 . 1 1 89 89 VAL HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 552 . 1 1 89 89 VAL C C 13 170.66 0.15 . 1 . . . . . . . . 4978 1 553 . 1 1 89 89 VAL CA C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 554 . 1 1 89 89 VAL CB C 13 33.05 0.25 . 1 . . . . . . . . 4978 1 555 . 1 1 89 89 VAL N N 15 124.16 0.10 . 1 . . . . . . . . 4978 1 556 . 1 1 90 90 VAL H H 1 7.58 0.03 . 1 . . . . . . . . 4978 1 557 . 1 1 90 90 VAL HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 558 . 1 1 90 90 VAL C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 559 . 1 1 90 90 VAL CA C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 560 . 1 1 90 90 VAL CB C 13 33.05 0.25 . 1 . . . . . . . . 4978 1 561 . 1 1 90 90 VAL N N 15 124.07 0.10 . 1 . . . . . . . . 4978 1 562 . 1 1 91 91 LEU H H 1 9.26 0.03 . 1 . . . . . . . . 4978 1 563 . 1 1 91 91 LEU HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 564 . 1 1 91 91 LEU C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 565 . 1 1 91 91 LEU CA C 13 52.73 0.25 . 1 . . . . . . . . 4978 1 566 . 1 1 91 91 LEU CB C 13 41.72 0.25 . 1 . . . . . . . . 4978 1 567 . 1 1 91 91 LEU N N 15 129.00 0.10 . 1 . . . . . . . . 4978 1 568 . 1 1 92 92 ARG H H 1 8.54 0.03 . 1 . . . . . . . . 4978 1 569 . 1 1 92 92 ARG HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 570 . 1 1 92 92 ARG HB2 H 1 1.57 0.07 . 2 . . . . . . . . 4978 1 571 . 1 1 92 92 ARG C C 13 174.31 0.15 . 1 . . . . . . . . 4978 1 572 . 1 1 92 92 ARG CA C 13 54.84 0.25 . 1 . . . . . . . . 4978 1 573 . 1 1 92 92 ARG CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 574 . 1 1 92 92 ARG N N 15 123.40 0.10 . 1 . . . . . . . . 4978 1 575 . 1 1 93 93 SER H H 1 8.22 0.03 . 1 . . . . . . . . 4978 1 576 . 1 1 93 93 SER HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 577 . 1 1 93 93 SER HB2 H 1 4.18 0.07 . 2 . . . . . . . . 4978 1 578 . 1 1 93 93 SER C C 13 174.03 0.15 . 1 . . . . . . . . 4978 1 579 . 1 1 93 93 SER CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 580 . 1 1 93 93 SER CB C 13 62.34 0.25 . 1 . . . . . . . . 4978 1 581 . 1 1 93 93 SER N N 15 117.82 0.10 . 1 . . . . . . . . 4978 1 582 . 1 1 94 94 THR H H 1 9.70 0.03 . 1 . . . . . . . . 4978 1 583 . 1 1 94 94 THR HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 584 . 1 1 94 94 THR C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 585 . 1 1 94 94 THR CA C 13 61.64 0.25 . 1 . . . . . . . . 4978 1 586 . 1 1 94 94 THR CB C 13 69.84 0.25 . 1 . . . . . . . . 4978 1 587 . 1 1 94 94 THR N N 15 115.64 0.10 . 1 . . . . . . . . 4978 1 588 . 1 1 95 95 VAL H H 1 7.96 0.03 . 1 . . . . . . . . 4978 1 589 . 1 1 95 95 VAL HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 590 . 1 1 95 95 VAL HB H 1 1.83 0.07 . 1 . . . . . . . . 4978 1 591 . 1 1 95 95 VAL C C 13 172.77 0.15 . 1 . . . . . . . . 4978 1 592 . 1 1 95 95 VAL CA C 13 59.06 0.25 . 1 . . . . . . . . 4978 1 593 . 1 1 95 95 VAL CB C 13 33.04 0.25 . 1 . . . . . . . . 4978 1 594 . 1 1 95 95 VAL N N 15 125.23 0.10 . 1 . . . . . . . . 4978 1 595 . 1 1 96 96 PRO HA H 1 3.74 0.07 . 1 . . . . . . . . 4978 1 596 . 1 1 96 96 PRO C C 13 177.69 0.15 . 1 . . . . . . . . 4978 1 597 . 1 1 96 96 PRO CA C 13 62.58 0.25 . 1 . . . . . . . . 4978 1 598 . 1 1 96 96 PRO CB C 13 30.23 0.25 . 1 . . . . . . . . 4978 1 599 . 1 1 97 97 ILE H H 1 7.94 0.03 . 1 . . . . . . . . 4978 1 600 . 1 1 97 97 ILE HA H 1 4.69 0.07 . 1 . . . . . . . . 4978 1 601 . 1 1 97 97 ILE C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 602 . 1 1 97 97 ILE CA C 13 56.01 0.25 . 1 . . . . . . . . 4978 1 603 . 1 1 97 97 ILE CB C 13 40.55 0.25 . 1 . . . . . . . . 4978 1 604 . 1 1 97 97 ILE N N 15 122.65 0.10 . 1 . . . . . . . . 4978 1 605 . 1 1 98 98 ASN H H 1 8.99 0.03 . 1 . . . . . . . . 4978 1 606 . 1 1 98 98 ASN HA H 1 4.69 0.07 . 1 . . . . . . . . 4978 1 607 . 1 1 98 98 ASN C C 13 175.86 0.15 . 1 . . . . . . . . 4978 1 608 . 1 1 98 98 ASN CA C 13 52.73 0.25 . 1 . . . . . . . . 4978 1 609 . 1 1 98 98 ASN CB C 13 33.75 0.25 . 1 . . . . . . . . 4978 1 610 . 1 1 98 98 ASN N N 15 122.03 0.10 . 1 . . . . . . . . 4978 1 611 . 1 1 99 99 THR H H 1 7.88 0.03 . 1 . . . . . . . . 4978 1 612 . 1 1 99 99 THR HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 613 . 1 1 99 99 THR HB H 1 4.15 0.07 . 1 . . . . . . . . 4978 1 614 . 1 1 99 99 THR HG21 H 1 0.99 0.07 . 1 . . . . . . . . 4978 1 615 . 1 1 99 99 THR HG22 H 1 0.99 0.07 . 1 . . . . . . . . 4978 1 616 . 1 1 99 99 THR HG23 H 1 0.99 0.07 . 1 . . . . . . . . 4978 1 617 . 1 1 99 99 THR C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 618 . 1 1 99 99 THR CA C 13 60.23 0.25 . 1 . . . . . . . . 4978 1 619 . 1 1 99 99 THR CB C 13 69.61 0.25 . 1 . . . . . . . . 4978 1 620 . 1 1 99 99 THR N N 15 109.35 0.10 . 1 . . . . . . . . 4978 1 621 . 1 1 100 100 ASN H H 1 8.62 0.03 . 1 . . . . . . . . 4978 1 622 . 1 1 100 100 ASN HA H 1 4.73 0.07 . 1 . . . . . . . . 4978 1 623 . 1 1 100 100 ASN HB2 H 1 2.12 0.07 . 2 . . . . . . . . 4978 1 624 . 1 1 100 100 ASN HB3 H 1 3.20 0.07 . 2 . . . . . . . . 4978 1 625 . 1 1 100 100 ASN HD21 H 1 6.58 0.03 . 2 . . . . . . . . 4978 1 626 . 1 1 100 100 ASN HD22 H 1 7.18 0.03 . 2 . . . . . . . . 4978 1 627 . 1 1 100 100 ASN C C 13 173.61 0.15 . 1 . . . . . . . . 4978 1 628 . 1 1 100 100 ASN CA C 13 52.26 0.25 . 1 . . . . . . . . 4978 1 629 . 1 1 100 100 ASN CB C 13 37.97 0.25 . 1 . . . . . . . . 4978 1 630 . 1 1 100 100 ASN CG C 13 176.85 0.15 . 1 . . . . . . . . 4978 1 631 . 1 1 100 100 ASN N N 15 120.99 0.10 . 1 . . . . . . . . 4978 1 632 . 1 1 100 100 ASN ND2 N 15 109.28 0.10 . 1 . . . . . . . . 4978 1 633 . 1 1 101 101 HIS H H 1 7.68 0.03 . 1 . . . . . . . . 4978 1 634 . 1 1 101 101 HIS HA H 1 4.92 0.07 . 1 . . . . . . . . 4978 1 635 . 1 1 101 101 HIS HB2 H 1 2.83 0.07 . 2 . . . . . . . . 4978 1 636 . 1 1 101 101 HIS C C 13 176.42 0.15 . 1 . . . . . . . . 4978 1 637 . 1 1 101 101 HIS CA C 13 53.00 0.25 . 1 . . . . . . . . 4978 1 638 . 1 1 101 101 HIS CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 639 . 1 1 101 101 HIS N N 15 114.70 0.10 . 1 . . . . . . . . 4978 1 640 . 1 1 102 102 TRP H H 1 8.86 0.03 . 1 . . . . . . . . 4978 1 641 . 1 1 102 102 TRP HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 642 . 1 1 102 102 TRP HD1 H 1 7.21 0.07 . 1 . . . . . . . . 4978 1 643 . 1 1 102 102 TRP HE1 H 1 10.26 0.03 . 1 . . . . . . . . 4978 1 644 . 1 1 102 102 TRP C C 13 177.69 0.15 . 1 . . . . . . . . 4978 1 645 . 1 1 102 102 TRP CA C 13 58.36 0.25 . 1 . . . . . . . . 4978 1 646 . 1 1 102 102 TRP CB C 13 28.36 0.25 . 1 . . . . . . . . 4978 1 647 . 1 1 102 102 TRP N N 15 127.17 0.10 . 1 . . . . . . . . 4978 1 648 . 1 1 102 102 TRP NE1 N 15 130.63 0.10 . 1 . . . . . . . . 4978 1 649 . 1 1 103 103 THR H H 1 9.81 0.03 . 1 . . . . . . . . 4978 1 650 . 1 1 103 103 THR HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 651 . 1 1 103 103 THR C C 13 172.21 0.15 . 1 . . . . . . . . 4978 1 652 . 1 1 103 103 THR CA C 13 62.11 0.25 . 1 . . . . . . . . 4978 1 653 . 1 1 103 103 THR CB C 13 71.25 0.25 . 1 . . . . . . . . 4978 1 654 . 1 1 103 103 THR N N 15 123.01 0.10 . 1 . . . . . . . . 4978 1 655 . 1 1 104 104 HIS H H 1 9.29 0.03 . 1 . . . . . . . . 4978 1 656 . 1 1 104 104 HIS HA H 1 5.17 0.07 . 1 . . . . . . . . 4978 1 657 . 1 1 104 104 HIS C C 13 173.62 0.15 . 1 . . . . . . . . 4978 1 658 . 1 1 104 104 HIS CA C 13 55.78 0.25 . 1 . . . . . . . . 4978 1 659 . 1 1 104 104 HIS CB C 13 30.00 0.25 . 1 . . . . . . . . 4978 1 660 . 1 1 104 104 HIS N N 15 128.51 0.10 . 1 . . . . . . . . 4978 1 661 . 1 1 105 105 ILE H H 1 9.13 0.03 . 1 . . . . . . . . 4978 1 662 . 1 1 105 105 ILE HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 663 . 1 1 105 105 ILE HB H 1 1.54 0.07 . 1 . . . . . . . . 4978 1 664 . 1 1 105 105 ILE C C 13 173.89 0.15 . 1 . . . . . . . . 4978 1 665 . 1 1 105 105 ILE CA C 13 60.47 0.25 . 1 . . . . . . . . 4978 1 666 . 1 1 105 105 ILE CB C 13 40.08 0.25 . 1 . . . . . . . . 4978 1 667 . 1 1 105 105 ILE N N 15 126.68 0.10 . 1 . . . . . . . . 4978 1 668 . 1 1 106 106 LYS H H 1 8.72 0.03 . 1 . . . . . . . . 4978 1 669 . 1 1 106 106 LYS HA H 1 4.90 0.07 . 1 . . . . . . . . 4978 1 670 . 1 1 106 106 LYS HB2 H 1 1.65 0.07 . 2 . . . . . . . . 4978 1 671 . 1 1 106 106 LYS C C 13 174.32 0.15 . 1 . . . . . . . . 4978 1 672 . 1 1 106 106 LYS CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 673 . 1 1 106 106 LYS CB C 13 34.45 0.25 . 1 . . . . . . . . 4978 1 674 . 1 1 106 106 LYS N N 15 125.81 0.10 . 1 . . . . . . . . 4978 1 675 . 1 1 107 107 ALA H H 1 9.23 0.03 . 1 . . . . . . . . 4978 1 676 . 1 1 107 107 ALA HA H 1 5.35 0.07 . 1 . . . . . . . . 4978 1 677 . 1 1 107 107 ALA HB1 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 678 . 1 1 107 107 ALA HB2 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 679 . 1 1 107 107 ALA HB3 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 680 . 1 1 107 107 ALA C C 13 171.08 0.15 . 1 . . . . . . . . 4978 1 681 . 1 1 107 107 ALA CA C 13 49.92 0.25 . 1 . . . . . . . . 4978 1 682 . 1 1 107 107 ALA CB C 13 22.02 0.25 . 1 . . . . . . . . 4978 1 683 . 1 1 107 107 ALA N N 15 131.08 0.10 . 1 . . . . . . . . 4978 1 684 . 1 1 108 108 TYR H H 1 8.90 0.03 . 1 . . . . . . . . 4978 1 685 . 1 1 108 108 TYR HA H 1 5.27 0.07 . 1 . . . . . . . . 4978 1 686 . 1 1 108 108 TYR C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 687 . 1 1 108 108 TYR CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 688 . 1 1 108 108 TYR CB C 13 35.39 0.25 . 1 . . . . . . . . 4978 1 689 . 1 1 108 108 TYR N N 15 126.32 0.10 . 1 . . . . . . . . 4978 1 690 . 1 1 109 109 ARG H H 1 8.16 0.03 . 1 . . . . . . . . 4978 1 691 . 1 1 109 109 ARG HA H 1 4.36 0.07 . 1 . . . . . . . . 4978 1 692 . 1 1 109 109 ARG C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 693 . 1 1 109 109 ARG CA C 13 58.36 0.25 . 1 . . . . . . . . 4978 1 694 . 1 1 109 109 ARG CB C 13 25.54 0.25 . 1 . . . . . . . . 4978 1 695 . 1 1 109 109 ARG N N 15 116.16 0.10 . 1 . . . . . . . . 4978 1 696 . 1 1 110 110 VAL H H 1 8.47 0.03 . 1 . . . . . . . . 4978 1 697 . 1 1 110 110 VAL HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 698 . 1 1 110 110 VAL C C 13 179.24 0.15 . 1 . . . . . . . . 4978 1 699 . 1 1 110 110 VAL CA C 13 57.66 0.25 . 1 . . . . . . . . 4978 1 700 . 1 1 110 110 VAL CB C 13 29.53 0.25 . 1 . . . . . . . . 4978 1 701 . 1 1 110 110 VAL N N 15 120.33 0.10 . 1 . . . . . . . . 4978 1 702 . 1 1 111 111 GLN H H 1 8.13 0.03 . 1 . . . . . . . . 4978 1 703 . 1 1 111 111 GLN HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 704 . 1 1 111 111 GLN HB2 H 1 2.11 0.07 . 2 . . . . . . . . 4978 1 705 . 1 1 111 111 GLN HB3 H 1 1.85 0.07 . 2 . . . . . . . . 4978 1 706 . 1 1 111 111 GLN HG2 H 1 2.34 0.07 . 2 . . . . . . . . 4978 1 707 . 1 1 111 111 GLN HG3 H 1 2.44 0.07 . 2 . . . . . . . . 4978 1 708 . 1 1 111 111 GLN HE21 H 1 6.76 0.03 . 2 . . . . . . . . 4978 1 709 . 1 1 111 111 GLN HE22 H 1 7.38 0.03 . 2 . . . . . . . . 4978 1 710 . 1 1 111 111 GLN C C 13 178.11 0.15 . 1 . . . . . . . . 4978 1 711 . 1 1 111 111 GLN CA C 13 56.48 0.25 . 1 . . . . . . . . 4978 1 712 . 1 1 111 111 GLN CB C 13 29.53 0.25 . 1 . . . . . . . . 4978 1 713 . 1 1 111 111 GLN CD C 13 179.66 0.15 . 1 . . . . . . . . 4978 1 714 . 1 1 111 111 GLN N N 15 123.29 0.10 . 1 . . . . . . . . 4978 1 715 . 1 1 111 111 GLN NE2 N 15 112.12 0.10 . 1 . . . . . . . . 4978 1 716 . 1 1 112 112 ARG H H 1 8.67 0.03 . 1 . . . . . . . . 4978 1 717 . 1 1 112 112 ARG HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 718 . 1 1 112 112 ARG C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 719 . 1 1 112 112 ARG CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 720 . 1 1 112 112 ARG CB C 13 35.16 0.25 . 1 . . . . . . . . 4978 1 721 . 1 1 112 112 ARG N N 15 122.66 0.10 . 1 . . . . . . . . 4978 1 722 . 1 1 113 113 GLU H H 1 7.89 0.03 . 1 . . . . . . . . 4978 1 723 . 1 1 113 113 GLU C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 724 . 1 1 113 113 GLU CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 725 . 1 1 113 113 GLU CB C 13 32.58 0.25 . 1 . . . . . . . . 4978 1 726 . 1 1 113 113 GLU N N 15 127.28 0.10 . 1 . . . . . . . . 4978 1 727 . 1 1 114 114 GLY H H 1 9.33 0.03 . 1 . . . . . . . . 4978 1 728 . 1 1 114 114 GLY HA2 H 1 3.64 0.07 . 2 . . . . . . . . 4978 1 729 . 1 1 114 114 GLY C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 730 . 1 1 114 114 GLY CA C 13 43.36 0.25 . 1 . . . . . . . . 4978 1 731 . 1 1 114 114 GLY N N 15 116.63 0.10 . 1 . . . . . . . . 4978 1 732 . 1 1 115 115 SER H H 1 8.69 0.03 . 1 . . . . . . . . 4978 1 733 . 1 1 115 115 SER HA H 1 5.26 0.07 . 1 . . . . . . . . 4978 1 734 . 1 1 115 115 SER C C 13 171.92 0.15 . 1 . . . . . . . . 4978 1 735 . 1 1 115 115 SER CA C 13 55.78 0.25 . 1 . . . . . . . . 4978 1 736 . 1 1 115 115 SER CB C 13 63.52 0.25 . 1 . . . . . . . . 4978 1 737 . 1 1 115 115 SER N N 15 115.80 0.10 . 1 . . . . . . . . 4978 1 738 . 1 1 116 116 LEU H H 1 9.07 0.03 . 1 . . . . . . . . 4978 1 739 . 1 1 116 116 LEU HA H 1 5.08 0.07 . 1 . . . . . . . . 4978 1 740 . 1 1 116 116 LEU C C 13 173.47 0.15 . 1 . . . . . . . . 4978 1 741 . 1 1 116 116 LEU CA C 13 52.73 0.25 . 1 . . . . . . . . 4978 1 742 . 1 1 116 116 LEU CB C 13 45.70 0.25 . 1 . . . . . . . . 4978 1 743 . 1 1 116 116 LEU N N 15 128.98 0.10 . 1 . . . . . . . . 4978 1 744 . 1 1 117 117 GLN H H 1 9.00 0.03 . 1 . . . . . . . . 4978 1 745 . 1 1 117 117 GLN HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 746 . 1 1 117 117 GLN C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 747 . 1 1 117 117 GLN CA C 13 55.08 0.25 . 1 . . . . . . . . 4978 1 748 . 1 1 117 117 GLN CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 749 . 1 1 117 117 GLN N N 15 126.40 0.10 . 1 . . . . . . . . 4978 1 750 . 1 1 118 118 VAL H H 1 10.14 0.03 . 1 . . . . . . . . 4978 1 751 . 1 1 118 118 VAL HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 752 . 1 1 118 118 VAL HG11 H 1 0.39 0.07 . 2 . . . . . . . . 4978 1 753 . 1 1 118 118 VAL HG12 H 1 0.39 0.07 . 2 . . . . . . . . 4978 1 754 . 1 1 118 118 VAL HG13 H 1 0.39 0.07 . 2 . . . . . . . . 4978 1 755 . 1 1 118 118 VAL C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 756 . 1 1 118 118 VAL CA C 13 60.47 0.25 . 1 . . . . . . . . 4978 1 757 . 1 1 118 118 VAL CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 758 . 1 1 118 118 VAL N N 15 132.43 0.10 . 1 . . . . . . . . 4978 1 759 . 1 1 119 119 GLY H H 1 9.18 0.03 . 1 . . . . . . . . 4978 1 760 . 1 1 119 119 GLY HA2 H 1 4.00 0.07 . 2 . . . . . . . . 4978 1 761 . 1 1 119 119 GLY C C 13 175.16 0.15 . 1 . . . . . . . . 4978 1 762 . 1 1 119 119 GLY CA C 13 46.40 0.25 . 1 . . . . . . . . 4978 1 763 . 1 1 119 119 GLY N N 15 114.27 0.10 . 1 . . . . . . . . 4978 1 764 . 1 1 120 120 ASN H H 1 8.80 0.03 . 1 . . . . . . . . 4978 1 765 . 1 1 120 120 ASN HA H 1 4.90 0.07 . 1 . . . . . . . . 4978 1 766 . 1 1 120 120 ASN HB2 H 1 2.48 0.07 . 2 . . . . . . . . 4978 1 767 . 1 1 120 120 ASN HB3 H 1 2.93 0.07 . 2 . . . . . . . . 4978 1 768 . 1 1 120 120 ASN HD21 H 1 7.52 0.03 . 2 . . . . . . . . 4978 1 769 . 1 1 120 120 ASN HD22 H 1 6.83 0.03 . 2 . . . . . . . . 4978 1 770 . 1 1 120 120 ASN C C 13 175.58 0.15 . 1 . . . . . . . . 4978 1 771 . 1 1 120 120 ASN CA C 13 51.56 0.25 . 1 . . . . . . . . 4978 1 772 . 1 1 120 120 ASN CB C 13 37.97 0.25 . 1 . . . . . . . . 4978 1 773 . 1 1 120 120 ASN CG C 13 177.97 0.15 . 1 . . . . . . . . 4978 1 774 . 1 1 120 120 ASN N N 15 124.00 0.10 . 1 . . . . . . . . 4978 1 775 . 1 1 120 120 ASN ND2 N 15 112.75 0.10 . 1 . . . . . . . . 4978 1 776 . 1 1 121 121 GLU H H 1 7.53 0.03 . 1 . . . . . . . . 4978 1 777 . 1 1 121 121 GLU HA H 1 4.36 0.07 . 1 . . . . . . . . 4978 1 778 . 1 1 121 121 GLU C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 779 . 1 1 121 121 GLU CA C 13 55.08 0.25 . 1 . . . . . . . . 4978 1 780 . 1 1 121 121 GLU CB C 13 28.59 0.25 . 1 . . . . . . . . 4978 1 781 . 1 1 121 121 GLU N N 15 120.86 0.10 . 1 . . . . . . . . 4978 1 782 . 1 1 122 122 ALA H H 1 8.27 0.03 . 1 . . . . . . . . 4978 1 783 . 1 1 122 122 ALA HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 784 . 1 1 122 122 ALA C C 13 176.28 0.15 . 1 . . . . . . . . 4978 1 785 . 1 1 122 122 ALA CA C 13 49.69 0.25 . 1 . . . . . . . . 4978 1 786 . 1 1 122 122 ALA CB C 13 15.93 0.25 . 1 . . . . . . . . 4978 1 787 . 1 1 122 122 ALA N N 15 125.79 0.10 . 1 . . . . . . . . 4978 1 788 . 1 1 123 123 PRO HA H 1 4.19 0.07 . 1 . . . . . . . . 4978 1 789 . 1 1 123 123 PRO C C 13 176.14 0.15 . 1 . . . . . . . . 4978 1 790 . 1 1 123 123 PRO CA C 13 63.05 0.25 . 1 . . . . . . . . 4978 1 791 . 1 1 123 123 PRO CB C 13 30.47 0.25 . 1 . . . . . . . . 4978 1 792 . 1 1 124 124 ILE H H 1 9.30 0.03 . 1 . . . . . . . . 4978 1 793 . 1 1 124 124 ILE HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 794 . 1 1 124 124 ILE HB H 1 2.01 0.07 . 1 . . . . . . . . 4978 1 795 . 1 1 124 124 ILE C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 796 . 1 1 124 124 ILE CA C 13 58.59 0.25 . 1 . . . . . . . . 4978 1 797 . 1 1 124 124 ILE CB C 13 36.80 0.25 . 1 . . . . . . . . 4978 1 798 . 1 1 124 124 ILE N N 15 127.75 0.10 . 1 . . . . . . . . 4978 1 799 . 1 1 125 125 THR H H 1 8.14 0.03 . 1 . . . . . . . . 4978 1 800 . 1 1 125 125 THR HA H 1 5.53 0.07 . 1 . . . . . . . . 4978 1 801 . 1 1 125 125 THR C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 802 . 1 1 125 125 THR CA C 13 58.36 0.25 . 1 . . . . . . . . 4978 1 803 . 1 1 125 125 THR CB C 13 71.48 0.25 . 1 . . . . . . . . 4978 1 804 . 1 1 125 125 THR N N 15 115.41 0.10 . 1 . . . . . . . . 4978 1 805 . 1 1 126 126 GLY H H 1 7.97 0.03 . 1 . . . . . . . . 4978 1 806 . 1 1 126 126 GLY HA2 H 1 3.91 0.07 . 2 . . . . . . . . 4978 1 807 . 1 1 126 126 GLY HA3 H 1 4.18 0.07 . 2 . . . . . . . . 4978 1 808 . 1 1 126 126 GLY C C 13 170.80 0.15 . 1 . . . . . . . . 4978 1 809 . 1 1 126 126 GLY CA C 13 44.53 0.25 . 1 . . . . . . . . 4978 1 810 . 1 1 126 126 GLY N N 15 108.32 0.10 . 1 . . . . . . . . 4978 1 811 . 1 1 127 127 SER H H 1 8.41 0.03 . 1 . . . . . . . . 4978 1 812 . 1 1 127 127 SER HA H 1 5.71 0.07 . 1 . . . . . . . . 4978 1 813 . 1 1 127 127 SER HB2 H 1 3.46 0.07 . 2 . . . . . . . . 4978 1 814 . 1 1 127 127 SER C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 815 . 1 1 127 127 SER CA C 13 55.78 0.25 . 1 . . . . . . . . 4978 1 816 . 1 1 127 127 SER CB C 13 64.92 0.25 . 1 . . . . . . . . 4978 1 817 . 1 1 127 127 SER N N 15 113.24 0.10 . 1 . . . . . . . . 4978 1 818 . 1 1 128 128 SER H H 1 8.70 0.03 . 1 . . . . . . . . 4978 1 819 . 1 1 128 128 SER HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 820 . 1 1 128 128 SER C C 13 171.92 0.15 . 1 . . . . . . . . 4978 1 821 . 1 1 128 128 SER CA C 13 57.58 0.25 . 1 . . . . . . . . 4978 1 822 . 1 1 128 128 SER CB C 13 59.76 0.25 . 1 . . . . . . . . 4978 1 823 . 1 1 128 128 SER N N 15 119.70 0.10 . 1 . . . . . . . . 4978 1 824 . 1 1 129 129 PRO HA H 1 4.73 0.07 . 1 . . . . . . . . 4978 1 825 . 1 1 129 129 PRO C C 13 175.86 0.15 . 1 . . . . . . . . 4978 1 826 . 1 1 129 129 PRO CA C 13 62.81 0.25 . 1 . . . . . . . . 4978 1 827 . 1 1 129 129 PRO CB C 13 30.93 0.25 . 1 . . . . . . . . 4978 1 828 . 1 1 130 130 LEU H H 1 8.22 0.03 . 1 . . . . . . . . 4978 1 829 . 1 1 130 130 LEU HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 830 . 1 1 130 130 LEU HB2 H 1 1.56 0.07 . 4 . . . . . . . . 4978 1 831 . 1 1 130 130 LEU HD11 H 1 0.48 0.07 . 2 . . . . . . . . 4978 1 832 . 1 1 130 130 LEU HD12 H 1 0.48 0.07 . 2 . . . . . . . . 4978 1 833 . 1 1 130 130 LEU HD13 H 1 0.48 0.07 . 2 . . . . . . . . 4978 1 834 . 1 1 130 130 LEU C C 13 176.71 0.15 . 1 . . . . . . . . 4978 1 835 . 1 1 130 130 LEU CA C 13 56.01 0.25 . 1 . . . . . . . . 4978 1 836 . 1 1 130 130 LEU CB C 13 41.48 0.25 . 1 . . . . . . . . 4978 1 837 . 1 1 130 130 LEU N N 15 121.88 0.10 . 1 . . . . . . . . 4978 1 838 . 1 1 131 131 GLY H H 1 8.03 0.03 . 1 . . . . . . . . 4978 1 839 . 1 1 131 131 GLY HA2 H 1 4.72 0.07 . 2 . . . . . . . . 4978 1 840 . 1 1 131 131 GLY HA3 H 1 3.46 0.07 . 2 . . . . . . . . 4978 1 841 . 1 1 131 131 GLY C C 13 173.33 0.15 . 1 . . . . . . . . 4978 1 842 . 1 1 131 131 GLY CA C 13 44.30 0.25 . 1 . . . . . . . . 4978 1 843 . 1 1 131 131 GLY N N 15 110.25 0.10 . 1 . . . . . . . . 4978 1 844 . 1 1 132 132 ALA H H 1 7.84 0.03 . 1 . . . . . . . . 4978 1 845 . 1 1 132 132 ALA HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 846 . 1 1 132 132 ALA HB1 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 847 . 1 1 132 132 ALA HB2 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 848 . 1 1 132 132 ALA HB3 H 1 1.47 0.07 . 1 . . . . . . . . 4978 1 849 . 1 1 132 132 ALA C C 13 177.13 0.15 . 1 . . . . . . . . 4978 1 850 . 1 1 132 132 ALA CA C 13 50.86 0.25 . 1 . . . . . . . . 4978 1 851 . 1 1 132 132 ALA CB C 13 20.39 0.25 . 1 . . . . . . . . 4978 1 852 . 1 1 132 132 ALA N N 15 124.91 0.10 . 1 . . . . . . . . 4978 1 853 . 1 1 133 133 THR H H 1 8.90 0.03 . 1 . . . . . . . . 4978 1 854 . 1 1 133 133 THR HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 855 . 1 1 133 133 THR C C 13 175.01 0.15 . 1 . . . . . . . . 4978 1 856 . 1 1 133 133 THR CA C 13 61.64 0.25 . 1 . . . . . . . . 4978 1 857 . 1 1 133 133 THR CB C 13 67.58 0.25 . 1 . . . . . . . . 4978 1 858 . 1 1 133 133 THR N N 15 120.40 0.10 . 1 . . . . . . . . 4978 1 859 . 1 1 134 134 GLN H H 1 9.19 0.03 . 1 . . . . . . . . 4978 1 860 . 1 1 134 134 GLN HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 861 . 1 1 134 134 GLN HG2 H 1 2.03 0.07 . 4 . . . . . . . . 4978 1 862 . 1 1 134 134 GLN HE21 H 1 6.69 0.03 . 2 . . . . . . . . 4978 1 863 . 1 1 134 134 GLN HE22 H 1 7.59 0.03 . 2 . . . . . . . . 4978 1 864 . 1 1 134 134 GLN C C 13 177.85 0.15 . 1 . . . . . . . . 4978 1 865 . 1 1 134 134 GLN CA C 13 53.44 0.25 . 1 . . . . . . . . 4978 1 866 . 1 1 134 134 GLN CB C 13 31.87 0.25 . 1 . . . . . . . . 4978 1 867 . 1 1 134 134 GLN CD C 13 180.78 0.15 . 1 . . . . . . . . 4978 1 868 . 1 1 134 134 GLN N N 15 128.90 0.10 . 1 . . . . . . . . 4978 1 869 . 1 1 134 134 GLN NE2 N 15 112.33 0.10 . 1 . . . . . . . . 4978 1 870 . 1 1 135 135 LEU H H 1 8.72 0.03 . 1 . . . . . . . . 4978 1 871 . 1 1 135 135 LEU HA H 1 4.28 0.07 . 1 . . . . . . . . 4978 1 872 . 1 1 135 135 LEU C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 873 . 1 1 135 135 LEU CA C 13 54.74 0.25 . 1 . . . . . . . . 4978 1 874 . 1 1 135 135 LEU CB C 13 41.37 0.25 . 1 . . . . . . . . 4978 1 875 . 1 1 135 135 LEU N N 15 122.02 0.10 . 1 . . . . . . . . 4978 1 876 . 1 1 136 136 ASP H H 1 8.84 0.03 . 1 . . . . . . . . 4978 1 877 . 1 1 136 136 ASP HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 878 . 1 1 136 136 ASP C C 13 174.03 0.15 . 1 . . . . . . . . 4978 1 879 . 1 1 136 136 ASP CA C 13 52.26 0.25 . 1 . . . . . . . . 4978 1 880 . 1 1 136 136 ASP CB C 13 39.84 0.25 . 1 . . . . . . . . 4978 1 881 . 1 1 136 136 ASP N N 15 122.15 0.10 . 1 . . . . . . . . 4978 1 882 . 1 1 137 137 THR H H 1 8.56 0.03 . 1 . . . . . . . . 4978 1 883 . 1 1 137 137 THR HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 884 . 1 1 137 137 THR HB H 1 4.71 0.07 . 1 . . . . . . . . 4978 1 885 . 1 1 137 137 THR C C 13 176.71 0.15 . 1 . . . . . . . . 4978 1 886 . 1 1 137 137 THR CA C 13 62.11 0.25 . 1 . . . . . . . . 4978 1 887 . 1 1 137 137 THR N N 15 116.76 0.10 . 1 . . . . . . . . 4978 1 888 . 1 1 138 138 ASP H H 1 8.53 0.03 . 1 . . . . . . . . 4978 1 889 . 1 1 138 138 ASP HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 890 . 1 1 138 138 ASP C C 13 177.55 0.15 . 1 . . . . . . . . 4978 1 891 . 1 1 138 138 ASP CA C 13 51.33 0.25 . 1 . . . . . . . . 4978 1 892 . 1 1 138 138 ASP CB C 13 40.54 0.25 . 1 . . . . . . . . 4978 1 893 . 1 1 138 138 ASP N N 15 122.07 0.10 . 1 . . . . . . . . 4978 1 894 . 1 1 139 139 GLY H H 1 8.62 0.03 . 1 . . . . . . . . 4978 1 895 . 1 1 139 139 GLY HA2 H 1 4.09 0.07 . 2 . . . . . . . . 4978 1 896 . 1 1 139 139 GLY HA3 H 1 3.45 0.07 . 2 . . . . . . . . 4978 1 897 . 1 1 139 139 GLY C C 13 172.77 0.15 . 1 . . . . . . . . 4978 1 898 . 1 1 139 139 GLY CA C 13 44.30 0.25 . 1 . . . . . . . . 4978 1 899 . 1 1 139 139 GLY N N 15 107.57 0.10 . 1 . . . . . . . . 4978 1 900 . 1 1 140 140 ALA H H 1 7.81 0.03 . 1 . . . . . . . . 4978 1 901 . 1 1 140 140 ALA HA H 1 5.08 0.07 . 1 . . . . . . . . 4978 1 902 . 1 1 140 140 ALA C C 13 172.21 0.15 . 1 . . . . . . . . 4978 1 903 . 1 1 140 140 ALA CA C 13 52.03 0.25 . 1 . . . . . . . . 4978 1 904 . 1 1 140 140 ALA CB C 13 19.92 0.25 . 1 . . . . . . . . 4978 1 905 . 1 1 140 140 ALA N N 15 124.62 0.10 . 1 . . . . . . . . 4978 1 906 . 1 1 141 141 LEU H H 1 9.16 0.03 . 1 . . . . . . . . 4978 1 907 . 1 1 141 141 LEU HA H 1 5.00 0.07 . 1 . . . . . . . . 4978 1 908 . 1 1 141 141 LEU C C 13 172.63 0.15 . 1 . . . . . . . . 4978 1 909 . 1 1 141 141 LEU CA C 13 53.90 0.25 . 1 . . . . . . . . 4978 1 910 . 1 1 141 141 LEU CB C 13 44.76 0.25 . 1 . . . . . . . . 4978 1 911 . 1 1 141 141 LEU N N 15 115.29 0.10 . 1 . . . . . . . . 4978 1 912 . 1 1 142 142 TRP H H 1 9.63 0.03 . 1 . . . . . . . . 4978 1 913 . 1 1 142 142 TRP HA H 1 5.89 0.07 . 1 . . . . . . . . 4978 1 914 . 1 1 142 142 TRP HD1 H 1 7.31 0.07 . 1 . . . . . . . . 4978 1 915 . 1 1 142 142 TRP HE1 H 1 10.28 0.03 . 1 . . . . . . . . 4978 1 916 . 1 1 142 142 TRP C C 13 176.85 0.15 . 1 . . . . . . . . 4978 1 917 . 1 1 142 142 TRP CA C 13 55.31 0.25 . 1 . . . . . . . . 4978 1 918 . 1 1 142 142 TRP CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 919 . 1 1 142 142 TRP N N 15 127.49 0.10 . 1 . . . . . . . . 4978 1 920 . 1 1 142 142 TRP NE1 N 15 130.11 0.10 . 1 . . . . . . . . 4978 1 921 . 1 1 143 143 LEU H H 1 9.87 0.03 . 1 . . . . . . . . 4978 1 922 . 1 1 143 143 LEU HA H 1 5.53 0.07 . 1 . . . . . . . . 4978 1 923 . 1 1 143 143 LEU C C 13 177.55 0.15 . 1 . . . . . . . . 4978 1 924 . 1 1 143 143 LEU CA C 13 57.50 0.25 . 1 . . . . . . . . 4978 1 925 . 1 1 143 143 LEU CB C 13 44.76 0.25 . 1 . . . . . . . . 4978 1 926 . 1 1 143 143 LEU N N 15 122.78 0.10 . 1 . . . . . . . . 4978 1 927 . 1 1 144 144 GLY H H 1 8.62 0.03 . 1 . . . . . . . . 4978 1 928 . 1 1 144 144 GLY HA2 H 1 3.28 0.07 . 2 . . . . . . . . 4978 1 929 . 1 1 144 144 GLY C C 13 172.21 0.15 . 1 . . . . . . . . 4978 1 930 . 1 1 144 144 GLY N N 15 109.65 0.10 . 1 . . . . . . . . 4978 1 931 . 1 1 145 145 GLY H H 1 7.38 0.03 . 1 . . . . . . . . 4978 1 932 . 1 1 145 145 GLY HA2 H 1 3.84 0.07 . 2 . . . . . . . . 4978 1 933 . 1 1 145 145 GLY C C 13 169.95 0.15 . 1 . . . . . . . . 4978 1 934 . 1 1 145 145 GLY CA C 13 45.70 0.25 . 1 . . . . . . . . 4978 1 935 . 1 1 145 145 GLY N N 15 106.30 0.10 . 1 . . . . . . . . 4978 1 936 . 1 1 146 146 MET H H 1 7.13 0.03 . 1 . . . . . . . . 4978 1 937 . 1 1 146 146 MET HA H 1 3.64 0.07 . 1 . . . . . . . . 4978 1 938 . 1 1 146 146 MET HB2 H 1 0.75 0.07 . 4 . . . . . . . . 4978 1 939 . 1 1 146 146 MET C C 13 174.87 0.15 . 1 . . . . . . . . 4978 1 940 . 1 1 146 146 MET CA C 13 52.26 0.25 . 1 . . . . . . . . 4978 1 941 . 1 1 146 146 MET CB C 13 33.51 0.25 . 1 . . . . . . . . 4978 1 942 . 1 1 146 146 MET N N 15 114.02 0.10 . 1 . . . . . . . . 4978 1 943 . 1 1 147 147 GLU H H 1 7.36 0.03 . 1 . . . . . . . . 4978 1 944 . 1 1 147 147 GLU HA H 1 3.91 0.07 . 1 . . . . . . . . 4978 1 945 . 1 1 147 147 GLU HB2 H 1 1.47 0.07 . 2 . . . . . . . . 4978 1 946 . 1 1 147 147 GLU C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 947 . 1 1 147 147 GLU CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 948 . 1 1 147 147 GLU CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 949 . 1 1 147 147 GLU N N 15 123.46 0.10 . 1 . . . . . . . . 4978 1 950 . 1 1 148 148 ARG H H 1 7.56 0.03 . 1 . . . . . . . . 4978 1 951 . 1 1 148 148 ARG HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 952 . 1 1 148 148 ARG HB2 H 1 1.56 0.07 . 2 . . . . . . . . 4978 1 953 . 1 1 148 148 ARG C C 13 175.44 0.15 . 1 . . . . . . . . 4978 1 954 . 1 1 148 148 ARG CA C 13 54.61 0.25 . 1 . . . . . . . . 4978 1 955 . 1 1 148 148 ARG CB C 13 30.70 0.25 . 1 . . . . . . . . 4978 1 956 . 1 1 148 148 ARG N N 15 119.39 0.10 . 1 . . . . . . . . 4978 1 957 . 1 1 149 149 LEU H H 1 7.30 0.03 . 1 . . . . . . . . 4978 1 958 . 1 1 149 149 LEU HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 959 . 1 1 149 149 LEU HD11 H 1 1.20 0.07 . 4 . . . . . . . . 4978 1 960 . 1 1 149 149 LEU HD12 H 1 1.20 0.07 . 4 . . . . . . . . 4978 1 961 . 1 1 149 149 LEU HD13 H 1 1.20 0.07 . 4 . . . . . . . . 4978 1 962 . 1 1 149 149 LEU C C 13 174.03 0.15 . 1 . . . . . . . . 4978 1 963 . 1 1 149 149 LEU CA C 13 51.56 0.25 . 1 . . . . . . . . 4978 1 964 . 1 1 149 149 LEU CB C 13 41.01 0.25 . 1 . . . . . . . . 4978 1 965 . 1 1 149 149 LEU N N 15 122.65 0.10 . 1 . . . . . . . . 4978 1 966 . 1 1 150 150 SER H H 1 7.48 0.03 . 1 . . . . . . . . 4978 1 967 . 1 1 150 150 SER HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 968 . 1 1 150 150 SER HB2 H 1 3.83 0.07 . 2 . . . . . . . . 4978 1 969 . 1 1 150 150 SER HB3 H 1 3.91 0.07 . 2 . . . . . . . . 4978 1 970 . 1 1 150 150 SER C C 13 175.44 0.15 . 1 . . . . . . . . 4978 1 971 . 1 1 150 150 SER CA C 13 56.01 0.25 . 1 . . . . . . . . 4978 1 972 . 1 1 150 150 SER CB C 13 65.62 0.25 . 1 . . . . . . . . 4978 1 973 . 1 1 150 150 SER N N 15 113.50 0.10 . 1 . . . . . . . . 4978 1 974 . 1 1 151 151 VAL H H 1 8.91 0.03 . 1 . . . . . . . . 4978 1 975 . 1 1 151 151 VAL C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 976 . 1 1 151 151 VAL CA C 13 65.62 0.25 . 1 . . . . . . . . 4978 1 977 . 1 1 151 151 VAL N N 15 124.25 0.10 . 1 . . . . . . . . 4978 1 978 . 1 1 152 152 ALA H H 1 8.66 0.03 . 1 . . . . . . . . 4978 1 979 . 1 1 152 152 ALA HA H 1 4.10 0.07 . 1 . . . . . . . . 4978 1 980 . 1 1 152 152 ALA HB1 H 1 1.21 0.07 . 1 . . . . . . . . 4978 1 981 . 1 1 152 152 ALA HB2 H 1 1.21 0.07 . 1 . . . . . . . . 4978 1 982 . 1 1 152 152 ALA HB3 H 1 1.21 0.07 . 1 . . . . . . . . 4978 1 983 . 1 1 152 152 ALA C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 984 . 1 1 152 152 ALA CB C 13 17.34 0.25 . 1 . . . . . . . . 4978 1 985 . 1 1 152 152 ALA N N 15 126.99 0.10 . 1 . . . . . . . . 4978 1 986 . 1 1 153 153 HIS H H 1 7.43 0.03 . 1 . . . . . . . . 4978 1 987 . 1 1 153 153 HIS HA H 1 4.73 0.07 . 1 . . . . . . . . 4978 1 988 . 1 1 153 153 HIS HB2 H 1 3.64 0.07 . 2 . . . . . . . . 4978 1 989 . 1 1 153 153 HIS C C 13 176.28 0.15 . 1 . . . . . . . . 4978 1 990 . 1 1 153 153 HIS CA C 13 57.66 0.25 . 1 . . . . . . . . 4978 1 991 . 1 1 153 153 HIS CB C 13 28.36 0.25 . 1 . . . . . . . . 4978 1 992 . 1 1 153 153 HIS N N 15 123.34 0.10 . 1 . . . . . . . . 4978 1 993 . 1 1 154 154 LYS H H 1 7.46 0.03 . 1 . . . . . . . . 4978 1 994 . 1 1 154 154 LYS HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 995 . 1 1 154 154 LYS HB2 H 1 1.48 0.07 . 2 . . . . . . . . 4978 1 996 . 1 1 154 154 LYS C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 997 . 1 1 154 154 LYS CA C 13 54.84 0.25 . 1 . . . . . . . . 4978 1 998 . 1 1 154 154 LYS CB C 13 29.53 0.25 . 1 . . . . . . . . 4978 1 999 . 1 1 154 154 LYS N N 15 116.86 0.10 . 1 . . . . . . . . 4978 1 1000 . 1 1 155 155 LEU H H 1 7.80 0.03 . 1 . . . . . . . . 4978 1 1001 . 1 1 155 155 LEU HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 1002 . 1 1 155 155 LEU C C 13 177.69 0.15 . 1 . . . . . . . . 4978 1 1003 . 1 1 155 155 LEU CA C 13 53.44 0.25 . 1 . . . . . . . . 4978 1 1004 . 1 1 155 155 LEU CB C 13 41.95 0.25 . 1 . . . . . . . . 4978 1 1005 . 1 1 155 155 LEU N N 15 124.03 0.10 . 1 . . . . . . . . 4978 1 1006 . 1 1 156 156 PRO HA H 1 4.46 0.07 . 1 . . . . . . . . 4978 1 1007 . 1 1 156 156 PRO C C 13 177.97 0.15 . 1 . . . . . . . . 4978 1 1008 . 1 1 156 156 PRO CA C 13 62.34 0.25 . 1 . . . . . . . . 4978 1 1009 . 1 1 156 156 PRO CB C 13 31.40 0.25 . 1 . . . . . . . . 4978 1 1010 . 1 1 157 157 LYS H H 1 8.96 0.03 . 1 . . . . . . . . 4978 1 1011 . 1 1 157 157 LYS HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 1012 . 1 1 157 157 LYS HB2 H 1 1.38 0.07 . 2 . . . . . . . . 4978 1 1013 . 1 1 157 157 LYS C C 13 178.67 0.15 . 1 . . . . . . . . 4978 1 1014 . 1 1 157 157 LYS CA C 13 58.36 0.25 . 1 . . . . . . . . 4978 1 1015 . 1 1 157 157 LYS CB C 13 30.47 0.25 . 1 . . . . . . . . 4978 1 1016 . 1 1 157 157 LYS N N 15 127.26 0.10 . 1 . . . . . . . . 4978 1 1017 . 1 1 158 158 ALA H H 1 8.80 0.03 . 1 . . . . . . . . 4978 1 1018 . 1 1 158 158 ALA HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 1019 . 1 1 158 158 ALA HB1 H 1 1.62 0.07 . 1 . . . . . . . . 4978 1 1020 . 1 1 158 158 ALA HB2 H 1 1.62 0.07 . 1 . . . . . . . . 4978 1 1021 . 1 1 158 158 ALA HB3 H 1 1.62 0.07 . 1 . . . . . . . . 4978 1 1022 . 1 1 158 158 ALA C C 13 178.25 0.15 . 1 . . . . . . . . 4978 1 1023 . 1 1 158 158 ALA CA C 13 54.84 0.25 . 1 . . . . . . . . 4978 1 1024 . 1 1 158 158 ALA CB C 13 21.09 0.25 . 1 . . . . . . . . 4978 1 1025 . 1 1 158 158 ALA N N 15 123.70 0.10 . 1 . . . . . . . . 4978 1 1026 . 1 1 159 159 TYR H H 1 7.85 0.03 . 1 . . . . . . . . 4978 1 1027 . 1 1 159 159 TYR HA H 1 3.82 0.07 . 1 . . . . . . . . 4978 1 1028 . 1 1 159 159 TYR HB2 H 1 2.66 0.07 . 2 . . . . . . . . 4978 1 1029 . 1 1 159 159 TYR HB3 H 1 2.80 0.07 . 2 . . . . . . . . 4978 1 1030 . 1 1 159 159 TYR C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 1031 . 1 1 159 159 TYR CA C 13 60.47 0.25 . 1 . . . . . . . . 4978 1 1032 . 1 1 159 159 TYR CB C 13 36.33 0.25 . 1 . . . . . . . . 4978 1 1033 . 1 1 159 159 TYR N N 15 111.43 0.10 . 1 . . . . . . . . 4978 1 1034 . 1 1 160 160 SER H H 1 7.54 0.03 . 1 . . . . . . . . 4978 1 1035 . 1 1 160 160 SER HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 1036 . 1 1 160 160 SER HB2 H 1 3.82 0.07 . 2 . . . . . . . . 4978 1 1037 . 1 1 160 160 SER C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 1038 . 1 1 160 160 SER CA C 13 56.72 0.25 . 1 . . . . . . . . 4978 1 1039 . 1 1 160 160 SER CB C 13 62.34 0.25 . 1 . . . . . . . . 4978 1 1040 . 1 1 160 160 SER N N 15 111.21 0.10 . 1 . . . . . . . . 4978 1 1041 . 1 1 161 161 THR H H 1 7.35 0.03 . 1 . . . . . . . . 4978 1 1042 . 1 1 161 161 THR HA H 1 4.36 0.07 . 1 . . . . . . . . 4978 1 1043 . 1 1 161 161 THR HB H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 1044 . 1 1 161 161 THR HG21 H 1 1.17 0.07 . 1 . . . . . . . . 4978 1 1045 . 1 1 161 161 THR HG22 H 1 1.17 0.07 . 1 . . . . . . . . 4978 1 1046 . 1 1 161 161 THR HG23 H 1 1.17 0.07 . 1 . . . . . . . . 4978 1 1047 . 1 1 161 161 THR C C 13 173.19 0.15 . 1 . . . . . . . . 4978 1 1048 . 1 1 161 161 THR CA C 13 60.70 0.25 . 1 . . . . . . . . 4978 1 1049 . 1 1 161 161 THR CB C 13 69.61 0.25 . 1 . . . . . . . . 4978 1 1050 . 1 1 161 161 THR N N 15 119.39 0.10 . 1 . . . . . . . . 4978 1 1051 . 1 1 162 162 GLY H H 1 8.87 0.03 . 1 . . . . . . . . 4978 1 1052 . 1 1 162 162 GLY HA2 H 1 4.27 0.07 . 2 . . . . . . . . 4978 1 1053 . 1 1 162 162 GLY C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 1054 . 1 1 162 162 GLY CA C 13 44.76 0.25 . 1 . . . . . . . . 4978 1 1055 . 1 1 162 162 GLY N N 15 116.50 0.10 . 1 . . . . . . . . 4978 1 1056 . 1 1 163 163 PHE H H 1 8.80 0.03 . 1 . . . . . . . . 4978 1 1057 . 1 1 163 163 PHE HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 1058 . 1 1 163 163 PHE HB2 H 1 2.48 0.07 . 2 . . . . . . . . 4978 1 1059 . 1 1 163 163 PHE HB3 H 1 3.20 0.07 . 2 . . . . . . . . 4978 1 1060 . 1 1 163 163 PHE C C 13 173.75 0.15 . 1 . . . . . . . . 4978 1 1061 . 1 1 163 163 PHE CA C 13 57.89 0.25 . 1 . . . . . . . . 4978 1 1062 . 1 1 163 163 PHE CB C 13 39.16 0.25 . 1 . . . . . . . . 4978 1 1063 . 1 1 163 163 PHE N N 15 127.35 0.10 . 1 . . . . . . . . 4978 1 1064 . 1 1 164 164 ILE H H 1 6.20 0.03 . 1 . . . . . . . . 4978 1 1065 . 1 1 164 164 ILE HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 1066 . 1 1 164 164 ILE HB H 1 1.20 0.07 . 4 . . . . . . . . 4978 1 1067 . 1 1 164 164 ILE HG12 H 1 2.11 0.07 . 4 . . . . . . . . 4978 1 1068 . 1 1 164 164 ILE C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 1069 . 1 1 164 164 ILE CA C 13 59.30 0.25 . 1 . . . . . . . . 4978 1 1070 . 1 1 164 164 ILE CB C 13 37.97 0.25 . 1 . . . . . . . . 4978 1 1071 . 1 1 164 164 ILE N N 15 126.16 0.10 . 1 . . . . . . . . 4978 1 1072 . 1 1 165 165 GLY H H 1 8.08 0.03 . 1 . . . . . . . . 4978 1 1073 . 1 1 165 165 GLY HA2 H 1 3.82 0.07 . 2 . . . . . . . . 4978 1 1074 . 1 1 165 165 GLY C C 13 171.50 0.15 . 1 . . . . . . . . 4978 1 1075 . 1 1 165 165 GLY CA C 13 44.06 0.25 . 1 . . . . . . . . 4978 1 1076 . 1 1 165 165 GLY N N 15 115.63 0.10 . 1 . . . . . . . . 4978 1 1077 . 1 1 166 166 CYS H H 1 9.30 0.03 . 1 . . . . . . . . 4978 1 1078 . 1 1 166 166 CYS HA H 1 6.43 0.07 . 1 . . . . . . . . 4978 1 1079 . 1 1 166 166 CYS HB2 H 1 3.10 0.07 . 2 . . . . . . . . 4978 1 1080 . 1 1 166 166 CYS C C 13 172.63 0.15 . 1 . . . . . . . . 4978 1 1081 . 1 1 166 166 CYS CA C 13 53.44 0.25 . 1 . . . . . . . . 4978 1 1082 . 1 1 166 166 CYS CB C 13 47.34 0.25 . 1 . . . . . . . . 4978 1 1083 . 1 1 166 166 CYS N N 15 118.54 0.10 . 1 . . . . . . . . 4978 1 1084 . 1 1 167 167 ILE H H 1 9.10 0.03 . 1 . . . . . . . . 4978 1 1085 . 1 1 167 167 ILE HA H 1 5.35 0.07 . 1 . . . . . . . . 4978 1 1086 . 1 1 167 167 ILE C C 13 173.33 0.15 . 1 . . . . . . . . 4978 1 1087 . 1 1 167 167 ILE CA C 13 60.94 0.25 . 1 . . . . . . . . 4978 1 1088 . 1 1 167 167 ILE CB C 13 41.01 0.25 . 1 . . . . . . . . 4978 1 1089 . 1 1 167 167 ILE N N 15 120.87 0.10 . 1 . . . . . . . . 4978 1 1090 . 1 1 168 168 ARG H H 1 8.86 0.03 . 1 . . . . . . . . 4978 1 1091 . 1 1 168 168 ARG HA H 1 4.90 0.07 . 1 . . . . . . . . 4978 1 1092 . 1 1 168 168 ARG C C 13 172.49 0.15 . 1 . . . . . . . . 4978 1 1093 . 1 1 168 168 ARG CA C 13 53.90 0.25 . 1 . . . . . . . . 4978 1 1094 . 1 1 168 168 ARG CB C 13 33.04 0.25 . 1 . . . . . . . . 4978 1 1095 . 1 1 168 168 ARG N N 15 121.84 0.10 . 1 . . . . . . . . 4978 1 1096 . 1 1 169 169 ASP H H 1 8.68 0.03 . 1 . . . . . . . . 4978 1 1097 . 1 1 169 169 ASP HA H 1 4.18 0.07 . 1 . . . . . . . . 4978 1 1098 . 1 1 169 169 ASP C C 13 173.89 0.15 . 1 . . . . . . . . 4978 1 1099 . 1 1 169 169 ASP CA C 13 54.37 0.25 . 1 . . . . . . . . 4978 1 1100 . 1 1 169 169 ASP CB C 13 38.44 0.25 . 1 . . . . . . . . 4978 1 1101 . 1 1 169 169 ASP N N 15 118.37 0.10 . 1 . . . . . . . . 4978 1 1102 . 1 1 170 170 VAL H H 1 8.86 0.03 . 1 . . . . . . . . 4978 1 1103 . 1 1 170 170 VAL HA H 1 4.70 0.07 . 1 . . . . . . . . 4978 1 1104 . 1 1 170 170 VAL C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 1105 . 1 1 170 170 VAL CA C 13 61.41 0.25 . 1 . . . . . . . . 4978 1 1106 . 1 1 170 170 VAL CB C 13 30.00 0.25 . 1 . . . . . . . . 4978 1 1107 . 1 1 170 170 VAL N N 15 120.35 0.10 . 1 . . . . . . . . 4978 1 1108 . 1 1 171 171 ILE H H 1 9.47 0.03 . 1 . . . . . . . . 4978 1 1109 . 1 1 171 171 ILE HA H 1 4.53 0.07 . 1 . . . . . . . . 4978 1 1110 . 1 1 171 171 ILE HB H 1 1.65 0.07 . 1 . . . . . . . . 4978 1 1111 . 1 1 171 171 ILE C C 13 175.86 0.15 . 1 . . . . . . . . 4978 1 1112 . 1 1 171 171 ILE CA C 13 59.30 0.25 . 1 . . . . . . . . 4978 1 1113 . 1 1 171 171 ILE CB C 13 38.44 0.25 . 1 . . . . . . . . 4978 1 1114 . 1 1 171 171 ILE N N 15 130.50 0.10 . 1 . . . . . . . . 4978 1 1115 . 1 1 172 172 VAL H H 1 8.85 0.03 . 1 . . . . . . . . 4978 1 1116 . 1 1 172 172 VAL HA H 1 4.63 0.07 . 1 . . . . . . . . 4978 1 1117 . 1 1 172 172 VAL C C 13 176.00 0.15 . 1 . . . . . . . . 4978 1 1118 . 1 1 172 172 VAL CA C 13 60.00 0.25 . 1 . . . . . . . . 4978 1 1119 . 1 1 172 172 VAL CB C 13 32.34 0.25 . 1 . . . . . . . . 4978 1 1120 . 1 1 172 172 VAL N N 15 127.90 0.10 . 1 . . . . . . . . 4978 1 1121 . 1 1 173 173 ASP H H 1 9.69 0.03 . 1 . . . . . . . . 4978 1 1122 . 1 1 173 173 ASP HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 1123 . 1 1 173 173 ASP C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 1124 . 1 1 173 173 ASP CA C 13 56.02 0.25 . 1 . . . . . . . . 4978 1 1125 . 1 1 173 173 ASP CB C 13 38.44 0.25 . 1 . . . . . . . . 4978 1 1126 . 1 1 173 173 ASP N N 15 129.95 0.10 . 1 . . . . . . . . 4978 1 1127 . 1 1 174 174 ARG H H 1 8.35 0.03 . 1 . . . . . . . . 4978 1 1128 . 1 1 174 174 ARG HA H 1 3.37 0.07 . 4 . . . . . . . . 4978 1 1129 . 1 1 174 174 ARG C C 13 174.88 0.15 . 1 . . . . . . . . 4978 1 1130 . 1 1 174 174 ARG CA C 13 57.42 0.25 . 1 . . . . . . . . 4978 1 1131 . 1 1 174 174 ARG CB C 13 26.48 0.25 . 1 . . . . . . . . 4978 1 1132 . 1 1 174 174 ARG N N 15 107.79 0.10 . 1 . . . . . . . . 4978 1 1133 . 1 1 175 175 GLN H H 1 7.95 0.03 . 1 . . . . . . . . 4978 1 1134 . 1 1 175 175 GLN HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 1135 . 1 1 175 175 GLN HB2 H 1 2.01 0.07 . 2 . . . . . . . . 4978 1 1136 . 1 1 175 175 GLN HG2 H 1 2.50 0.07 . 2 . . . . . . . . 4978 1 1137 . 1 1 175 175 GLN HE21 H 1 7.99 0.03 . 2 . . . . . . . . 4978 1 1138 . 1 1 175 175 GLN HE22 H 1 6.76 0.03 . 2 . . . . . . . . 4978 1 1139 . 1 1 175 175 GLN C C 13 174.17 0.15 . 1 . . . . . . . . 4978 1 1140 . 1 1 175 175 GLN CA C 13 53.44 0.25 . 1 . . . . . . . . 4978 1 1141 . 1 1 175 175 GLN CB C 13 30.00 0.25 . 1 . . . . . . . . 4978 1 1142 . 1 1 175 175 GLN CD C 13 180.64 0.15 . 1 . . . . . . . . 4978 1 1143 . 1 1 175 175 GLN N N 15 121.38 0.10 . 1 . . . . . . . . 4978 1 1144 . 1 1 175 175 GLN NE2 N 15 112.46 0.10 . 1 . . . . . . . . 4978 1 1145 . 1 1 176 176 GLU C C 13 173.05 0.15 . 1 . . . . . . . . 4978 1 1146 . 1 1 176 176 GLU CB C 13 32.34 0.25 . 1 . . . . . . . . 4978 1 1147 . 1 1 177 177 LEU H H 1 9.05 0.03 . 1 . . . . . . . . 4978 1 1148 . 1 1 177 177 LEU HA H 1 5.17 0.07 . 1 . . . . . . . . 4978 1 1149 . 1 1 177 177 LEU C C 13 173.89 0.15 . 1 . . . . . . . . 4978 1 1150 . 1 1 177 177 LEU CA C 13 53.67 0.25 . 1 . . . . . . . . 4978 1 1151 . 1 1 177 177 LEU CB C 13 40.78 0.25 . 1 . . . . . . . . 4978 1 1152 . 1 1 177 177 LEU N N 15 122.50 0.10 . 1 . . . . . . . . 4978 1 1153 . 1 1 178 178 HIS H H 1 8.68 0.03 . 1 . . . . . . . . 4978 1 1154 . 1 1 178 178 HIS HA H 1 5.44 0.07 . 1 . . . . . . . . 4978 1 1155 . 1 1 178 178 HIS C C 13 175.16 0.15 . 1 . . . . . . . . 4978 1 1156 . 1 1 178 178 HIS CA C 13 54.14 0.25 . 1 . . . . . . . . 4978 1 1157 . 1 1 178 178 HIS CB C 13 26.24 0.25 . 1 . . . . . . . . 4978 1 1158 . 1 1 178 178 HIS N N 15 118.16 0.10 . 1 . . . . . . . . 4978 1 1159 . 1 1 179 179 LEU H H 1 8.56 0.03 . 1 . . . . . . . . 4978 1 1160 . 1 1 179 179 LEU HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 1161 . 1 1 179 179 LEU C C 13 178.25 0.15 . 1 . . . . . . . . 4978 1 1162 . 1 1 179 179 LEU CA C 13 57.66 0.25 . 1 . . . . . . . . 4978 1 1163 . 1 1 179 179 LEU CB C 13 40.78 0.25 . 1 . . . . . . . . 4978 1 1164 . 1 1 179 179 LEU N N 15 125.23 0.10 . 1 . . . . . . . . 4978 1 1165 . 1 1 180 180 VAL H H 1 8.27 0.03 . 1 . . . . . . . . 4978 1 1166 . 1 1 180 180 VAL HA H 1 3.91 0.07 . 1 . . . . . . . . 4978 1 1167 . 1 1 180 180 VAL HB H 1 2.11 0.07 . 1 . . . . . . . . 4978 1 1168 . 1 1 180 180 VAL C C 13 179.10 0.15 . 1 . . . . . . . . 4978 1 1169 . 1 1 180 180 VAL CA C 13 64.45 0.25 . 1 . . . . . . . . 4978 1 1170 . 1 1 180 180 VAL CB C 13 30.94 0.25 . 1 . . . . . . . . 4978 1 1171 . 1 1 180 180 VAL N N 15 114.96 0.10 . 1 . . . . . . . . 4978 1 1172 . 1 1 181 181 GLU H H 1 8.80 0.03 . 1 . . . . . . . . 4978 1 1173 . 1 1 181 181 GLU HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 1174 . 1 1 181 181 GLU C C 13 178.39 0.15 . 1 . . . . . . . . 4978 1 1175 . 1 1 181 181 GLU CA C 13 59.76 0.25 . 1 . . . . . . . . 4978 1 1176 . 1 1 181 181 GLU CB C 13 28.36 0.25 . 1 . . . . . . . . 4978 1 1177 . 1 1 181 181 GLU N N 15 118.73 0.10 . 1 . . . . . . . . 4978 1 1178 . 1 1 182 182 ASP H H 1 8.58 0.03 . 1 . . . . . . . . 4978 1 1179 . 1 1 182 182 ASP HA H 1 4.99 0.07 . 1 . . . . . . . . 4978 1 1180 . 1 1 182 182 ASP HB2 H 1 3.09 0.07 . 2 . . . . . . . . 4978 1 1181 . 1 1 182 182 ASP C C 13 175.72 0.15 . 1 . . . . . . . . 4978 1 1182 . 1 1 182 182 ASP CA C 13 54.84 0.25 . 1 . . . . . . . . 4978 1 1183 . 1 1 182 182 ASP CB C 13 39.84 0.25 . 1 . . . . . . . . 4978 1 1184 . 1 1 182 182 ASP N N 15 115.01 0.10 . 1 . . . . . . . . 4978 1 1185 . 1 1 183 183 ALA H H 1 6.94 0.03 . 1 . . . . . . . . 4978 1 1186 . 1 1 183 183 ALA HA H 1 3.99 0.07 . 1 . . . . . . . . 4978 1 1187 . 1 1 183 183 ALA HB1 H 1 1.29 0.07 . 1 . . . . . . . . 4978 1 1188 . 1 1 183 183 ALA HB2 H 1 1.29 0.07 . 1 . . . . . . . . 4978 1 1189 . 1 1 183 183 ALA HB3 H 1 1.29 0.07 . 1 . . . . . . . . 4978 1 1190 . 1 1 183 183 ALA C C 13 180.08 0.15 . 1 . . . . . . . . 4978 1 1191 . 1 1 183 183 ALA CA C 13 52.03 0.25 . 1 . . . . . . . . 4978 1 1192 . 1 1 183 183 ALA CB C 13 17.11 0.25 . 1 . . . . . . . . 4978 1 1193 . 1 1 183 183 ALA N N 15 122.92 0.10 . 1 . . . . . . . . 4978 1 1194 . 1 1 184 184 LEU H H 1 8.98 0.03 . 1 . . . . . . . . 4978 1 1195 . 1 1 184 184 LEU HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 1196 . 1 1 184 184 LEU C C 13 178.11 0.15 . 1 . . . . . . . . 4978 1 1197 . 1 1 184 184 LEU CA C 13 54.14 0.25 . 1 . . . . . . . . 4978 1 1198 . 1 1 184 184 LEU CB C 13 41.72 0.25 . 1 . . . . . . . . 4978 1 1199 . 1 1 184 184 LEU N N 15 120.61 0.10 . 1 . . . . . . . . 4978 1 1200 . 1 1 185 185 ASN H H 1 8.53 0.03 . 1 . . . . . . . . 4978 1 1201 . 1 1 185 185 ASN HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 1202 . 1 1 185 185 ASN HB2 H 1 2.60 0.07 . 2 . . . . . . . . 4978 1 1203 . 1 1 185 185 ASN C C 13 173.89 0.15 . 1 . . . . . . . . 4978 1 1204 . 1 1 185 185 ASN CA C 13 52.50 0.25 . 1 . . . . . . . . 4978 1 1205 . 1 1 185 185 ASN CB C 13 41.72 0.25 . 1 . . . . . . . . 4978 1 1206 . 1 1 185 185 ASN N N 15 115.13 0.10 . 1 . . . . . . . . 4978 1 1207 . 1 1 186 186 ASN H H 1 8.60 0.03 . 1 . . . . . . . . 4978 1 1208 . 1 1 186 186 ASN HA H 1 4.45 0.07 . 1 . . . . . . . . 4978 1 1209 . 1 1 186 186 ASN C C 13 174.74 0.15 . 1 . . . . . . . . 4978 1 1210 . 1 1 186 186 ASN CA C 13 52.97 0.25 . 1 . . . . . . . . 4978 1 1211 . 1 1 186 186 ASN CB C 13 37.50 0.25 . 1 . . . . . . . . 4978 1 1212 . 1 1 186 186 ASN N N 15 116.71 0.10 . 1 . . . . . . . . 4978 1 1213 . 1 1 187 187 PRO HA H 1 4.51 0.07 . 1 . . . . . . . . 4978 1 1214 . 1 1 187 187 PRO C C 13 176.56 0.15 . 1 . . . . . . . . 4978 1 1215 . 1 1 187 187 PRO CA C 13 62.34 0.25 . 1 . . . . . . . . 4978 1 1216 . 1 1 187 187 PRO CB C 13 31.17 0.25 . 1 . . . . . . . . 4978 1 1217 . 1 1 188 188 THR H H 1 8.48 0.03 . 1 . . . . . . . . 4978 1 1218 . 1 1 188 188 THR HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 1219 . 1 1 188 188 THR HB H 1 4.02 0.07 . 1 . . . . . . . . 4978 1 1220 . 1 1 188 188 THR C C 13 173.75 0.15 . 1 . . . . . . . . 4978 1 1221 . 1 1 188 188 THR CA C 13 62.34 0.25 . 1 . . . . . . . . 4978 1 1222 . 1 1 188 188 THR CB C 13 67.97 0.25 . 1 . . . . . . . . 4978 1 1223 . 1 1 188 188 THR N N 15 118.33 0.10 . 1 . . . . . . . . 4978 1 1224 . 1 1 189 189 ILE H H 1 8.30 0.03 . 1 . . . . . . . . 4978 1 1225 . 1 1 189 189 ILE HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 1226 . 1 1 189 189 ILE HB H 1 1.83 0.07 . 1 . . . . . . . . 4978 1 1227 . 1 1 189 189 ILE C C 13 175.02 0.15 . 1 . . . . . . . . 4978 1 1228 . 1 1 189 189 ILE CA C 13 58.36 0.25 . 1 . . . . . . . . 4978 1 1229 . 1 1 189 189 ILE CB C 13 36.09 0.25 . 1 . . . . . . . . 4978 1 1230 . 1 1 189 189 ILE N N 15 128.05 0.10 . 1 . . . . . . . . 4978 1 1231 . 1 1 190 190 LEU H H 1 9.16 0.03 . 1 . . . . . . . . 4978 1 1232 . 1 1 190 190 LEU HA H 1 4.54 0.07 . 1 . . . . . . . . 4978 1 1233 . 1 1 190 190 LEU C C 13 176.14 0.15 . 1 . . . . . . . . 4978 1 1234 . 1 1 190 190 LEU CA C 13 52.50 0.25 . 1 . . . . . . . . 4978 1 1235 . 1 1 190 190 LEU CB C 13 42.66 0.25 . 1 . . . . . . . . 4978 1 1236 . 1 1 190 190 LEU N N 15 131.41 0.10 . 1 . . . . . . . . 4978 1 1237 . 1 1 191 191 HIS H H 1 8.68 0.03 . 1 . . . . . . . . 4978 1 1238 . 1 1 191 191 HIS HA H 1 4.81 0.07 . 1 . . . . . . . . 4978 1 1239 . 1 1 191 191 HIS HB2 H 1 2.87 0.07 . 2 . . . . . . . . 4978 1 1240 . 1 1 191 191 HIS C C 13 175.16 0.15 . 1 . . . . . . . . 4978 1 1241 . 1 1 191 191 HIS CA C 13 55.53 0.25 . 1 . . . . . . . . 4978 1 1242 . 1 1 191 191 HIS CB C 13 29.30 0.25 . 1 . . . . . . . . 4978 1 1243 . 1 1 191 191 HIS N N 15 120.01 0.10 . 1 . . . . . . . . 4978 1 1244 . 1 1 192 192 CYS H H 1 8.28 0.03 . 1 . . . . . . . . 4978 1 1245 . 1 1 192 192 CYS HA H 1 4.72 0.07 . 1 . . . . . . . . 4978 1 1246 . 1 1 192 192 CYS C C 13 174.03 0.15 . 1 . . . . . . . . 4978 1 1247 . 1 1 192 192 CYS CA C 13 56.48 0.00 . 1 . . . . . . . . 4978 1 1248 . 1 1 192 192 CYS CB C 13 43.36 0.25 . 1 . . . . . . . . 4978 1 1249 . 1 1 192 192 CYS N N 15 122.03 0.10 . 1 . . . . . . . . 4978 1 1250 . 1 1 193 193 SER H H 1 8.58 0.03 . 1 . . . . . . . . 4978 1 1251 . 1 1 193 193 SER HA H 1 4.00 0.07 . 1 . . . . . . . . 4978 1 1252 . 1 1 193 193 SER HB2 H 1 3.91 0.07 . 2 . . . . . . . . 4978 1 1253 . 1 1 193 193 SER C C 13 170.24 0.15 . 1 . . . . . . . . 4978 1 1254 . 1 1 193 193 SER CA C 13 57.89 0.25 . 1 . . . . . . . . 4978 1 1255 . 1 1 193 193 SER CB C 13 62.81 0.25 . 1 . . . . . . . . 4978 1 1256 . 1 1 193 193 SER N N 15 121.18 0.10 . 1 . . . . . . . . 4978 1 1257 . 1 1 194 194 ALA H H 1 8.28 0.03 . 1 . . . . . . . . 4978 1 1258 . 1 1 194 194 ALA HA H 1 4.27 0.07 . 1 . . . . . . . . 4978 1 1259 . 1 1 194 194 ALA HB1 H 1 1.39 0.07 . 1 . . . . . . . . 4978 1 1260 . 1 1 194 194 ALA HB2 H 1 1.39 0.07 . 1 . . . . . . . . 4978 1 1261 . 1 1 194 194 ALA HB3 H 1 1.39 0.07 . 1 . . . . . . . . 4978 1 1262 . 1 1 194 194 ALA C C 13 176.55 0.15 . 1 . . . . . . . . 4978 1 1263 . 1 1 194 194 ALA CA C 13 51.80 0.25 . 1 . . . . . . . . 4978 1 1264 . 1 1 194 194 ALA CB C 13 18.28 0.25 . 1 . . . . . . . . 4978 1 1265 . 1 1 194 194 ALA N N 15 127.45 0.10 . 1 . . . . . . . . 4978 1 1266 . 1 1 195 195 LYS H H 1 7.78 0.03 . 1 . . . . . . . . 4978 1 1267 . 1 1 195 195 LYS HA H 1 4.09 0.07 . 1 . . . . . . . . 4978 1 1268 . 1 1 195 195 LYS HB2 H 1 1.65 0.07 . 4 . . . . . . . . 4978 1 1269 . 1 1 195 195 LYS HB3 H 1 1.29 0.07 . 4 . . . . . . . . 4978 1 1270 . 1 1 195 195 LYS C C 13 181.84 0.15 . 1 . . . . . . . . 4978 1 1271 . 1 1 195 195 LYS CA C 13 56.95 0.25 . 1 . . . . . . . . 4978 1 1272 . 1 1 195 195 LYS CB C 13 32.34 0.25 . 1 . . . . . . . . 4978 1 1273 . 1 1 195 195 LYS N N 15 125.71 0.10 . 1 . . . . . . . . 4978 1 stop_ save_