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      <image:caption>Regulation of the number of functionally accessible cardiac myosin heads for interaction with actin</image:caption>
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    <loc>http://spudlab.stanford.edu/lab-movies</loc>
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      <image:title>Lab Movies</image:title>
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  <url>
    <loc>http://spudlab.stanford.edu/homology-models</loc>
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    <lastmod>2017-06-30</lastmod>
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      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1498858447401-MNFHC4T41ZR416XA095V/MS03_5TBY+ELCs+Jun2017.png</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>same as above ELCs only</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1498858357800-KDNYW4ZE9CNGL0S3MD05/MS03_5TBY+RLCs+Jun2017.png</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>Same as above RLCs only</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1498061449605-XRGKKX1WF2APO0DJBOCD/prestroke+poststroke+eval+metrics.jpeg</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>The models were evaluated using ModEval [1] methodology. Evaluation metrics are tabulated for the two models that were developed. The TSVMod predicted Cα root-mean-square deviation (RMSD) shows the Cα-RMSD of the model from the template structure and predicted native overlap provides the fraction of Cα atoms in the model within 3.5 Å of the corresponding atoms in the template structure after rigid-body superposition [2]. zDOPE is a normalized Discrete Optimized Protein Energy (DOPE), an atomic distance-dependent statistical score. Negative values indicate better models [3]. GA341 model score is derived from residue-level statistical potential that was optimized, including distance-dependent, contact, Phi/Psi dihedral angle, and accessible surface statistical potentials. A value &gt; 0.7 generally indicates a reliable model, defined as ≥ 95% probability of correct fold [4]. 1.     Pieper U et al, ModBase, a database of annotated comparative protein structure models, and associated resources. Nucleic Acids Res (2011). 2.     Eramian et al, How well can the accuracy of comparative protein structure models be predicted? Protein Sci (2008). 3.     Shen MY et al, Statistical potential for assessment and prediction of protein structures. Protein Sci (2006) 4.     Melo F et al, Statistical potentials for fold assessment. Protein Sci (2002).</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1494023480824-5IH0GK2WFOX15N1MR1F0/image-asset.jpeg</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>The first homology model of full-length human beta-cardiac myosin S1 was described in Spudich, J.A. (2015). The myosin mesa and a possible unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathy. Biochem Soc Trans. 43:64–72. Also see, Homburger, J.R. et al. Multidimensional structure-function relationships in human β-cardiac myosin from population-scale genetic variation. Proc Natl Acad Sci USA 113, 6701–6706 (2016). Image from Adhikari, A.S., Kooiker, K.B., Sarkar, S.S., Liu, C., Bernstein, D., Spudich, J.A. and Ruppel, K.M. (2016). Early Onset HCM Mutations H251N and D239N Significantly Increase the Velocity, Force, and Actin-activated ATPase activity of human β-cardiac Myosin.  Cell Rep. 17:2857-2864.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1492612443094-LCKA2YYSRBN7Z809RT8A/image-asset.jpeg</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS01C0C2                                    MS01C0C10</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1494092606192-9W9KH7MH4RGEL0V013JR/Slide2.jpg</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS03C0C2                                                        MS03C0C10v3</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1494092834574-VNUPQF0OIFWWTT6DQ3MI/image-asset.jpeg</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS01C0C10                                 MS03C0C10v2                                Ms03C0C10v3</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1498858924417-HWVCJH13BEZORWWU0CH7/MS03_5TBY+complete+Jun2017.png</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS03: HC white, ELCs brown, RLCs green                 5TBY: HC black, ELCs yellow, RLCs blue</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1498858058509-1EXNXJ9FDGENJ4ERHWG8/image-asset.png</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS03: yellow     5TBY: red     From left to right, mesa residues Arg453, Arg249, Arg663     Note different orientations of side chains for MS03 and 5TBY</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1494024908973-BF4TYWPTWNLPAR35BKCH/PDB+MS01%3A+A+complete+folded-back+model+of+human+beta-cardiac+myosin</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS01: A complete folded-back model of human beta-cardiac myosin with human cardiac light chains. The first homology model of the human beta-cardiac myosin in its folded back off-state (IHM motif) was described in Adhikari, A.S., Kooiker, K.B., Sarkar, S.S., Liu, C., Bernstein, D., Spudich, J.A. and Ruppel, K.M. (2016). Early Onset HCM Mutations H251N and D239N Significantly Increase the Velocity, Force, and Actin-activated ATPase activity of human β-cardiac Myosin.  Cell Rep. 17:2857-2864. Image from Nag, S., Trivedi, D.V., Sarkar, S.S., Adhikari, A.S., Sunitha, M.S., Sutton, S., Ruppel, K.M. and Spudich, J.A. The myosin mesa and the basis of hypercontractility caused by hypertrophic cardiomyopathy mutations. Nat. Struct. Mol. Biol., Advance Online Publication. DOI: 10.1038/nsmb.3408 (2017).</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1494024625381-4TG0AZZIA888FPWHQMHI/image-asset.png</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>MS03 showing the location of a number of Arg residues that cause HCM when mutated.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1497558164023-DDREY887ET52K4DM9JKR/image-asset.jpeg</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>The models were evaluated using ModEval [1] methodology. Evaluation metrics are tabulated for the three models that were developed. The TSVMod predicted Cα root-mean-square deviation (RMSD) shows the Cα-RMSD of the model from the template structure and predicted native overlap provides the fraction of Cα atoms in the model within 3.5 Å of the corresponding atoms in the template structure after rigid-body superposition [2]. zDOPE is a normalized Discrete Optimized Protein Energy (DOPE), an atomic distance-dependent statistical score. Negative values indicate better models [3]. GA341 model score is derived from residue-level statistical potential that was optimized, including distance-dependent, contact, Phi/Psi dihedral angle, and accessible surface statistical potentials. A value &gt; 0.7 generally indicates a reliable model, defined as ≥ 95% probability of correct fold [4]. 1.     Pieper U et al, ModBase, a database of annotated comparative protein structure models, and associated resources. Nucleic Acids Res (2011). 2.     Eramian et al, How well can the accuracy of comparative protein structure models be predicted? Protein Sci (2008). 3.     Shen MY et al, Statistical potential for assessment and prediction of protein structures. Protein Sci (2006) 4.     Melo F et al, Statistical potentials for fold assessment. Protein Sci (2002).</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/55cbcdf4e4b0fe0a5d68c8fa/1498858979280-XXFYONR2MM6SOVLRZTMT/MS03_5TBY+wo+LCs+Jun2017.png</image:loc>
      <image:title>Homology models</image:title>
      <image:caption>Same as above without LCs</image:caption>
    </image:image>
  </url>
</urlset>

