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The research question for this dataset was: How will climate change impact the growth of spring wheat in Fairbanks, Alaska? The DSSAT CERES-Wheat crop simulation model was used to answer this research question. Data consists of DSSAT V4.7.0.0 Files and Field Data. Data in the Field Data files were collected at the University of Alaska Fairbanks small grains variety trial plot in Fairbanks, AK. This field data was input into DSSAT. DSSAT Files were used to calibrate, validate, and apply the DSSAT CERES-Wheat crop simulation model for simulating spring wheat growth (cultivar Ingal) in projected climate change scenarios. These DSSAT files are ready for a modeler to use.
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GIS data associated with Neugarten RA et al. 2020. Trends in protected area representation of biodiversity and ecosystem services in five tropical countries. Ecosystem Services 42:101078. Includes data from Cambodia, Guyana, Liberia, Madagascar, and Suriname Datasets included: country boundaries, protected areas in 2003 and 2017, biodiversity priority areas, forest cover in 2003 and 2015, forest carbon stocks, non-timber forest products, and freshwater ecosystem services
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Primary and raw data from the manuscript "CACNA1S haploinsufficiency confers resistance to New World arenavirus infection"
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Collected data from patients
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Excel and other file sources for the Golden Droplets series
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Data Related to Fig 2. A mouse line carrying floxed Tgfbr2 and SMC lineage-tracing mT/mG alleles under control of a myosin heavy chain (Myh11) promoter on an Ldlr null background (Ldlr-/-;Myh11CreERT2;mT/mGf/f;Tgfbr2f/f) hereafter called TGFβR2iSMC-Ldlr. These mice were treated with Tamoxifen at 6 week of age and fed high cholesterol high fat diet for 4 months. Ascending aorta smooth muscle cells from these mice express macrophage, chondrocyte, adipocyte, and osteoblast lineage markers as shown by immunocytochemistry and qRT-PCT from laser micro dissection tissues compared to controls.
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Data and code files for manuscript submitted to the Journal of Theoretical Biology.
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Hardware design for build a Step Width System Capture
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Different human linker histone (H1) variants are expected to have distinct binding modes to the nucleosome. The position and orientation of a number of different H1 globular domains on the nucleosome were investigated through molecular docking using MGLTools and HADDOCK. The nucleosome core and linker DNA in the GH5-chromatosome structure (PDB: 4QLC) were used as a docking template. GH5 (in PDB: 4QLC) was re-docked to this template to test the docking algorithm. Docked and re-docked GH5 compared well. The docking algorithm was further tested by docking the NMR solution structure of the globular domain of chicken H1 (GH1, PDB: 1GHC) to the nucleosome template. The position of docked GH1 on the nucleosome agreed with literature. 
The N-terminal - and globular domain H1x hybrid (NGH1x) was studied using solution NMR in both low (20 mM sodium phosphate, pH 7.0) and high (20 mM sodium phosphate, 1 M sodium perchlorate, pH 7.0) ionic strength conditions (de Wit, H., Vallet, A., Brutscher, B. et al. Biomol NMR Assign (2019) 13: 249. https://doi.org/10.1007/s12104-019-09886-x). These low and high ionic strength structures were docked to the nucleosome template. 
Homology (MODELLER) and ab initio modeling (CS-ROSETTA) were employed to model structures for other human H1 globular domains: GH1.0, GH1.4, GH1oo, and GH1t. The modeled structures were also docked to the nucleosome template.
 All the docking procedures listed above produced 100 models of different energies. In each case, the lowest energy docked model was chosen. The structures of all the H1 globular domains that were docked to the template are given as PDB files (1GHC_lowest_energy.pdb; 2LSO_lowest_energy.pdb; GH5_re-docked_position.pdb; NGH1x_high_salt_NTD.pdb; NGH1x_low_salt_NTD.pdb; modeled_GH1_0_lowest_energy.pdb; modeled_GH1_4_lowest_energy.pdb; modeled_GH1oo_lowest_energy.pdb; modelled_GH1t_lowest_energy.pdb) in the data file. The nucleosome template structure is also given in PDB file format (4QLC_nucleosome_without_GH5.pdb). Finally, the docked models are also given (GH5-chromatosome.pdb; 1GHC-chromatosome.pdb; 2LSO-chromatosome.pdb; GH1_0-chromatosome.pdb; GH1_4-chromatosome.pdb; GH1oo-chromatosome.pdb; GH1t-chromatosome.pdb; NGH1x_no_salt-chromatosome.pdb; NGH1x_salt-chromatosome.pdb). The files are compatible with most molecular graphics software. The file Dockings_modelling_test_and_results.pdf provides the modeling and docking results in figures and tables. A short description of each figure and table is given within the PDF file.
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