Karlsen S, Iversen L F, Larsen I K, Flodgaard H J, Kastrup J S
Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):598-609. doi: 10.1107/s0907444997016193.
Crystals of human heparin binding protein (HBP) diffract to 1.1 A when flash-frozen at 120 K. The atomic resolution structure has been refined anisotropically using SHELXL96. The final model of HBP consists of 221 amino-acid residues of 225 possible, three glycosylation units, one chloride ion, 15 precipitant ethanol molecules and 323 water molecules. The structure is refined to a final crystallographic R factor of 15.9% and Rfree(5%) of 18.9% using all data. A putative protein kinase C activation site has been identified, involving residues 113-120. The structure is compared to the previously determined 2.3 A resolution structure of HBP.
人肝素结合蛋白（HBP）晶体在120K下快速冷冻时衍射至1.1埃。已使用SHELXL96对原子分辨率结构进行了各向异性精修。HBP的最终模型由225个可能的氨基酸残基中的221个、三个糖基化单元、一个氯离子、15个沉淀剂乙醇分子和323个水分子组成。使用所有数据将该结构精修至最终晶体学R因子为15.9%，Rfree(5%)为18.9%。已鉴定出一个假定的蛋白激酶C激活位点，涉及113 - 120位残基。将该结构与先前确定的分辨率为2.3埃的HBP结构进行了比较。
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