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article científic наукова стаття, опублікована в березні 1992 artikull shkencor i botuar më 5 mars 1992 tieteellinen artikkeli 1992年学术文章 1992年學術文章 artículu científicu espublizáu en 1992 wetenschappelijk artikel (gepubliceerd op 1992/03/05) teaduslik artikkel maqolai ilmiy 1992年学术文章 1992년 논문 мақолаи илмӣ bài báo khoa học xuất bản ngày 5 tháng 3, 1992 vitenskapelig artikkel επιστημονικό άρθρο scienca artikolo im 5. März 1992 veröffentlichter wissenschaftlicher Artikel 1992年學術文章 1992 nî ê lūn-bûn article scientific artikulong pang-agham научни чланак објављен 5. март 1992. article scientifique publié le 5 mars 1992 5 Mart 1992'de yayımlanmış bilimsel makale 1992年の学術論文 სამეცნიერო სტატია videnskabelig artikel offentliggjort den 5. marts 1992 1992年学术文章 1992年學術文章 vedecký článok publikovaný 5. marca 1992 научна статия, публикувана на 5 март 1992 г. artigo científico publicado em 5 de março de 1992 vědecký článek publikovaný 5. března 1992 ১৯৯২-এ প্রকাশিত বৈজ্ঞানিক নিবন্ধ znanstveni članek objavljen 5. marec 1992 мақолаи илмӣ mokslinis straipsnis, publikuotas 1992 m. kovo 5 d. 1992年学术文章 scientific article published on 5 March 1992 1992 թվականի մարտին հրատարակված գիտական հոդված artykuł naukowy opublikowany 5 marca 1992 מאמר מדעי articol științific 1992年學術文章 artikel ilmiah научни чланак објављен 5. март 1992. 1992 թուականի Մարտին հրատարակուած գիտական յօդուած مقالة علمية (نشرت في 5-3-1992) บทความทางวิทยาศาสตร์ 1992年学术文章 artículo científico publicado el 5 de marzo de 1992 1992年學術文章 vetenskaplig artikel publicerad den 5 mars 1992 artigo científico научная статья опубликованная 5 марта 1992 г. tudományos cikk scientific article published on March 5, 1992 artigo científico publicado em 5 de março de 1992 1992年學術文章 naučni članak articolo scientifico pubblicato il 5 marzo 1992 vitskapeleg artikkel
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Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state
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Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state
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Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state
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Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state
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