{"references": ["Berman HM, Battistuz T, Bhat TN, Bluhm WF, Bourne PE, Burkhardt K, et al. The protein data bank. Acta Crystallogr Sect D Biol Crystallogr. 2002;58(6 I):899\u2013907.", "Prestegard JH. REVIEWS A perspective on the PDB ' s impact on the fi eld of glycobiology. 2021;(8):1\u201311.", "Chadarevian S De. John Kendrew and myoglobin\u202f: Protein structure determination in the 1950s. 2018;27:1136\u201343.", "Li Z, Albert J, Ve C. topical reviews Cryo-electron microscopy and X-ray crystallography\u202f: complementary approaches to structural biology and drug discovery 1. 2017;174\u201383.", "Ferry G. Osamu Shimomura (1928\u20132018). Nature. 2018;563(7733):627\u2013627.", "G\u00fcnther S, Reinke PYA, Fern\u00e1ndez-Garc\u00eda Y, Lieske J, Lane TJ, Ginn HM, et al. X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease. 2021;646(May):642\u20136.", "Ishima R, Torchia DA. Protein dynamics from NMR. Nat Struct Biol. 2000;7(9):740\u20133.", "Rhs CJ. Magnetic resonance spectroscopy. 2017;100:241\u201392.", "Murata K, Wolf M. Cryo-electron microscopy for structural analysis of dynamic biological macromolecules. Biochim Biophys Acta - Gen Subj [Internet]. 2018;1862(2):324\u201334. Available from: https://doi.org/10.1016/j.bbagen.2017.07.020", "Carroni M, Saibil HR. Cryo electron microscopy to determine the structure of macromolecular complexes. Methods [Internet]. 2016;95:78\u201385. Available from: http://dx.doi.org/10.1016/j.ymeth.2015.11.023", "Hori Y. Crystal structure of the Aequorea victoria green fluorescent protein. Tanpakushitsu Kakusan Koso. 2007;52(13 Suppl):1768\u20139.", "Gayt\u00e1n P, Rold\u00e1n-Salgado A, Y\u00e1\u00f1ez JA, Morales-Arrieta S, Ju\u00e1rez-Gonz\u00e1lez VR. CiPerGenesis, A. Mutagenesis Approach that Produces Small Libraries of Circularly Permuted Proteins Randomly Opened at a Focused Region: Testing on the Green Fluorescent Protein. ACS Comb Sci. 2018;20(7):400\u201313.", "Sawano A, Miyawaki A. Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis. Nucleic Acids Res. 2000;28(16).", "Chalfie M. GFP: lighting up life (Nobel Lecture). Angew Chem Int Ed Engl. 2009;48(31):5603\u201311.", "Cressey D. Roger Tsien's legacy: The creations that lit up biology. Nature. 2020;(September):1\u20135.", "Remington SJ. Green fluorescent protein: A perspective. Protein Sci. 2011;20(9):1509\u201319.", "Yang F, Moss LG, Phillips GN. The Molecular Structure of Green Fluorescent Protein. Nat Biotechnol. 1996;14(10):1246\u201351.", "Zimmer M. Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior. Chem Rev. 2002;102(3):759\u201381.", "Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remingtont SJ. Crystal Structure of the Aequorea victoria Green Fluorescent Protein Author ( s ): Mats Orm\u00f6 , Andrew B . Cubitt , Karen Kallio , Larry A . Gross , Roger Y . Tsien and Published by\u202f: American Association for the Advancement of Science Stable URL\u202f: http://. Science (80- ). 1996;273(5280):1392\u20135.https://www.science.org/doi/10.1126/science.273.5280.1392", "Selisko B, Licea AF, Becerril B, Zamudio F, Possani LD, Horjales E. Antibody BCF2 Against Scorpion Toxin Cn2 From Centruroides noxius Hoffmann\u202f: Primary Structure and Three-Dimensional Model as Free Fv Fragment and Complexed With Its Antigen. 2001;143(January 1999):130\u201343.", "Ju\u00e1rez-Gonz\u00e1lez VR, Ria\u00f1o-Umbarila L, Quintero-Hern\u00e1ndez V, Olamendi-Portugal T, Ortiz-Le\u00f3n M, Ort\u00edz E, et al. Directed evolution, phage display and combination of evolved mutants: A strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2. J Mol Biol. 2005;346(5):1287\u201397.", "Quintero-Hern\u00e1ndez V, Ju\u00e1rez-Gonz\u00e1lez VR, Ort\u00edz-Le\u00f3n M, S\u00e1nchez R, Possani LD, Becerril B. The change of the scFv into the Fab format improves the stability and in vivo toxin neutralization capacity of recombinant antibodies. Mol Immunol. 2007;44(6):1307\u201315.", "Pintar A, Possani LD, Delepierre M. Solution structure of toxin 2 from Centruroides noxius Hoffmann, a \u03b2-scorpion neurotoxin acting on sodium channels. J Mol Biol. 1999;287(2):359\u201367.", "Canul-tec JC, Rian L, Rudin E, Torres-larios A. Structural Basis of Neutralization of the Major Toxic Component from the Scorpion Centruroides noxius Hoffmann by a Human-derived Single-chain Antibody Fragment. 2011;286(23):20892\u2013900.", "Rian L, Ledezma-candanoza LM, Serrano-Posada H, Ferna G, Olamendi-portugal T, Rojas-trejo S, et al. Optimal Neutralization of Centruroides noxius Venom Is Understood through a Structural Complex between Two Antibody Fragments and the Cn2 Toxin. 2016;291(4):1619\u201330.", "Elizalde Gonz\u00e1lez JJ. SARS-CoV-2 y COVID-19. Una revisi\u00f3n de la pandemia. Med Cr\u00edtica. 2020;33(1):53\u201367.", "Casalino L, Gaieb Z, Dommer AC, Harbison AM, Fogarty CA, Barros EP, et al. Shielding and Beyond\u202f: The Roles of Glycans in SARS-CoV-2 Spike Protein. 2020; 28;6(10):1722-1734.", "Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science (80- ). 2020;367(6483):1260\u20133.", "Wilson IA. 50 Years of structural immunology. 2021;1\u201320.", "Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell [Internet]. 2020;181(2):281-292.e6. Available from: http://dx.doi.org/10.1016/j.cell.2020.02.058"]}

RESUMEN El Protein Data Bank (banco de datos de proteínas), abreviado como PDB, es el banco de información estructural de proteínas a nivel atómico, donde están depositadas todas las estructuras tridimensionales de las macromoléculas biológicas determinadas por la comunidad científica mundial y que incluye a proteínas, ácidos nucleicos, carbohidratos y lípidos. Su uso es libre y hasta noviembre del 2021 tiene 184,202 estructuras depositadas. La mayor parte de la información tridimensional con la que cuenta el PDB con respecto a las biomoléculas es la referente a proteínas con 158,644 estructuras depositadas y la técnica más utilizada para la determinación de las estructuras es la difracción de rayos X con 161,144 estructuras depositadas. En este año, el PDB cumple 50 años y la información que nos proporciona ha revolucionado la visión que teníamos sobre los procesos biológicos a nivel atómico. El PDB es una enorme base de datos de estructuras y una fuente de información importante sobre diversas macromoléculas, las cuales pueden ser analizadas por una diversidad de profesionales como: cristalógrafos, químicos, biólogos, bioquímicos, microbiólogos, médicos, farmacéuticos, entre otros. El conocer la estructura de una macromolécula de interés puede ayudar a entender una gran cantidad de procesos químicos, biológicos y enfermedades, ya que entender a detalle atómico la alteración química y estructural de una macromolécula permite descifrar los mecanismos que participan en el proceso químico o biológico de estudio o en una enfermedad y el daño en el organismo; además se puede realizar el diseño de fármacos para su tratamiento. ABSTRACT The Protein Data Bank, abbreviated as PDB, is the structural information bank of proteins at the atomic level, where all the three-dimensional structures of biological macromolecules determined by the world scientific community are deposited and which includes proteins, nucleic acids, carbohydrates, and lipids. Its use is free, and until november 2021 it has 184,202 structures deposited. Most of the three-dimensional information that the PDB has with respect to biomolecules refers to proteins with 158,644 structures deposited and the most used technique for the determination of structures is X-ray diffraction with 161,144 structures deposited. In this year, the PDB celebrates 50 years, and the information it provides us has revolutionized the vision we had about biological processes at the atomic level. The Protein Data Bank is a very large database of structures and is also a source of much important information on various macromolecules, which can be analyzed by a variety of professionals such as: crystallographers, chemists, biologists, biochemists, microbiologists, doctors, pharmacists, among others. Knowing the structure of a macromolecule of interest can help to understand a large number of chemical and biological processes and diseases, since understanding in atomic detail the chemical and structural alteration of a macromolecule allow us to decipher mechanisms that participate in the chemical or biological process or the one that cause disease and damage in the organism; In addition, the design of drugs for its treatment can be carried out.