6FYY

Structure of a partial yeast 48S preinitiation complex with eIF5 N-terminal domain (model C2)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.02 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation 3D Report Full Report


This is version 1.1 of the entry. See complete history

Literature

Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition.

Llacer, J.L.Hussain, T.Saini, A.K.Nanda, J.D.Kaur, S.Gordiyenko, Y.Kumar, R.Hinnebusch, A.G.Lorsch, J.R.Ramakrishnan, V.

(2018) Elife 7: --

  • DOI: 10.7554/eLife.39273
  • Primary Citation of Related Structures:  

  • PubMed Abstract: 
  • In eukaryotic translation initiation, AUG recognition of the mRNA requires accommodation of Met-tRNA <sub>i </sub> in a 'P <sub>IN </sub>' state, which is antagonized by the factor eIF1. eIF5 is a GTPase activating protein (GAP) of eIF2 that addition ...

    In eukaryotic translation initiation, AUG recognition of the mRNA requires accommodation of Met-tRNA i in a 'P IN ' state, which is antagonized by the factor eIF1. eIF5 is a GTPase activating protein (GAP) of eIF2 that additionally promotes stringent AUG selection, but the molecular basis of its dual function was unknown. We present a cryo-electron microscopy (cryo-EM) reconstruction of a yeast 48S pre-initiation complex (PIC), at an overall resolution of 3.0 Å, featuring the N-terminal domain (NTD) of eIF5 bound to the 40S subunit at the location vacated by eIF1. eIF5 interacts with and allows a more accommodated orientation of Met-tRNA i . Substitutions of eIF5 residues involved in the eIF5-NTD/tRNA i interaction influenced initiation at near-cognate UUG codons in vivo, and the closed/open PIC conformation in vitro, consistent with direct stabilization of the codon:anticodon duplex by the wild-type eIF5-NTD. The present structure reveals the basis for a key role of eIF5 in start-codon selection.


    Organizational Affiliation

    School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea.,Japan Science and Technology Agency (JST), Precursory Research for Embryonic Science and Technology (PRESTO), Saitama, Japan.,Japan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST), Kyoto, Japan.,From the Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP and scg34@cam.ac.uk.,Department of Molecular Pharmacology and Cell Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), 13125 Berlin, Germany.,State Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University , Shanghai, China.,Department of Chemistry, University of Florence, 50019 Sesto Fiorentino (FI), Italy. luigi.messori@unifi.it.,Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Alexandria University, Alexandria, 21521, Egypt. Electronic address: ahmed.belal@alexu.edu.eg.,Department of Medical Biophysics, University of Toronto, Toronto, ON M5G 1L7, Canada.,Sanofi-Aventis Pharma Deutschland GmbH, Frankfurt am Main, Germany.,College of Pharmacy, Oregon State University , Corvallis, Oregon 97331, United States.,Department of Chemistry and Chemical Biology, Cornell University , Ithaca, New York 14853, United States.,Department of Integrative Structural Biology, Institute of Genetics and of Molecular and Cellular Biology, Centre National de la Recherche Scientifique, Institut National de la Santé de la Recherche Médicale, Université de Strasbourg, 1 rue Laurent Fries, Illkirch, 67404, France.,Department of Biochemistry and Molecular Biology, Monash University, Clayton, Melbourne, VIC, Australia.,Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States.,Synchrotron Radiation Research Section of Macromolecular Crystallography Laboratory, National Cancer Institute, South Cass Avenue 9700, Argonne, IL 60439, U.S.A. bartosz.sekula@nih.gov.,Department of Chemical Sciences, University of Naples Federico II, 80126 Napoli, Italy. ruffo@unina.it.,National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 201210, China; Shanghai Science Research Center, Chinese Academy of Sciences, Shanghai 201210, China.,Department of Quantitative Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo, Japan.,I2BC, SB2SM, CNRS UMR 9198, CEA Saclay, 91191, Gif-sur-Yvette, France.,Charles River , Chesterford Research Park , Saffron Walden CB10 1XL , U.K.,Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.,Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan. shen@cc.okayama-u.ac.jp.,Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Republic of Korea. Sunglee@chosun.ac.kr.,Department of Immunology, Juntendo University School of Medicine, Tokyo, 113-8421, Japan.,Faculty of Science, Ibaraki University, Mito, Japan.,The ARC Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, Australia.,Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Alexandria University, Alexandria, 21521, Egypt; Department of Analytical & Pharmaceutical Chemistry, Faculty of Pharmacy & Drug Manufacturing, Pharos University in Alexandria, Egypt.,Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.; Department of Anatomy, University of California San Francisco, San Francisco, CA 94143, USA.,CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; University of Chinese Academy of Sciences, Beijing, 100049, China.,School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, 5005, Australia.,School of Physical Sciences & Computing, Division of Chemistry, University of Central Lancashire, Preston PR1 2HE, United Kingdom; School of Chemistry, University of Leeds, Leeds, LS2 9JT, United Kingdom.,Department of Pharmaceutical Sciences, University of Tennessee Health Science Center, Memphis, TN, 38163, United States. wli@uthsc.edu.,Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore, India.,Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.,Louis V. Gerstner Jr. Graduate School of Biomedical Sciences, Memorial Sloan Kettering Cancer Center, New York, United States.,Department of Anatomy, University of California San Francisco, San Francisco, CA 94143, USA.,National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 201210, China; Center for Precision Medicine Multi-Omics Research, Peking University Health Science Center; State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100191, China.,Department of Pharmacology and Toxicology, Faculty of Medicine and Medical Centre, American University of Beirut, Beirut, Lebanon; Department of Pharmacology and Toxicology, Faculty of Pharmacy, Alexandria University, Alexandria, 21521, Egypt. Electronic address: ae88@aub.edu.lb.,Pathology and Laboratory Medicine Service, VA Medical Center at Birmingham, Birmingham, AL, 35294, United States.,Department of Biochemistry & Biotechnology, University of Thessaly, Biopolis, 41500 Larissa, Greece. Electronic address: ddleonidas@bio.uth.gr.,From the Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP and.,Molecular Genetics, Institute of Life Science, Kurume University, Fukuoka, Japan.,Protein Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany; BioSupraMol Core Facility, Freie Universität Berlin, 14195 Berlin, Germany.,Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan. s.iwata@mfour.med.kyoto-u.ac.jp.,Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.,Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.,Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.,Department of Organic Chemistry, University of Debrecen, POB 400, H-4002 Debrecen, Hungary. Electronic address: somsak.laszlo@science.unideb.hu.,Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.,Department of Biochemistry & Biotechnology, University of Thessaly, Biopolis, 41500 Larissa, Greece.,Department of Neurology and Neurological Sciences, Stanford University, Stanford, United States.,Sir Peter MacCallum Department of Oncology, University of Melbourne, Melbourne, VIC, Australia. ilia.voskoboinik@petermac.org.,Synchrotron Radiation Research Section of Macromolecular Crystallography Laboratory, National Cancer Institute, South Cass Avenue 9700, Argonne, IL 60439, U.S.A.,Molecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.,Département de Biochimie, de Microbiologie et de Bio-Informatique, IBIS et PROTEO, Université Laval, Pavillon Charles-Eugène Marchand, Québec, Canada.,Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.,Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, United States.,Biotechnology Research Centre, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.,Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.,Institute of Molecular Biology and Biophysics, ETH Zurich, Swiss Federal Institute of Technology, 8093 Zurich, Switzerland.,Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.; Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA.,Department of Pharmacy, University of Pisa, 56126 Pisa, Italy. tiziano.marzo@unipi.it.,Ion Mobility-Mass Spectrometry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany; Department of Molecular Physics, Fritz Haber Institute of the Max Planck Society, 14195 Berlin, Germany.,BIOSS Centre for Biological Signalling Studies, Schänzlestr. 1, 79104, Freiburg, Germany. einsle@biochemie.uni-freiburg.de.,Protein Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.,School of Molecular Sciences, University of Western Australia, Perth, WA, 6009, Australia.,Department of Dermatology, Comprehensive Cancer Center, Cancer Chemoprevention Program, University of Alabama at Birmingham, Birmingham, AL, 35294, United States.,Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow 226031, India.,National Center for Protein Science Shanghai , Shanghai, China.,Department of Chemical Sciences, University of Naples Federico II, 80126 Napoli, Italy. giarita.ferraro@gmail.com.,Health and Life Sciences, De Montfort University, Gateway House, Leicester, LE1 9BH, United Kingdom.,X-ray Crystallography Facility, National Institute of Immunology, New Delhi 110067, India.,Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, No. 20, Nanxincun, Xiangshan, Beijing, 100093, China. shen@cc.okayama-u.ac.jp.,CHDI Management/CHDI Foundation , 6080 Center Drive , Los Angeles , California 90045 , United States.,Department of Chemistry, University of Basel, BPR 1096, Mattenstrasse 24a, 4058 Basel, Switzerland.,Department of Pharmacology and Toxicology, Faculty of Medicine and Medical Centre, American University of Beirut, Beirut, Lebanon.,Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.,Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju, 61452, Republic of Korea.,Department of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.,Axe Molecular Endocrinology and Nephrology, CHU de Québec Research Center, Department of Molecular Medicine, Laval University, Québec, Canada.,University of Chinese Academy of Sciences, Yuquan Rd, Shijingshan District, Beijing, 100049, China.,RIKEN, SPring-8 Center, Hyogo, Japan. s.iwata@mfour.med.kyoto-u.ac.jp.,Department of Veterans Affairs Medical Center, Memphis, TN, 38104, United States.,Clean Energy Research Center, Korea Institute of Science and Technology (KIST), Seoul 02792, Republic of Korea.,Instituto de Biomedicina de Valencia (IBV-CSIC), Valencia, Spain.,Molecular Biology Institute, University of California, Los Angeles, CA, USA.,Institute for Biochemistry, Albert-Ludwigs-University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany. einsle@biochemie.uni-freiburg.de.,Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow 226031, India ashish_arora@cdri.res.in.,KNU Institute for Microorganisms, Kyungpook National University, Daegu 41566, Republic of Korea.,Department of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, United States.,GlaxoSmithKline, 1250 South Collegeville Road, Collegeville, PA 19426, USA.,RIKEN, SPring-8 Center, Hyogo, Japan.,Institute for Biochemistry, Albert-Ludwigs-University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany.,Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.,Howard Hughes Medical Institute, Stanford University, Stanford, United States.,Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.,Department of Organic Chemistry, University of Debrecen, POB 400, H-4002 Debrecen, Hungary.,Department of Chemistry, University of Washington, 4000 15th Ave NE, Bagley Hall, Seattle, WA, 98195-1700, USA.,Laboratory on the Mechanism and Regulation of Protein Synthesis, Eunice K Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.,Protein Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany. Electronic address: chfreund@zedat.fu-berlin.de.,Department of Chemical Sciences, University of Naples Federico II, 80126 Napoli, Italy. antonello.merlino@unina.it.,MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.,Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Alexandria University, Alexandria, 21521, Egypt.,Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, United States.,Department of Chemical Sciences, University of Naples Federico II, 80126 Napoli, Italy. cuccioli@unina.it.,Cancer Cell Death Laboratory, Peter MacCallum Cancer Centre, Melbourne, VIC, Australia.,Max Planck Institute for Terrestrial Microbiology, D-35043 Marburg, Germany.,College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado, USA.,Department of Photon Science, Stanford University, Stanford, United States.,Astex Pharmaceuticals, 436 Cambridge Science Park, Milton Road, Cambridge CB4 0QA, UK.,Killer Cell Biology Laboratory, Peter MacCallum Cancer Centre, Melbourne, VIC, Australia. ilia.voskoboinik@petermac.org.,National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 201210, China.,Department of Medical Biochemistry, Faculty of Medicine, Alexandria University, Egypt.,Killer Cell Biology Laboratory, Peter MacCallum Cancer Centre, Melbourne, VIC, Australia. amelia.brennan@petermac.org.,Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.,Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, No. 20, Nanxincun, Xiangshan, Beijing, 100093, China.,Department of Crystallography/Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London, UK.,Department of Integrative Structural Biology, Institute of Genetics and of Molecular and Cellular Biology, Centre National de la Recherche Scientifique, Institut National de la Santé de la Recherche Médicale, Université de Strasbourg, 1 rue Laurent Fries, Illkirch, 67404, France. rochel@igbmc.fr.,Department of Environmental Engineering, Chosun University, Gwangju, 61452, Republic of Korea.,National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 201210, China; Shanghai Science Research Center, Chinese Academy of Sciences, Shanghai 201210, China. Electronic address: cong@sibcb.ac.cn.,Microbiology Division, CSIR-Central Drug Research Institute, Lucknow 226031, India.,GlaxoSmithKline, 5 Moore Drive, P.O. Box 13398, Research Triangle Park, NC 27709, USA. Electronic address: david.n.deaton@gsk.com.,Department of Orthopaedic Surgery, University of California, Los Angeles, CA, USA.,Sir Peter MacCallum Department of Oncology, University of Melbourne, Melbourne, VIC, Australia.,Department of Biochemistry, Geisel School of Medicine, Dartmouth College, Hanover, New Hampshire, USA.,Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.,Shoolini University of Biotechnology and Management Sciences, Himachal Pradesh, India.,GlaxoSmithKline, 5 Moore Drive, P.O. Box 13398, Research Triangle Park, NC 27709, USA.,Institute for Photonics and Advanced Sensing, The School of Biological Sciences, The University of Adelaide, North Tce, Adelaide, South Australia, 5005, Australia.,Department of Pharmaceutical Sciences, University of Tennessee Health Science Center, Memphis, TN, 38163, United States.,Department of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel; dan.tawfik@weizmann.ac.il Bar-Even@mpimp-golm.mpg.de.,School of Physical Sciences & Computing, Division of Chemistry, University of Central Lancashire, Preston PR1 2HE, United Kingdom. Electronic address: jhayes@uclan.ac.uk.,Physical and Theoretical Chemistry Laboratory, University of Oxford, OX1 3QZ Oxford, United Kingdom.,Molecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada; john.rubinstein@utoronto.ca.,Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Project Group Translational Medicine & Pharmacology TMP, Theodor-Stern-Kai 7, 60596, Frankfurt, Germany.,the Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge CB2 0XY, United Kingdom.,Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Kafrelsheikh University, Kafr El-Sheikh, 33516, Egypt.,CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China. Electronic address: fengyg@qibebt.ac.cn.,Department of Material Science, Graduate School of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka, 558-8585, Japan.,Ion Mobility-Mass Spectrometry, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.,Charles River , Leiden 2333 CR , Netherlands.,Laboratory of Gene Regulation and Development, Eunice K Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, United States.,GlaxoSmithKline, Gunnels Wood Road, Stevenage, Hertfordshire SG1 2NY, UK.,Killer Cell Biology Laboratory, Peter MacCallum Cancer Centre, Melbourne, VIC, Australia.,Department of Medicine, University of Tennessee Health Science Center, Memphis, TN, 38163, United States.,Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany; dan.tawfik@weizmann.ac.il Bar-Even@mpimp-golm.mpg.de.,Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Project Group Translational Medicine & Pharmacology TMP, Theodor-Stern-Kai 7, 60596, Frankfurt, Germany; Institute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, Theodor-Stern-Kai 7, 60596, Frankfurt, Germany.,Institute of Microbial Technology, Chandigarh, Council of Scientific and Industrial Research, Chandigarh 160 036, India.,Department of Structural Biology, Stanford University, Stanford, United States.,CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.,Institute of Bioinformatics and Applied Biotechnology, Bangalore, India.




Macromolecules

Find similar proteins by: Sequence  |  Structure


Entity ID: 4
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S0
A
254Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS0
Find proteins for Q6CN12 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CN12
Entity ID: 5
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S1
B
255Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS1
Find proteins for Q6CWD0 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CWD0
Entity ID: 6
MoleculeChainsSequence LengthOrganismDetails
KLLA0F09812p
C
259Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CKL3 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CKL3
Entity ID: 7
MoleculeChainsSequence LengthOrganismDetails
KLLA0D08305p
D
237Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CRK7 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CRK7
Entity ID: 8
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S4
E
261Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CWJ2 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CWJ2
Entity ID: 9
MoleculeChainsSequence LengthOrganismDetails
KLLA0D10659p
F
227Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CRA3 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CRA3
Entity ID: 10
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S6
G
236Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS6
Find proteins for Q6CM04 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to Gene View: RPS6
Go to UniProtKB:  Q6CM04
Entity ID: 11
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S7
H
190Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CTD6 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CTD6
Entity ID: 12
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S8
I
201Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CMG3 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CMG3
Entity ID: 13
MoleculeChainsSequence LengthOrganismDetails
KLLA0E23673p
J
188Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CM18 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CM18
Entity ID: 14
MoleculeChainsSequence LengthOrganismDetails
KLLA0B08173p
K
106Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CVZ5 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CVZ5
Entity ID: 15
MoleculeChainsSequence LengthOrganismDetails
KLLA0A10483p
L
156Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CX80 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CX80
Entity ID: 16
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S12
M
134Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CLU4 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CLU4
Entity ID: 17
MoleculeChainsSequence LengthOrganismDetails
KLLA0F18040p
N
151Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CJK0 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CJK0
Entity ID: 18
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S14
O
137Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS14 (CRY1)
Find proteins for P27069 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to Gene View: RPS14
Go to UniProtKB:  P27069
Entity ID: 19
MoleculeChainsSequence LengthOrganismDetails
KLLA0F07843p
P
142Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CKV4 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CKV4
Entity ID: 20
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S16
Q
143Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS16
Find proteins for Q875N2 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to Gene View: RPS16
Go to UniProtKB:  Q875N2
Entity ID: 21
MoleculeChainsSequence LengthOrganismDetails
KLLA0B01474p
R
136Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CWU3 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CWU3
Entity ID: 22
MoleculeChainsSequence LengthOrganismDetails
KLLA0B01562p
S
146Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CWT9 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CWT9
Entity ID: 23
MoleculeChainsSequence LengthOrganismDetails
KLLA0A07194p
T
144Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CXM0 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CXM0
Entity ID: 24
MoleculeChainsSequence LengthOrganismDetails
KLLA0F25542p
U
117Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CIM1 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CIM1
Entity ID: 25
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S21
V
87Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS21
Find proteins for Q6CXT6 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to Gene View: RPS21
Go to UniProtKB:  Q6CXT6
Entity ID: 26
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S22
W
130Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS22
Find proteins for Q6CW21 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CW21
Entity ID: 27
MoleculeChainsSequence LengthOrganismDetails
KLLA0B11231p
X
145Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for F2Z602 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  F2Z602
Entity ID: 28
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S24
Y
135Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CU44 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CU44
Entity ID: 29
MoleculeChainsSequence LengthOrganismDetails
KLLA0B06182p
Z
108Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CW78 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CW78
Entity ID: 30
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S26
a
119Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CS01 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CS01
Entity ID: 31
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S27
b
82Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CNL2 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CNL2
Entity ID: 32
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S28
c
67Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS28
Find proteins for P33285 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to Gene View: RPS28
Go to UniProtKB:  P33285
Entity ID: 33
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S29
d
56Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: RPS29
Find proteins for Q6CPG3 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to Gene View: RPS29
Go to UniProtKB:  Q6CPG3
Entity ID: 34
MoleculeChainsSequence LengthOrganismDetails
40S ribosomal protein S30
e
63Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CUH5 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CUH5
Entity ID: 35
MoleculeChainsSequence LengthOrganismDetails
Ubiquitin-40S ribosomal protein S27a
f
150Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Gene Names: ubi3
Find proteins for P69061 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  P69061
Entity ID: 36
MoleculeChainsSequence LengthOrganismDetails
KLLA0E12277p
g
326Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)Mutation(s): 0 
Find proteins for Q6CNI7 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37))
Go to UniProtKB:  Q6CNI7
Entity ID: 37
MoleculeChainsSequence LengthOrganismDetails
60S ribosomal protein L41-A
h
25Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: RPL41A (RPL47A, YL41A)
Find proteins for P0CX86 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P0CX86
Entity ID: 38
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 1A
i
153Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: TIF11
Find proteins for P38912 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P38912
Entity ID: 39
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 2 subunit alpha
j
304Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: SUI2 (TIF211)
Find proteins for P20459 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P20459
Entity ID: 40
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 2 subunit gamma
k
527Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: GCD11 (TIF213)
Find proteins for P32481 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P32481
Entity ID: 41
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 2 subunit beta
l
285Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: SUI3 (TIF212)
Find proteins for P09064 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P09064
Entity ID: 42
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 5
m
405Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: TIF5
Find proteins for P38431 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P38431
Entity ID: 43
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 3 subunit A
o
964Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: RPG1 (TIF32)
Find proteins for P38249 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P38249
Entity ID: 44
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 3 subunit B
p
763Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: PRT1 (CDC63)
Find proteins for P06103 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P06103
Entity ID: 45
MoleculeChainsSequence LengthOrganismDetails
eIF3c,Eukaryotic translation initiation factor 3 subunit C
q
812Saccharomyces cerevisiae (strain ATCC 204508 / S288c)Mutation(s): 0 
Gene Names: NIP1
Find proteins for P32497 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Go to UniProtKB:  P32497
Entity ID: 46
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 3 subunit G
r
274Saccharomyces cerevisiae (strain YJM789)Mutation(s): 0 
Gene Names: TIF35
Find proteins for A6ZZ25 (Saccharomyces cerevisiae (strain YJM789))
Go to UniProtKB:  A6ZZ25
Entity ID: 47
MoleculeChainsSequence LengthOrganismDetails
Eukaryotic translation initiation factor 3 subunit I
s
347Saccharomyces cerevisiae (strain YJM789)Mutation(s): 0 
Gene Names: TIF34
Find proteins for A6ZMK5 (Saccharomyces cerevisiae (strain YJM789))
Go to UniProtKB:  A6ZMK5
Entity ID: 1
MoleculeChainsLengthOrganism
tRNAi176Saccharomyces cerevisiae
Entity ID: 2
MoleculeChainsLengthOrganism
18S ribosomal RNA21798Kluyveromyces lactis NRRL Y-1140
Entity ID: 3
MoleculeChainsLengthOrganism
mRNA (31-MER)349Saccharomyces cerevisiae
Small Molecules
Ligands 4 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download SDF File 
Download CCD File 
a, b, f, l, m
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
 Ligand Interaction
MG
Query on MG

Download SDF File 
Download CCD File 
2, k
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
 Ligand Interaction
GCP
Query on GCP

Download SDF File 
Download CCD File 
k
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
C11 H18 N5 O13 P3
PHBDHXOBFUBCJD-KQYNXXCUSA-N
 Ligand Interaction
MET
Query on MET

Download SDF File 
Download CCD File 
k
METHIONINE
C5 H11 N O2 S
FFEARJCKVFRZRR-BYPYZUCNSA-N
 Ligand Interaction
Modified Residues  14 Unique
IDChainsTypeFormula2D DiagramParent
PSU
Query on PSU
2
RNA LINKINGC9 H13 N2 O9 PU
5MC
Query on 5MC
1, 2
RNA LINKINGC10 H16 N3 O8 PC
RIA
Query on RIA
1
RNA LINKINGC15 H23 N5 O14 P2A
1MG
Query on 1MG
1
RNA LINKINGC11 H16 N5 O8 PG
M2G
Query on M2G
1
RNA LINKINGC12 H18 N5 O8 PG
1MA
Query on 1MA
1
RNA LINKINGC11 H16 N5 O7 PA
AYA
Query on AYA
B
L-PEPTIDE LINKINGC5 H9 N O3ALA
C4J
Query on C4J
2
RNA linkingC14 H22 N3 O11 P

--

MA6
Query on MA6
2
RNA LINKINGC12 H18 N5 O7 PA
UNK
Query on UNK
1, q
L-PEPTIDE LINKINGC4 H9 N O2

--

T6A
Query on T6A
1
RNA LINKINGC15 H21 N6 O11 PA
2MG
Query on 2MG
1, 2
RNA LINKINGC11 H16 N5 O8 PG
7MG
Query on 7MG
1, 2
RNA LINKINGC11 H18 N5 O8 PG
H2U
Query on H2U
1
RNA LINKINGC9 H15 N2 O9 PU
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.02 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (United Kingdom)United KingdomMC_U105184332
Wellcome TrustUnited KingdomWT096570
FEBSUnited Kingdom--

Revision History 

  • Version 1.0: 2018-12-05
    Type: Initial release
  • Version 1.1: 2019-01-23
    Type: Advisory, Data collection, Derived calculations