#IFEStandardized nameMoleculeOrganismSourceRfamTitleMethodRes. ÅDate
11EHZ|A (rep)Transfer RNASaccharomyces cerevisiaeEukaryaRF00005The crystal structure of yeast phenylalanine tRNA at 1.93 A resolutionX-ray diffraction1.932000-10-02
21EVV|ATransfer RNASaccharomycesEukaryaRF00005CRYSTAL STRUCTURE OF YEAST PHENYLALANINE TRANSFER RNA AT 2.0 A RESOLUTIONX-ray diffraction22000-05-01
31FCW|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11
41I9V|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEXX-ray diffraction2.62001-06-04
51MJ1|CTransfer RNAEscherichia coliBacteriaRF00005FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GTP AND RIBOSOMAL PROTEINS INTO A 13 A CRYO-EM MAP OF THE COLI 70S RIBOSOMEElectron microscopy132002-11-01
61ML5|aLarge subunit ribosomal RNAEscherichia coliBacteriaRF02541Structure of the E. coli ribosomal termination complex with release factor 2Electron microscopy142003-01-14
71OB2|BTransfer RNASaccharomyces cerevisiaeEukaryaRF00005E. coli elongation factor EF-Tu complexed with the antibiotic kirromycin, a GTP analog, and Phe-tRNAX-ray diffraction3.352004-05-27
81OB5|BTransfer RNASaccharomyces cerevisiaeEukaryaRF00005T. aquaticus elongation factor EF-Tu complexed with the antibiotic enacyloxin IIa, a GTP analog, and Phe-tRNAX-ray diffraction3.12005-10-13
91SZ1|EMechanism of CCA-adding enzymes specificity revealed by crystal structures of ternary complexesX-ray diffraction6.212004-08-10
101TN1|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE TRNAX-ray diffraction31987-01-15
111TN2|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE T-RNAX-ray diffraction31986-10-24
121TRA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005RESTRAINED REFINEMENT OF THE MONOCLINIC FORM OF YEAST PHENYLALANINE TRANSFER RNA. TEMPERATURE FACTORS AND DYNAMICS, COORDINATED WATERS, AND BASE-PAIR PROPELLER TWIST ANGLESX-ray diffraction31986-07-14
131TTT|DPhe-tRNA, elongation factoR EF-TU:GDPNP ternary complexX-ray diffraction2.71996-12-23
141ZO1|FTransfer RNAEscherichia coliBacteriaRF00005IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complexElectron microscopy13.82005-06-14
151ZO3|ATransfer RNAEscherichia coliBacteriaRF00005The P-site and P/E-site tRNA structures fitted to P/I site codon.Electron microscopy13.82005-06-14
163IZY|NTransfer RNABos taurusMitochondriaRF00005Mammalian mitochondrial translation initiation factor 2Electron microscopy10.82011-03-23
173WC2|PCrystal structure of C. albicans tRNA(His) guanylyltransferase (Thg1) with a tRNA(Phe)(GUG)X-ray diffraction3.642013-12-18
184TNA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005FURTHER REFINEMENT OF THE STRUCTURE OF YEAST T-RNA-PHEX-ray diffraction2.51978-04-12
194TRA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005RESTRAINED REFINEMENT OF TWO CRYSTALLINE FORMS OF YEAST ASPARTIC ACID AND PHENYLALANINE TRANSFER RNA CRYSTALSX-ray diffraction31987-11-06
206TNA|ATransfer RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTAL STRUCTURE OF YEAST PHENYLALANINE T-RNA. I.CRYSTALLOGRAPHIC REFINEMENTX-ray diffraction2.71979-01-16

Release history

Release1.411.421.431.441.451.461.471.481.491.501.511.521.531.541.551.561.571.581.591.601.611.621.631.641.651.661.671.681.691.701.711.721.731.741.751.761.771.781.791.801.811.821.831.841.851.861.871.881.89
Date2013-12-212013-12-282014-01-042014-01-112014-01-182014-01-252014-02-012014-02-082014-02-152014-02-222014-03-012014-03-082014-03-172014-03-222014-03-292014-04-052014-04-122014-04-192014-04-262014-05-032014-05-102014-05-172014-05-312014-06-072014-06-132014-06-202014-06-272014-07-042014-07-182014-07-252014-08-012014-08-082014-08-152014-08-222014-08-292014-09-052014-09-122014-09-192014-09-262014-10-032014-10-102014-10-172014-10-242014-10-312014-11-072014-11-142014-11-212014-11-282014-12-05

Parents

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Children

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Heat map of mutual geometric discrepancy, in Angstroms per nucleotide. Instances are ordered to put similar structures near each other. The colorbar ranges from 0 to the maximum observed discrepancy, up to 0.5

#S - ordering by similarity (same as in the heat map).
#SPDBTitleMethodResolutionLength
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