#IFECompound(s)RNA source organismTitleMethodResolutionDate
11I9V|1|A (rep)PHENYLALANINE TRANSFER RNASaccharomyces cerevisiaeCRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEXX-RAY DIFFRACTION2.62001-06-04
21EHZ|1|ATRANSFER RNA (PHE)Saccharomyces cerevisiaeThe crystal structure of yeast phenylalanine tRNA at 1.93 A resolutionX-RAY DIFFRACTION1.932000-10-02
34TRA|1|ATRNAPHESaccharomyces cerevisiaeRESTRAINED REFINEMENT OF TWO CRYSTALLINE FORMS OF YEAST ASPARTIC ACID AND PHENYLALANINE TRANSFER RNA CRYSTALSX-RAY DIFFRACTION31987-11-06
41TRA|1|ATRNAPHESaccharomyces cerevisiaeRESTRAINED 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
56TNA|1|ATRNAPHESaccharomyces cerevisiaeCRYSTAL STRUCTURE OF YEAST PHENYLALANINE T-RNA. I.CRYSTALLOGRAPHIC REFINEMENTX-RAY DIFFRACTION2.71979-01-16
61FCW|1|ATRNAPHESaccharomyces cerevisiaeTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY172000-08-11
71FCW|1|BTRNAPHESaccharomyces cerevisiaeTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY172000-08-11
81FCW|1|CTRNAPHESaccharomyces cerevisiaeTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY172000-08-11
91FCW|1|DTRNAPHESaccharomyces cerevisiaeTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY172000-08-11
101FCW|1|ETRNAPHESaccharomyces cerevisiaeTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY172000-08-11
111OB2|1|BTRANSFER-RNA, PHESaccharomyces cerevisiaeE. coli elongation factor EF-Tu complexed with the antibiotic kirromycin, a GTP analog, and Phe-tRNAX-RAY DIFFRACTION3.352004-05-27
121TN1|1|ATRNAPHESaccharomyces cerevisiaeCRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE TRNAX-RAY DIFFRACTION31987-01-15
134TNA|1|ATRNAPHESaccharomyces cerevisiaeFURTHER REFINEMENT OF THE STRUCTURE OF YEAST T-RNA-PHEX-RAY DIFFRACTION2.51978-04-12
141TN2|1|ATRNAPHESaccharomyces cerevisiaeCRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE T-RNAX-RAY DIFFRACTION31986-10-24
151LS2|1|BPhenylalanine transfer RNASaccharomyces cerevisiaeFitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S RibosomeELECTRON MICROSCOPY16.82002-06-26

Release history

Release2.02.12.22.32.42.52.62.72.82.92.102.112.122.132.142.152.162.172.182.192.202.212.222.232.242.252.262.272.282.292.302.312.322.332.342.352.362.372.382.392.402.412.422.432.442.452.462.472.482.492.502.512.522.532.542.552.562.572.582.592.602.612.622.632.642.652.662.672.682.692.702.712.722.732.742.752.762.772.782.792.802.812.822.832.842.852.86
Date2014-12-052014-12-122014-12-192014-12-262015-01-022015-01-092015-01-162015-01-232015-01-302015-02-062015-02-132015-02-202015-02-272015-03-062015-03-132015-03-202015-03-272015-04-032015-04-102015-04-172015-04-242015-05-012015-05-082015-05-152015-05-222015-05-292015-06-052015-06-122015-06-192015-06-262015-07-032015-07-102015-07-172015-07-242015-07-312015-08-072015-08-142015-08-212015-08-282015-09-042015-09-112015-09-182015-09-252015-10-022015-10-092015-10-162015-10-232015-10-302015-11-062015-11-132015-11-202015-11-272015-12-042015-12-112015-12-182015-12-252016-01-012016-01-082016-01-152016-01-222016-01-292016-02-052016-02-122016-02-192016-02-262016-03-042016-03-112016-03-182016-03-252016-04-012016-04-082016-04-152016-04-222016-04-292016-05-062016-05-132016-05-202016-05-272016-06-032016-06-102016-06-172016-06-242016-07-012016-07-082016-07-152016-07-222016-07-29

Parents

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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
11OB2|1|BE. coli elongation factor EF-Tu complexed with the antibiotic kirromycin, a GTP analog, and Phe-tRNAX-RAY DIFFRACTION3.3563
21I9V|1|ACRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEXX-RAY DIFFRACTION2.674
31FCW|1|DTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY1762
41FCW|1|BTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY1762
51FCW|1|ATRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY1762
61FCW|1|CTRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY1762
71FCW|1|ETRNA POSITIONS DURING THE ELONGATION CYCLEELECTRON MICROSCOPY1762
84TRA|1|ARESTRAINED REFINEMENT OF TWO CRYSTALLINE FORMS OF YEAST ASPARTIC ACID AND PHENYLALANINE TRANSFER RNA CRYSTALSX-RAY DIFFRACTION362
96TNA|1|ACRYSTAL STRUCTURE OF YEAST PHENYLALANINE T-RNA. I.CRYSTALLOGRAPHIC REFINEMENTX-RAY DIFFRACTION2.762
101EHZ|1|AThe crystal structure of yeast phenylalanine tRNA at 1.93 A resolutionX-RAY DIFFRACTION1.9362
111TRA|1|ARESTRAINED REFINEMENT OF THE MONOCLINIC FORM OF YEAST PHENYLALANINE TRANSFER RNA. TEMPERATURE FACTORS AND DYNAMICS, COORDINATED WATERS, AND BASE-PAIR PROPELLER TWIST ANGLESX-RAY DIFFRACTION362
124TNA|1|AFURTHER REFINEMENT OF THE STRUCTURE OF YEAST T-RNA-PHEX-RAY DIFFRACTION2.562
131TN2|1|ACRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE T-RNAX-RAY DIFFRACTION362
141TN1|1|ACRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE TRNAX-RAY DIFFRACTION362
151LS2|1|BFitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S RibosomeELECTRON MICROSCOPY16.876