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Equivalence class NR_20.0_30153.3 Obsolete

#IFEStandardized nameMoleculeOrganismSourceRfamTitleMethodRes. ÅDate
15AXM|1|P (rep)Transfer RNARNA (75-MER)Saccharomyces cerevisiaeEukaryaRF00005Crystal structure of Thg1 like protein (TLP) with tRNA(Phe)X-ray diffraction2.212016-08-03
25AXN|1|PTransfer RNARNA (75-MER)Saccharomyces cerevisiaeEukaryaRF00005Crystal structure of Thg1 like protein (TLP) with tRNA(Phe) and GDPNPX-ray diffraction2.72016-08-03
31OB2|1|BTransfer RNATRANSFER-RNA, PHESaccharomyces cerevisiaeEukaryaRF00005E. coli elongation factor EF-Tu complexed with the antibiotic kirromycin, a GTP analog, and Phe-tRNAX-ray diffraction3.352004-05-27
44TNA|1|ATransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005FURTHER REFINEMENT OF THE STRUCTURE OF YEAST T-RNA-PHEX-ray diffraction2.51978-04-12
51EHZ|1|ATransfer RNATRANSFER RNA (PHE)Saccharomyces cerevisiaeEukaryaRF00005The crystal structure of yeast phenylalanine tRNA at 1.93 A resolutionX-ray diffraction1.932000-10-02
61I9V|1|ATransfer RNAPHENYLALANINE TRANSFER RNASaccharomyces cerevisiaeEukaryaRF00005CRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEXX-ray diffraction2.62001-06-04
71TN1|1|ATransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005CRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE TRNAX-ray diffraction31987-01-15
81TN2|1|ATransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005CRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE T-RNAX-ray diffraction31986-10-24
95M1J|1|A3Transfer RNAyeast Phe-tRNA-Phe, nonstop mRNASaccharomyces cerevisiaeEukaryaRF00005Nonstop ribosomal complex bound with Dom34 and Hbs1Electron microscopy3.32017-01-18
104TRA|1|ATransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005RESTRAINED REFINEMENT OF TWO CRYSTALLINE FORMS OF YEAST ASPARTIC ACID AND PHENYLALANINE TRANSFER RNA CRYSTALSX-ray diffraction31987-11-06
116TNA|1|ATransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005CRYSTAL STRUCTURE OF YEAST PHENYLALANINE T-RNA. I.CRYSTALLOGRAPHIC REFINEMENTX-ray diffraction2.71979-01-16
121TRA|1|ATransfer RNATRNAPHESaccharomyces 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
131LS2|1|BTransfer RNAPhenylalanine transfer RNASaccharomyces cerevisiaeEukaryaRF00005Fitting 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
141FCW|1|ATransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11
151FCW|1|DTransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11
161FCW|1|BTransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11
171FCW|1|ETransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11
181FCW|1|CTransfer RNATRNAPHESaccharomyces cerevisiaeEukaryaRF00005TRNA POSITIONS DURING THE ELONGATION CYCLEElectron microscopy172000-08-11

Release history

Release2.1112.1122.1132.1142.1152.1162.1172.1182.1192.1202.1212.1222.1232.1242.1252.1262.1272.1282.1292.1302.1312.1322.1332.1342.1352.1362.1372.1382.1392.1402.1412.1422.1432.1442.1452.1462.1472.1482.1492.1502.1512.1522.1532.1542.1552.1562.1572.1583.03.13.23.33.43.53.63.73.83.93.103.113.123.133.143.153.163.173.183.193.203.213.223.233.243.253.263.273.283.29
Date2017-01-202017-01-272017-02-032017-02-102017-02-172017-02-242017-03-032017-03-102017-03-172017-03-242017-03-312017-04-112017-04-152017-04-262017-04-292017-05-092017-05-152017-05-202017-05-272017-06-072017-06-112017-06-212017-06-242017-06-282017-07-042017-07-102017-07-152017-07-262017-07-312017-08-052017-08-122017-08-192017-08-262017-09-032017-09-092017-09-162017-09-232017-09-302017-10-072017-10-142017-10-212017-10-282017-11-032017-11-102017-11-172017-11-242017-12-012017-12-082017-12-152017-12-222017-12-292018-01-052018-01-122018-01-192018-01-262018-02-022018-02-092018-02-162018-02-232018-03-012018-03-082018-03-152018-03-222018-03-292018-04-062018-04-132018-04-202018-04-272018-05-042018-05-112018-05-182018-05-252018-06-012018-06-082018-06-152018-06-222018-06-292018-07-06

Parents

This classParent classesRelease idIntersectionAdded to this classOnly in parent
NR_20.0_30153.3NR_20.0_30153.22.111(17) 6TNA|1|A, 5AXN|1|P, 5AXM|1|P, 4TRA|1|A, 4TNA|1|A, 1TRA|1|A, 1TN2|1|A, 1TN1|1|A, 1OB2|1|B, 1LS2|1|B, 1I9V|1|A, 1FCW|1|E, 1FCW|1|D, 1FCW|1|C, 1FCW|1|B, 1FCW|1|A, 1EHZ|1|A(1) 5M1J|1|A3(0)

Children

This class Descendant classesRelease idIntersectionOnly in this classAdded to child
NR_20.0_30153.3NR_20.0_30153.43.30(18) 1FCW|1|E, 1TN2|1|A, 5AXN|1|P, 1FCW|1|D, 1TN1|1|A, 5AXM|1|P, 1FCW|1|C, 1OB2|1|B, 4TRA|1|A, 1FCW|1|B, 1LS2|1|B, 4TNA|1|A, 1FCW|1|A, 6TNA|1|A, 1I9V|1|A, 1TRA|1|A, 1EHZ|1|A, 5M1J|1|A3(0) (3) 6GQ1|1|AX, 6GQB|1|AX, 6GQV|1|AY

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
131TN1|1|ACRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE TRNAX-RAY DIFFRACTION362
141TN2|1|ACRYSTALLOGRAPHIC AND BIOCHEMICAL INVESTIGATION OF THE LEAD(II)-CATALYZED HYDROLYSIS OF YEAST PHENYLALANINE T-RNAX-RAY DIFFRACTION362
155AXM|1|PCrystal structure of Thg1 like protein (TLP) with tRNA(Phe)X-RAY DIFFRACTION2.2172
165AXN|1|PCrystal structure of Thg1 like protein (TLP) with tRNA(Phe) and GDPNPX-RAY DIFFRACTION2.765
175M1J|1|A3Nonstop ribosomal complex bound with Dom34 and Hbs1ELECTRON MICROSCOPY3.362
181LS2|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
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