#IFECompound(s)RNA source organismTitleMethodResolutionDate
13J0E|1|A (rep)ribosomal 23S RNAEscherichia coliModels for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complexELECTRON MICROSCOPY9.92012-04-25
23J0D|1|Bribosomal 23S RNAEscherichia coliModels for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complexELECTRON MICROSCOPY11.12012-04-25
31QZC|1|B23S rRNAEscherichia coliCoordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosomeELECTRON MICROSCOPY92003-11-04
41MVR|1|CHelix 69 of 23S rRNAEscherichia coliDecoding Center & Peptidyl transferase center from the X-ray structure of the Thermus thermophilus 70S ribosome, aligned to the low resolution Cryo-EM map of E.coli 70S RibosomeELECTRON MICROSCOPY12.82003-04-01

Release history

Release2.1202.1212.1222.1232.1242.1252.1262.1272.1282.1292.1302.1312.1322.1332.1342.1352.1362.1372.1382.1392.1402.1412.1422.1432.1442.1452.1462.1472.1482.1492.1502.1512.1522.1532.1542.1552.1562.1572.1583.03.13.23.33.43.53.63.73.83.93.103.113.123.133.143.153.163.173.183.193.203.213.223.233.243.253.263.273.283.293.303.313.323.333.343.353.363.373.383.393.403.413.423.433.443.453.463.473.483.493.503.513.523.533.543.553.563.573.583.593.603.613.623.633.643.653.663.673.683.693.703.713.723.733.743.753.763.773.783.793.803.813.823.833.843.853.863.873.883.893.903.913.923.933.943.953.96
Date2017-03-242017-03-312017-04-112017-04-152017-04-262017-04-292017-05-092017-05-152017-05-202017-05-272017-06-072017-06-112017-06-212017-06-242017-06-282017-07-042017-07-102017-07-152017-07-262017-07-312017-08-052017-08-122017-08-192017-08-262017-09-032017-09-092017-09-162017-09-232017-09-302017-10-072017-10-142017-10-212017-10-282017-11-032017-11-102017-11-172017-11-242017-12-012017-12-082017-12-152017-12-222017-12-292018-01-052018-01-122018-01-192018-01-262018-02-022018-02-092018-02-162018-02-232018-03-012018-03-082018-03-152018-03-222018-03-292018-04-062018-04-132018-04-202018-04-272018-05-042018-05-112018-05-182018-05-252018-06-012018-06-082018-06-152018-06-222018-06-292018-07-062018-07-132018-07-202018-07-272018-08-032018-08-102018-08-172018-08-242018-08-312018-09-072018-09-142018-09-212018-09-282018-10-052018-10-122018-10-192018-10-262018-11-022018-11-092018-11-162018-11-232018-11-302018-12-072018-12-142018-12-212018-12-282019-01-042019-01-112019-01-182019-01-252019-02-012019-02-082019-02-152019-02-222019-03-012019-03-082019-03-152019-03-222019-03-292019-04-052019-04-122019-04-192019-04-262019-05-032019-05-102019-05-172019-05-242019-05-312019-06-072019-06-142019-06-212019-06-282019-07-052019-07-122019-07-192019-07-262019-08-022019-08-092019-08-162019-08-232019-08-282019-09-042019-09-112019-09-192019-09-252019-10-032019-10-092019-10-16

Parents

This classParent classesRelease idIntersectionAdded to this classOnly in parent
NR_20.0_18337.2NR_20.0_18337.12.120(4) 1MVR|1|C, 3J0D|1|B, 1QZC|1|B, 3J0E|1|A(0) (1) 1T1O|1|B

Children

This class Descendant classesRelease idIntersectionOnly in this classAdded to child

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
11QZC|1|BCoordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosomeELECTRON MICROSCOPY920
21MVR|1|CDecoding Center & Peptidyl transferase center from the X-ray structure of the Thermus thermophilus 70S ribosome, aligned to the low resolution Cryo-EM map of E.coli 70S RibosomeELECTRON MICROSCOPY12.819
33J0E|1|AModels for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complexELECTRON MICROSCOPY9.922
43J0D|1|BModels for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complexELECTRON MICROSCOPY11.122