Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer
MRGSHHHHHH GIRMPGCLPA YDALAGQFIE ASSREARQAI LKQGQDGLSG VKETDKKWAS QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL QRSLNILTAF RKKGAEKEEL
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 77.7 % (1100 of 1416) | 94.9 % (712 of 750) | 49.5 % (267 of 539) | 95.3 % (121 of 127) |
Backbone | 83.8 % (598 of 714) | 95.2 % (236 of 248) | 71.9 % (251 of 349) | 94.9 % (111 of 117) |
Sidechain | 64.9 % (526 of 811) | 94.8 % (476 of 502) | 13.4 % (40 of 299) | 100.0 % (10 of 10) |
Aromatic | 37.8 % (31 of 82) | 73.2 % (30 of 41) | 0.0 % (0 of 40) | 100.0 % (1 of 1) |
Methyl | 56.4 % (62 of 110) | 98.2 % (54 of 55) | 14.5 % (8 of 55) |
1. Endoplasmic reticulum protein p29
MRGSHHHHHH GIRMPGCLPA YDALAGQFIE ASSREARQAI LKQGQDGLSG VKETDKKWAS QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL QRSLNILTAF RKKGAEKEELTemperature 308 (±1) K, pH 4.9 (±0.1)
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Endoplasmic reticulum protein p29 | [U-15N; U-13C] | 2 mM |