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 GSLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYSGAVKVGA IQRWLKGQGV YLGMPGC
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 73.8 % (1199 of 1624) | 91.7 % (775 of 845) | 45.9 % (294 of 641) | 94.2 % (130 of 138) |
Backbone | 81.2 % (656 of 808) | 94.6 % (265 of 280) | 67.6 % (269 of 398) | 93.8 % (122 of 130) |
Sidechain | 59.7 % (561 of 940) | 90.3 % (510 of 565) | 11.7 % (43 of 367) | 100.0 % (8 of 8) |
Aromatic | 44.5 % (81 of 182) | 83.5 % (76 of 91) | 4.4 % (4 of 90) | 100.0 % (1 of 1) |
Methyl | 55.5 % (71 of 128) | 100.0 % (64 of 64) | 10.9 % (7 of 64) |
1. Endoplasmic reticulum protein p29
MRGSHHHHHH GSLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYSGAVKVGA IQRWLKGQGV YLGMPGCTemperature 308 (±1) K, pH 4.9 (±0.1)
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Endoplasmic reticulum protein p29 | [U-15N; U-13C] | 0.3 mM |