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Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer
Authors
Liepinsh, E., Baryshev, M., Sharipo, A., Ingelman-Sundberg, M., Otting, G., Mkrtchian, S.
Assembly
ERp29 C-domain
Entity
1. ERp29 C-domain (polymer, Thiol state: all free), 120 monomers, 13481.26 Da Detail

MRGSHHHHHH GIRMPGCLPA YDALAGQFIE ASSREARQAI LKQGQDGLSG VKETDKKWAS QYLKIMGKIL DQGEDFPASE LARISKLIEN KMSEGKKEEL QRSLNILTAF RKKGAEKEEL


Formula weight
13481.26 Da
Source organism
Rattus norvegicus
Exptl. method
NMR
Refine. method
PCS-Rosetta simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.7 %, Completeness: 77.7 %, Completeness (bb): 83.8 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All77.7 % (1100 of 1416)94.9 % (712 of 750)49.5 % (267 of 539)95.3 % (121 of 127)
Backbone83.8 % (598 of 714)95.2 % (236 of 248)71.9 % (251 of 349)94.9 % (111 of 117)
Sidechain64.9 % (526 of 811)94.8 % (476 of 502)13.4 % (40 of 299)100.0 % (10 of 10)
Aromatic37.8 % (31 of 82)73.2 % (30 of 41) 0.0 % (0 of 40)100.0 % (1 of 1)
Methyl56.4 % (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 RKKGAEKEEL

Sample

Temperature 308 (±1) K, pH 4.9 (±0.1)


#NameIsotope labelingTypeConcentration
1Endoplasmic reticulum protein p29[U-15N; U-13C]2 mM

Protein Blocks Logo
Calculated from 11 models in PDB: 2M66, Strand ID: A Detail


Release date
2001-08-07
Citation
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer
Liepinsh, E., Baryshev, M., Sharipo, A., Ingelman-Sundberg, M., Otting, G., Mkrtchian, S.
Structure (2001), 9, 457-471, PubMed 11435111 , DOI: ,
Related entities 1. ERp29 C-domain, : 1 : 4 : 19 entities Detail
Interaction partners 1. ERp29 C-domain, : 5 interactors Detail
Experiments performed 8 experiments Detail
nullKeywords Nuclear magnetic resonance spectroscopy, protein structure