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Protein complex
Authors
Chen, X., Walters, K.J.
Assembly
human Rpn13 Pru domain
Entity
1. human Rpn13 Pru domain, entity 1 (polymer, Thiol state: all free), 150 monomers, 16718.84 Da Detail

MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH CRKVNEYLNN PPMPGALGAS GSSGHELSAL


2. human Rpn13 Pru domain, entity 2 (polymer, Thiol state: all free), 78 monomers, 8749.065 Da Detail

APAEPKIIKV TVKTPKEKEE FAVPENSSVQ QFKEAISKRF KSQTDQLVLI FAGKILKDQD TLIQHGIHDG LTVHLVIK


Total weight
25467.906 Da
Max. entity weight
16718.84 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 65.8 %, Completeness: 56.5 %, Completeness (bb): 64.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All56.5 % (1524 of 2699)55.8 % (789 of 1414)55.6 % (585 of 1052)64.4 % (150 of 233)
Backbone64.9 % (869 of 1340)64.4 % (295 of 458)65.1 % (435 of 668)65.0 % (139 of 214)
Sidechain50.4 % (792 of 1571)51.7 % (494 of 956)48.2 % (287 of 596)57.9 % (11 of 19)
Aromatic 4.5 % (9 of 200) 7.0 % (7 of 100) 0.0 % (0 of 98)100.0 % (2 of 2)
Methyl54.6 % (130 of 238)54.6 % (65 of 119)54.6 % (65 of 119)

1. entity 1

MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH CRKVNEYLNN PPMPGALGAS GSSGHELSAL

2. entity 2

APAEPKIIKV TVKTPKEKEE FAVPENSSVQ QFKEAISKRF KSQTDQLVLI FAGKILKDQD TLIQHGIHDG LTVHLVIK

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1entity_1[U-100% 13C; U-100% 15N; U-70% 2H]protein0.7 mM
2entity_2natural abundanceprotein0.7 mM
3sodium phosphatenatural abundancebuffer20 mM
4sodium chloridenatural abundancesalt50 mM
5DTTnatural abundance2 mM
6sodium azidenatural abundance0.1 %
7H2Onatural abundancesolvent95 %
8D2O[U-2H]solvent5 %
Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
9entity_1[U-100% 15N]protein0.7 mM
10entity_2natural abundanceprotein0.7 mM
11sodium phosphatenatural abundancebuffer20 mM
12sodium chloridenatural abundancesalt50 mM
13DTTnatural abundance2 mM
14sodium azidenatural abundance0.1 %
15H2Onatural abundancesolvent95 %
16D2O[U-2H]solvent5 %
Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
17entity_1[U-100% 13C]protein0.7 mM
18entity_2natural abundanceprotein0.7 mM
19sodium phosphatenatural abundancebuffer20 mM
20sodium chloridenatural abundancesalt50 mM
21DTTnatural abundance2 mM
22sodium azidenatural abundance0.1 %
23D2O[U-2H]solvent100 %

LACS Plot; CA
Referencing offset: 0.31 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: 0.31 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: -0.06 ppm, Outliers: 4 Detail
LACS Plot; CO
Referencing offset: 3.1 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2NBV, Strand ID: A, B Detail


Release date
2016-07-17
Citation
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome
Chen, X., Randles, L., Shi, K., Tarasov, S.G., Aihara, H., Walters, K.J.
Structure (2016), 24, 1257-1270, PubMed 27396824 , DOI 10.1016/j.str.2016.05.018 ,
Related entities 1. human Rpn13 Pru domain, entity 1, : 1 : 7 : 2 : 18 entities Detail
Related entities 2. human Rpn13 Pru domain, entity 2, : 1 : 3 : 84 entities Detail
Interaction partners 2. human Rpn13 Pru domain, entity 2, : 20 interactors Detail
Experiments performed 11 experiments Detail
NMR combined restraints 5 contents Detail
Keywords protein