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Solution Structure of the RING domain of the human RING-box protein 2
Authors
Miyamoto, K., Tomizawa, T., Koshiba, S., Watanabe, S., Harada, T., Kigawa, T., Yokoyama, S.
Assembly
RING-box protein 2
Entity
1. RING domain (polymer, Thiol state: free and other bound), 81 monomers, 9231.458 Da Detail

GSSGSSGMWS WDVECDTCAI CRVQVMDACL RCQAENKQED CVVVWGECNH SFHNCCMSLW VKQNNRCPLC QQDWVVQRIG K


2. ZN (non-polymer), 65.409 × 3 Da
Total weight
9427.685 Da
Max. entity weight
9231.458 Da
Entity Connection
na 12 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1nasing1:CYS18:SG2:ZN1:ZN
2nasing1:CYS21:SG2:ZN1:ZN
3nasing1:HIS53:ND12:ZN1:ZN
4nasing1:CYS56:SG2:ZN1:ZN
5nasing1:CYS29:SG2:ZN1:ZN
6nasing1:CYS32:SG2:ZN1:ZN
7nasing1:CYS41:SG2:ZN1:ZN
8nasing1:CYS55:SG2:ZN1:ZN
9nasing1:HIS50:ND12:ZN1:ZN
10nasing1:CYS48:SG2:ZN1:ZN
11nasing1:CYS67:SG2:ZN1:ZN
12nasing1:CYS70:SG2:ZN1:ZN

Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 95.1 %, Completeness: 96.1 %, Completeness (bb): 94.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All96.1 % (878 of 914)95.8 % (455 of 475)96.8 % (331 of 342)94.8 % (92 of 97)
Backbone94.6 % (458 of 484)94.0 % (156 of 166)95.4 % (227 of 238)93.8 % (75 of 80)
Sidechain97.4 % (493 of 506)96.8 % (299 of 309)98.3 % (177 of 180)100.0 % (17 of 17)
Aromatic100.0 % (78 of 78)100.0 % (39 of 39)100.0 % (34 of 34)100.0 % (5 of 5)
Methyl100.0 % (64 of 64)100.0 % (32 of 32)100.0 % (32 of 32)

1. RING domain

GSSGSSGMWS WDVECDTCAI CRVQVMDACL RCQAENKQED CVVVWGECNH SFHNCCMSLW VKQNNRCPLC QQDWVVQRIG K

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.001) atm, Temperature 296 (±0.1) K, pH 7.0 (±0.05), Details 1.11mM RING domain {U-13C,15N;} 20mM {d-Tris-HCl(pH7.0);} 100mM {NaCl;} 1mM {d-DTT;} 0.02% {NaN3;} 0.05mM {ZNCl2;} 1.0mM {IDA;} 90% H2O, 10% D2O


#NameIsotope labelingTypeConcentration
1RING domain[U-13C; U-15N]protein1.11 mM
2d-Tris-HClnatural abundancebuffer20 mM
3NaClnatural abundancesalt100 mM
4d-DTTnatural abundancesalt1 mM
5NaN3natural abundancesalt0.02 %
6ZnCl2natural abundancesalt0.05 mM
7IDAnatural abundancesalt1.0 mM
8H2Osolvent90 %
9D2Osolvent10 %

LACS Plot; CA
Referencing offset: -0.27 ppm, Outliers: 4 Detail
LACS Plot; CB
Referencing offset: -0.27 ppm, Outliers: 4 Detail
LACS Plot; HA
Referencing offset: -0.07 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.28 ppm, Outliers: 3 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2ECL, Strand ID: A Detail


Release date
2011-08-18
Citation
Molecular basis of cullin-3 (Cul3) ubiquitin ligase subversion by vaccinia virus protein A55
Miyamoto, K., Tomizawa, T., Koshiba, S., Watanabe, S., Harada, T., Kigawa, T., Yokoyama, S.
J. Biol. Chem. (2019), 294, 6416-6429, PubMed 30819806 , DOI 10.1074/jbc.RA118.006561 ,
Related entities 1. RING domain, : 1 : 8 : 160 entities Detail
Interaction partners 1. RING domain, : 26 interactors Detail
Experiments performed 2 experiments Detail
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