BMRB Entry 18431

Title:
Solution structure of the mouse Rev1 C-terminal domain
Deposition date:
2012-04-30
Original release date:
2012-06-18
Authors:
Liu, Jiangxin; Wojtaszek, Jessica; Zhou, Pei
Citation:

Citation: Wojtaszek, Jessica; Liu, Jiangxin; Wang, Sanjay; Xue, Su; Walker, Yaohua; Zhou, Graham. "Multifaceted recognition of vertebrate Rev1 by translesion polymerases and ."  J. Biol. Chem. 287, 26400-26408 (2012).
PubMed: 22700975

Assembly members:

Assembly members:
entity, polymer, 104 residues, 11166.953 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMAL-C2

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts100
1H chemical shifts764

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1mouse Rev1 C-terminal domain1

Entities:

Entity 1, mouse Rev1 C-terminal domain 104 residues - 11166.953 Da.

1   GLYSERGLYGLYPHEARGPROALAALAPRO
2   ASNLEUALAGLYALAVALGLUPHESERASP
3   VALLYSTHRLEULEULYSGLUTRPILETHR
4   THRILESERASPPROMETGLUGLUASPILE
5   LEUGLNVALVALARGTYRCYSTHRASPLEU
6   ILEGLUGLULYSASPLEUGLULYSLEUASP
7   LEUVALILELYSTYRMETLYSARGLEUMET
8   GLNGLNSERVALGLUSERVALTRPASNMET
9   ALAPHEASPPHEILELEUASPASNVALGLN
10   VALVALLEUGLNGLNTHRTYRGLYSERTHR
11   LEULYSVALTHR

Samples:

sample_1: Rev1, [U-100% 15N], 0.9 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; PMSF 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: Rev1, [U-100% 13C; U-100% 15N], 0.9 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; PMSF 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_3: Rev1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; PMSF 1 mM; EDTA 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.113 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D (HCA)CO(CA)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)CBsample_2isotropicsample_conditions_1
3D HNCO(CA)CBsample_2isotropicsample_conditions_1
3D HA(CA)NHsample_2isotropicsample_conditions_1
3D HA(CACO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
4D HCCONH TOCSYsample_2isotropicsample_conditions_1
4D HCCH-TOCSYsample_3isotropicsample_conditions_1
4D 13C-HMQC-NOESY-HSQCsample_3isotropicsample_conditions_1
4D 13C-HMQC-NOESY-15N-HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

XEASY, Bartels et al. - peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 18433
PDB
DBJ BAB64933
GB AAF23323 AAH58093 EDL14541 EGW11994 EHB10584
REF NP_062516 XP_001490149 XP_002709984 XP_003503378 XP_004669836
SP Q920Q2
AlphaFold Q920Q2

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks