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Biological Magnetic Resonance Data Bank


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BMRB Entry 18432

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18432
MolProbity Validation Chart

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Title: Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa   PubMed: 23220741

Deposition date: 2012-05-01 Original release date: 2013-04-02

Authors: Liu, Dinan; Ryu, Kyoung-Seok; Ko, Junsang; Choi, Byong-Seok

Citation: Liu, Dinan; Ryu, Kyoung-Seok; Ko, Junsang; Sun, Dawei; Lim, Kyungeun; Lee, Jie-Oh; Hwang, Jung Me; Lee, Zee-Won; Choi, Byong-Seok. "Insights into the regulation of human Rev1 for translesion synthesis polymerases revealed by the structural studies on its polymerase-interacting domain."  J. Mol. Cell Biol. 5, 204-206 (2013).

Assembly members:
Rev1, polymer, 232 residues, 27163.572 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Rev1: GHMAPNLAGAVEFNDVKTLL REWITTISDPMEEDILQVVK YCTDLIEEKDLEKLDLVIKY MKRLMQQSVESVWNMAFDFI LDNVQVVLQQTYGSTLKVTG SHKKSFFDKKRSERKWGHMA PNLAGAVEFNDVKTLLREWI TTISDPMEEDILQVVKYCTD LIEEKDLEKLDLVIKYMKRL MQQSVESVWNMAFDFILDNV QVVLQQTYGSTLKVTGSHKK SFFDKKRSERKW

Data sets:
Data typeCount
13C chemical shifts520
15N chemical shifts119
1H chemical shifts839

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Rev11

Entities:

Entity 1, Rev1 232 residues - 27163.572 Da.

1   GLYHISMETALAPROASNLEUALAGLYALA
2   VALGLUPHEASNASPVALLYSTHRLEULEU
3   ARGGLUTRPILETHRTHRILESERASPPRO
4   METGLUGLUASPILELEUGLNVALVALLYS
5   TYRCYSTHRASPLEUILEGLUGLULYSASP
6   LEUGLULYSLEUASPLEUVALILELYSTYR
7   METLYSARGLEUMETGLNGLNSERVALGLU
8   SERVALTRPASNMETALAPHEASPPHEILE
9   LEUASPASNVALGLNVALVALLEUGLNGLN
10   THRTYRGLYSERTHRLEULYSVALTHRGLY
11   SERHISLYSLYSSERPHEPHEASPLYSLYS
12   ARGSERGLUARGLYSTRPGLYHISMETALA
13   PROASNLEUALAGLYALAVALGLUPHEASN
14   ASPVALLYSTHRLEULEUARGGLUTRPILE
15   THRTHRILESERASPPROMETGLUGLUASP
16   ILELEUGLNVALVALLYSTYRCYSTHRASP
17   LEUILEGLUGLULYSASPLEUGLULYSLEU
18   ASPLEUVALILELYSTYRMETLYSARGLEU
19   METGLNGLNSERVALGLUSERVALTRPASN
20   METALAPHEASPPHEILELEUASPASNVAL
21   GLNVALVALLEUGLNGLNTHRTYRGLYSER
22   THRLEULYSVALTHRGLYSERHISLYSLYS
23   SERPHEPHEASPLYSLYSARGSERGLUARG
24   LYSTRP

Samples:

sample_1: Rev1, [U-99% 13C; U-99% 15N], 0.8 mM; Bis-Tris 50 mM; NaCl 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts