BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19302

Title: Solution Structure of ERCC4 domain of human FAAP24   PubMed: 23999858

Deposition date: 2013-06-18 Original release date: 2013-09-16

Authors: Wu, Fangming; Han, Xiao; Shi, Chaowei; Gong, Weimin; Tian, Changlin

Citation: Wang, Yucai; Han, Xiao; Wu, Fangming; Leung, Justin; Lowery, Megan; Do, Huong; Chen, Junjie; Shi, Chaowei; Tian, Changlin; Li, Lei; Gong, Weimin. "Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response."  Cell Res. 23, 1215-1228 (2013).

Assembly members:
FAAP24-ERCC4, polymer, 147 residues, 15680.295 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):
FAAP24-ERCC4: MEKNPPDDTGPVHVPLGHIV ANEKWRGSQLAQEMQGKIKL IFEDGLTPDFYLSNRCCILY VTEADLVAGNGYRKRLVRVR NSNNLKGIVVVEKTRMSEQY FPALQKFTVLDLGMVLLPVA SQMEASCLVIQLVQEQTKEL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts131
1H chemical shifts867

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ERCC4 domain of human FAAP241

Entities:

Entity 1, ERCC4 domain of human FAAP24 147 residues - 15680.295 Da.

1   METGLULYSASNPROPROASPASPTHRGLY
2   PROVALHISVALPROLEUGLYHISILEVAL
3   ALAASNGLULYSTRPARGGLYSERGLNLEU
4   ALAGLNGLUMETGLNGLYLYSILELYSLEU
5   ILEPHEGLUASPGLYLEUTHRPROASPPHE
6   TYRLEUSERASNARGCYSCYSILELEUTYR
7   VALTHRGLUALAASPLEUVALALAGLYASN
8   GLYTYRARGLYSARGLEUVALARGVALARG
9   ASNSERASNASNLEULYSGLYILEVALVAL
10   VALGLULYSTHRARGMETSERGLUGLNTYR
11   PHEPROALALEUGLNLYSPHETHRVALLEU
12   ASPLEUGLYMETVALLEULEUPROVALALA
13   SERGLNMETGLUALASERCYSLEUVALILE
14   GLNLEUVALGLNGLUGLNTHRLYSGLULEU
15   GLUHISHISHISHISHISHIS

Samples:

sample_1: FAAP24-ERCC4, [U-100% 13C; U-100% 15N], 0.5 – 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_2: FAAP24-ERCC4, [U-100% 13C; U-100% 15N], 0.5 – 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM; EDTA 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.35 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 700 MHz

Related Database Links:

UNP Q9BTP7
PDB
DBJ BAG54708
GB AAH03535 AAH10170 AAH20247 ADQ32151 AIC52732
REF NP_689479 XP_003780763 XP_003915337 XP_004093270 XP_005259450
SP Q9BTP7

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