BMRB Entry 19303

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19303
MolProbity Validation Chart

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Title:
Solution Structure of (HhH)2 domain of human FAAP24
Deposition date:
2013-06-18
Original release date:
2013-09-16
Authors:
Wu, Fangming; Han, Xiao; Shi, Chaowei; Gong, Weimin; Tian, Changlin
Citation:

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).
PubMed: 23999858

Assembly members:

Assembly members:
FAAP24_HhH2, polymer, 63 residues, 6628.704 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FAAP24_HhH2: GSSEPSLLRTVQQIPGVGKV KAPLLLQKFPSIQQLSNASI GELEQVVGQAVAQQIHAFFT QPR

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts56
1H chemical shifts415

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1(HhH)2 domain of human FAAP241

Entities:

Entity 1, (HhH)2 domain of human FAAP24 63 residues - 6628.704 Da.

1   GLYSERSERGLUPROSERLEULEUARGTHR
2   VALGLNGLNILEPROGLYVALGLYLYSVAL
3   LYSALAPROLEULEULEUGLNLYSPHEPRO
4   SERILEGLNGLNLEUSERASNALASERILE
5   GLYGLULEUGLUGLNVALVALGLYGLNALA
6   VALALAGLNGLNILEHISALAPHEPHETHR
7   GLNPROARG

Samples:

sample_1: FAAP24_HhH2, [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_HhH2, [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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

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

NMR spectrometers:

  • Bruker DMX 850 MHz
  • Varian INOVA 700 MHz

Related Database Links:

BMRB 18725
PDB
DBJ BAG54708
GB AAH03535 AAH10170 AAH20247 ADQ32151 AIC52732
REF NP_001287907 NP_689479 XP_003780763 XP_003816251 XP_004060528
SP Q9BTP7
AlphaFold Q9BTP7

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