BMRB Entry 15240

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15240
MolProbity Validation Chart

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Title:
Solution structure of the ERCC1 central domain
Deposition date:
2007-05-07
Original release date:
2007-08-28
Authors:
Tripsianes, Konstantinos; Folkers, Gert; Zheng, Chao; Das, Devashish; Grinstead, Jeffrey; Kaptein, Robert; Boelens, Rolf
Citation:

Citation: Tripsianes, Konstantinos; Folkers, Gert; Zheng, Chao; Das, Devashish; Grinstead, Jeffrey; Kaptein, Robert; Boelens, Rolf. "Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization"  Nucleic Acids Res. 35, 5789-5798 (2007).
PubMed: 17720715

Assembly members:

Assembly members:
ERCC1 central, polymer, 135 residues, 14153.570 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ERCC1 central: MAKSNSIIVSPRQRGNPVLK FVRNVPWEFGDVIPDYVLGQ STCALFLSLRYHNLHPDYIH GRLQSLGKNFALRVLLVQVD VKDPQQALKELAKMCILADC TLILAWSPEEAGRYLETYKA YEQKPGGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts443
15N chemical shifts125
1H chemical shifts914

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ERCC1 central1

Entities:

Entity 1, ERCC1 central 135 residues - 14153.570 Da.

1   METALALYSSERASNSERILEILEVALSER
2   PROARGGLNARGGLYASNPROVALLEULYS
3   PHEVALARGASNVALPROTRPGLUPHEGLY
4   ASPVALILEPROASPTYRVALLEUGLYGLN
5   SERTHRCYSALALEUPHELEUSERLEUARG
6   TYRHISASNLEUHISPROASPTYRILEHIS
7   GLYARGLEUGLNSERLEUGLYLYSASNPHE
8   ALALEUARGVALLEULEUVALGLNVALASP
9   VALLYSASPPROGLNGLNALALEULYSGLU
10   LEUALALYSMETCYSILELEUALAASPCYS
11   THRLEUILELEUALATRPSERPROGLUGLU
12   ALAGLYARGTYRLEUGLUTHRTYRLYSALA
13   TYRGLUGLNLYSPROGLYGLYLEUGLUHIS
14   HISHISHISHISHIS

Samples:

sample_1: ERCC1 central, [U-13C; U-15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_2: ERCC1 central, [U-15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 5.5; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D (H)CCH 1H-13C NOESYsample_1isotropicsample_conditions_1
2D NOESY 15N filteredsample_1isotropicsample_conditions_1

Software:

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAB62810 BAG37398
GB AAA35810 AAA52394 AAC16253 AAH08930 AAH52813
PRF 1403276A
REF NP_001159521 NP_001181860 NP_001974 NP_973730 XP_001105868
SP P07992
AlphaFold P07992

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