BMRB Entry 6551

Title:
Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF
Deposition date:
2005-03-18
Original release date:
2005-12-14
Authors:
Tripsianes, K.; Folkers, G.; Odijk, H.; Jaspers, N.; Hoeijmakers, J.; Kaptein, R.; Boelens, R.
Citation:

Citation: Tripsianes, Konstantinos; Folkers, Gert; AB, Eiso; Das, Devashish; Odijk, Hanny; Jaspers, Nicolaas; Hoeijmakers, Jan; Kaptein, Robert; Boelens, Rolf. "The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision Repair "  Structure (Cambridge, MA, U. S.) 13, 1849-1858 (2005).
PubMed: 16338413

Assembly members:

Assembly members:
ERCC-1, polymer, 89 residues, Formula weight is not available
XPF, polymer, 84 residues, Formula weight is not available

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

Data sets:
Data typeCount
1H chemical shifts1184
13C chemical shifts575
15N chemical shifts165

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA excision repair protein ERCC-11
2DNA repair endonuclease XPF2

Entities:

Entity 1, DNA excision repair protein ERCC-1 89 residues - Formula weight is not available

1   METALAASPLEULEUMETGLULYSLEUGLU
2   GLNASPPHEVALSERARGVALTHRGLUCYS
3   LEUTHRTHRVALLYSSERVALASNLYSTHR
4   ASPSERGLNTHRLEULEUTHRTHRPHEGLY
5   SERLEUGLUGLNLEUILEALAALASERARG
6   GLUASPLEUALALEUCYSPROGLYLEUGLY
7   PROGLNLYSALAARGARGLEUPHEASPVAL
8   LEUHISGLUPROPHELEULYSVALPROGLY
9   GLYLEUGLUHISHISHISHISHISHIS

Entity 2, DNA repair endonuclease XPF 84 residues - Formula weight is not available

1   METASPSERGLUTHRLEUPROGLUSERGLU
2   LYSTYRASNPROGLYPROGLNASPPHELEU
3   LEULYSMETPROGLYVALASNALALYSASN
4   CYSARGSERLEUMETHISHISVALLYSASN
5   ILEALAGLULEUALAALALEUSERGLNASP
6   GLULEUTHRSERILELEUGLYASNALAALA
7   ASNALALYSGLNLEUTYRASPPHEILEHIS
8   THRSERPHEALAGLUVALVALSERLYSGLY
9   LYSGLYLYSLYS

Samples:

sample_1: ERCC-1, [U-15N; U-13C], 1.5 mM; XPF, [U-15N; U-13C], 1.5 mM; phosphate 50 mM; NaCl 100 mM; D2O 8%; H2O 92%

sample_2: ERCC-1, [U-15N], 1 mM; XPF, [U-15N], 1 mM; phosphate 50 mM; NaCl 100 mM; D2O 8%; H2O 92%

sample_cond_1: pH: 7.0; temperature: 295.5 K; ionic strength: 150 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
(h)cCH NOESY HSQCnot availablenot availablenot available
(h)nCH NOESY HSQCnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D NOESY 15N filterednot availablenot availablenot available

Software:

XWINNMR v3.5 - collection

NMRPipe v2.3 - processing

Sparky v3.110 - data analysis

cyana v2.0 - structure solution

CNS v1.1 - refinement

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

BMRB 6851 6851 6502
PDB
DBJ BAF82415 BAG63350 BAG63350 BAF82415
GB AAB07689 AAB50174 AAI60102 AAL91593 EAW85117
REF NP_005227 XP_003832737 XP_004057285 XP_510831 XP_510831 NP_005227
SP Q92889
SWISS-PROT Q92889
GenBank EAW85117 AAL91593 AAI60102 AAB50174 AAB07689
AlphaFold Q92889 Q92889

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