BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25232

Title: Solution structure of the F231L mutant ERCC1-XPF dimerization region   PubMed: 26085086

Deposition date: 2014-09-17 Original release date: 2015-06-22

Authors: Faridounnia, Maryam; Wienk, Hans; Kovacic, Lidija; Folkers, Gert; Jaspers, Nicolaas; Kaptein, Robert; Hoeijmakers, Jan; Boelens, Rolf

Citation: Faridounnia, Maryam; Wienk, Hans; Kovacic, Lidija; Folkers, Gert; Jaspers, Nicolaas; Boelens, Rolf. "The Cerebro-Oculo-Facio-Skeletal (COFS) Syndrome point mutation F231L in the ERCC1 DNA repair protein causes dissociation of the ERCC1-XPF complex"  J. Biol. Chem. ., .-. (2015).

Assembly members:
entity_1, polymer, 96 residues, 10985.764 Da.
entity_2, polymer, 84 residues, 9230.592 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):
entity_1: RIRRRYNMADLLMEKLEQDL VSRVTECLTTVKSVNKTDSQ TLLTTFGSLEQLIAASREDL ALCPGLGPQKARRLFDVLHE PFLKVPGGLEHHHHHH
entity_2: MDSETLPESEKYNPGPQDFL LKMPGVNAKNCRSLMHHVKN IAELAALSQDELTSILGNAA NAKQLYDFIHTSFAEVVSKG KGKK

Data sets:
Data typeCount
13C chemical shifts695
15N chemical shifts172
1H chemical shifts1173

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 96 residues - 10985.764 Da.

1   ARGILEARGARGARGTYRASNMETALAASP
2   LEULEUMETGLULYSLEUGLUGLNASPLEU
3   VALSERARGVALTHRGLUCYSLEUTHRTHR
4   VALLYSSERVALASNLYSTHRASPSERGLN
5   THRLEULEUTHRTHRPHEGLYSERLEUGLU
6   GLNLEUILEALAALASERARGGLUASPLEU
7   ALALEUCYSPROGLYLEUGLYPROGLNLYS
8   ALAARGARGLEUPHEASPVALLEUHISGLU
9   PROPHELEULYSVALPROGLYGLYLEUGLU
10   HISHISHISHISHISHIS

Entity 2, entity_2 84 residues - 9230.592 Da.

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

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.4 mM; entity_2, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 8%; H2O 92%; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D HSQCsample_1isotropicsample_conditions_1
triple resonancesample_1isotropicsample_conditions_1
NOESYsample_1isotropicsample_conditions_1
2D HSQCsample_1isotropicsample_conditions_1
2D HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

CING, Doreleijers et al - validation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAG37398 BAG52472
GB AAA35810 AAA52394 AAC16253 AAH08930 AAM34796
PRF 1403276A
REF NP_001181860 NP_001974 XP_003817569 XP_003915760 XP_003915761
SP P07992

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