Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62

The global genome nucleotide excision repair factor XPC firstly detects DNA lesions and then recruits a ten-subunit complex TFIIH through binding to the subunit p62 to unwind the damaged DNA for excision repair. This data article contains detailed nuclear magnetic resonance (NMR) restraints (nuclear Overhauser enhancement (NOE)-derived distance restraints, dihedral angle restraints, and hydrogen bond restraints) used for the structure determination of the complex formed between the intrinsically disordered acidic region of XPC and the pleckstrin homology (PH) domain of TFIIH p62, related to the recent work entitled “Structural insight into the mechanism of TFIIH recognition by the acidic string of the nucleotide excision repair factor XPC.” [1].


a b s t r a c t
The global genome nucleotide excision repair factor XPC firstly detects DNA lesions and then recruits a ten-subunit complex TFIIH through binding to the subunit p62 to unwind the damaged DNA for excision repair. This data article contains detailed nuclear magnetic resonance (NMR) restraints (nuclear Overhauser enhancement (NOE)-derived distance restraints, dihedral angle restraints, and hydrogen bond restraints) used for the structure determination of the complex formed between the intrinsically disordered acidic region of XPC and the pleckstrin homology (PH) domain of TFIIH p62, related to the recent work entitled "Structural insight into the mechanism of TFIIH recognition by the acidic string of the nucleotide excision repair factor XPC." [1]. & 2016 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

Value of the data
The dataset helps researchers to design their NMR experiments. The dataset is useful for the trial calculation of a protein complex structure. The detailed NMR restraint dataset is useful for evaluation of structure simulation procedures of a protein complex by using a limited amount of data from the data set.
The dataset provides structural insights into intrinsically disordered regions.
Note that we chose the intraresidue NOEs from only residues whose side-chains were stereospecifically assigned.

Hydrogen bond restraints
We performed the H/D-exchange experiment to obtain hydrogen bond restraints. As a reference spectrum, a 1 H, 15 N HSQC spectrum was taken for the sample of p62-XPC_H 2 O. We prepared the lyophilized sample of p62-XPC_H 2 O, and then immediately after adding D 2 O to the lyophilized sample, a series of 1 H, 15 N HSQC spectra were taken. Hydrogen-bond donors were identified by comparing those spectra with the reference spectrum. Hydrogen-bond donor-acceptor pairs were determined based on the final structure.
The H/D-exchange experiment provided 96 (48 Â 2) hydrogen bond restraints for the p62 PH domain in complex (Tables 2 and S9). No hydrogen bond restraints were available for XPC 109-156 , because of the fast H/D-exchange.