BMRB Entry 30098

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30098
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR structure of the HLTF HIRAN domain
Deposition date:
2016-05-23
Original release date:
2016-06-06
Authors:
Bezsonova, I.; Neculai, D.; Korzhnev, D.; Weigelt, J.; Bountra, C.; Edwards, A.; Arrowsmith, C.; Dhe-Paganon, S.; Structural Genomics Consortium (SGC), SGC
Citation:

Citation: Korzhnev, Dmitry; Neculai, Dante; Dhe-Paganon, Sirano; Arrowsmith, Cheryl; Bezsonova, Irina. "Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins"  J. Biomol. NMR 66, 209-219 (2016).
PubMed: 27771863

Assembly members:

Assembly members:
entity_1, polymer, 122 residues, 13532.326 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDEEVDSVLFGSLRGHVVG LRYYTGVVNNNEMVALQRDP NNPYDKNAIKVNNVNGNQVG HLKKELAGALAYIMDNKLAQ IEGVVPFGANNAFTMPLHMT FWGKEENRKAVSDQLKKHGF KL

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts129
1H chemical shifts808

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 122 residues - 13532.326 Da.

1   GLYSERASPGLUGLUVALASPSERVALLEU
2   PHEGLYSERLEUARGGLYHISVALVALGLY
3   LEUARGTYRTYRTHRGLYVALVALASNASN
4   ASNGLUMETVALALALEUGLNARGASPPRO
5   ASNASNPROTYRASPLYSASNALAILELYS
6   VALASNASNVALASNGLYASNGLNVALGLY
7   HISLEULYSLYSGLULEUALAGLYALALEU
8   ALATYRILEMETASPASNLYSLEUALAGLN
9   ILEGLUGLYVALVALPROPHEGLYALAASN
10   ASNALAPHETHRMETPROLEUHISMETTHR
11   PHETRPGLYLYSGLUGLUASNARGLYSALA
12   VALSERASPGLNLEULYSLYSHISGLYPHE
13   LYSLEU

Samples:

sample_1: HLTF HIRAN domain, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

ABACUS, Lemak and Arrowsmith - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

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

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

NMR spectrometers:

  • Agilent VNMRS 800 MHz

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