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Biological Magnetic Resonance Data Bank


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BMRB Entry 25492

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25492
MolProbity Validation Chart

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Title: NMR structure of the HLTF HIRAN domain in its DNA-bound conformation.   PubMed: 26051180

Deposition date: 2015-02-18 Original release date: 2015-06-29

Authors: Korzhnev, Dmitry; Eldirany, Sherif

Citation: Kile, Andrew; Chavez, Diana; Bacal, Julien; Korzhnev, Dmitry; Eldirany, Sherif; Bezsonova, Irina; Eichman, Brandt; Cimprich, Karlene. "HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal"  Mol. Cell 58, 1090-1100 (2015).

Assembly members:
entity, polymer, 122 residues, 13532.442 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: GSDEEVDSVLFGSLRGHVVG LRYYTGVVNNNEMVALQRDP NNPYDKNAIKVNNVNGNQVG HLKKELAGALAYIMDNKLAQ IEGVVPFGANNAFTMPLHMT FWGKEENRKAVSDQLKKHGF KL

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts116
1H chemical shifts753

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 122 residues - 13532.442 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: entity, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

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 HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY CN_filteredsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement

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

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Agilent PremiumCOMPACT 800 MHz

Related Database Links:

BMRB 17085 18458
PDB
DBJ BAD92289 BAF83920
EMBL CAA86571 CAD10805
GB AAA67436 AAB27691 AAH05260 AAH15498 AAH30976
REF NP_003062 NP_620636 XP_001138277 XP_002814205 XP_003256297
SP Q14527

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