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Biological Magnetic Resonance Data Bank


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BMRB Entry 17085

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17085

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Title: NMR structure of the HLTF HIRAN domain

Deposition date: 2010-07-28 Original release date: 2012-05-14

Authors: Bezsonova, Irina; Neculai, Dante; Weigelt, Johan; Bountra, Chas; Edwards, Aled; Arrowsmith, Cheryl; Dhe-Paganon, Sirano

Citation: Neculai, Dante; Bezsonova, Irina; Weigelt, Johan; Bountra, Chas; Edwards, Aled; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "NMR structure of the HLTF HIRAN domain"  Not known ., .-..

Assembly members:
HLTF, 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):
HLTF: GSDEEVDSVLFGSLRGHVVG LRYYTGVVNNNEMVALQRDP NNPYDKNAIKVNNVNGNQVG HLKKELAGALAYIMDNKLAQ IEGVVPFGANNAFTMPLHMT FWGKEENRKAVSDQLKKHGF KL

Data sets:
Data typeCount
13C chemical shifts453
15N chemical shifts116
1H chemical shifts750

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HLTF1

Entities:

Entity 1, HLTF 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: HLTF HIRAN domain, [U-100% 13C; U-100% 15N], 1-1.6 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O 10%; H2O 90%

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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CC-TOCSYsample_1isotropicsample_conditions_1
3D aro-NOESYsample_1isotropicsample_conditions_1
3D aro-TOCSYsample_1isotropicsample_conditions_1
2D aro-HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

ABACUS, Lemak, Steren et al. - chemical shift assignment

MDDNMR, Jaravine and Orekhov - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18458 25492
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