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 27533

Title: NBPF-15 HLS2-domain   PubMed: 31264103

Authors: Issaian, Aaron; Hansen, Kirk; Sikela, James; Vogeli, Beat; Henen, Morkos

Citation: Issaian, Aaron; Schmitt, Lauren; Born, Alexandra; Nichols, Parker; Sikela, James; Hansen, Kirk; Vogeli, Beat; Henen, Morkos. "Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains"  Biomol. NMR Assign. 13, 339-343 (2019).

Assembly members:
HLS-2, polymer, 106 residues, Formula weight is not available

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):
HLS-2: SAAAASSASLEIDMDEIEKY QEVEEDQDPSCPRLSRELLD EKEPEVLQDSLDRCYSTPSD YLELPDLGQPYSSAVYSLEE QYLGLALDVDRIKKDQEELE HHHHHH

Data sets:
Data typeCount
13C chemical shifts229
15N chemical shifts77
1H chemical shifts77

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HLS21

Entities:

Entity 1, HLS2 106 residues - Formula weight is not available

The numbering goes from 1-106 where 1-11 and 100-106 are cloning artifact and tags while actual protein is 12-99.

1   SERALAALAALAALASERSERALASERLEU
2   GLUILEASPMETASPGLUILEGLULYSTYR
3   GLNGLUVALGLUGLUASPGLNASPPROSER
4   CYSPROARGLEUSERARGGLULEULEUASP
5   GLULYSGLUPROGLUVALLEUGLNASPSER
6   LEUASPARGCYSTYRSERTHRPROSERASP
7   TYRLEUGLULEUPROASPLEUGLYGLNPRO
8   TYRSERSERALAVALTYRSERLEUGLUGLU
9   GLNTYRLEUGLYLEUALALEUASPVALASP
10   ARGILELYSLYSASPGLNGLUGLULEUGLU
11   HISHISHISHISHISHIS

Samples:

sample_1: HLS-2, [U-99% 13C; U-99% 15N], 320 uM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 600 MHz

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