BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34185

Title: 6th KOW domain of human hSpt5   PubMed: 30076330

Deposition date: 2017-10-16 Original release date: 2018-10-26

Authors: Hahn, L.; Schweimer, K.; Roesch, P.; Woehrl, B.

Citation: Zuber, P.; Hahn, L.; Reinl, A.; Schweimer, K.; Knauer, S.; Gottesman, M.; Rosch, P.; Wohrl, B.. "Structure and nucleic acid binding properties of KOW domains 4 and 6-7 of human transcription elongation factor DSIF."  Sci. Rep. 8, 11660-11660 (2018).

Assembly members:
entity_1, polymer, 127 residues, 13857.621 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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: GGYNPHTPGSGIEQNSSDWV TTDIQVKVRDTYLDTQVVGQ TGVIRSVTGGMCSVYLKDSE KVVSISSEHLEPITPTKNNK VKVILGEDREATGVLLSIDG EDGIVRMDLDEQLKILNLRF LGKLLEA

Data sets:
Data typeCount
13C chemical shifts516
15N chemical shifts124
1H chemical shifts817

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 127 residues - 13857.621 Da.

1   GLYGLYTYRASNPROHISTHRPROGLYSER
2   GLYILEGLUGLNASNSERSERASPTRPVAL
3   THRTHRASPILEGLNVALLYSVALARGASP
4   THRTYRLEUASPTHRGLNVALVALGLYGLN
5   THRGLYVALILEARGSERVALTHRGLYGLY
6   METCYSSERVALTYRLEULYSASPSERGLU
7   LYSVALVALSERILESERSERGLUHISLEU
8   GLUPROILETHRPROTHRLYSASNASNLYS
9   VALLYSVALILELEUGLYGLUASPARGGLU
10   ALATHRGLYVALLEULEUSERILEASPGLY
11   GLUASPGLYILEVALARGMETASPLEUASP
12   GLUGLNLEULYSILELEUASNLEUARGPHE
13   LEUGLYLYSLEULEUGLUALA

Samples:

sample_1: KOW6, [U-99% 13C; U-99% 15N], 0.44 mM; sodium phosphate 20 mM; sodium chloride 20 mM; DTT 0.5 mM

sample_conditions_1: ionic strength: 40 mM; pH: 6.4; 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
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 1000 MHz

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