BMRB Entry 34185

Name: 6th KOW domain of human hSpt5
Published: 2018-10-26

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PDB ID: 6er0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34185
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

6th KOW domain of human hSpt5

Deposition date:

2017-10-16

Original release date:

2018-10-26

Authors:

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

Citation:

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).
PubMed: 30076330

Assembly members:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	516
15N chemical shifts	124
1H chemical shifts	817

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 127 residues - 13857.621 Da.

1

GLY

TYR

ASN

PRO

HIS

THR

PRO

GLY

SER

2

GLY

ILE

GLU

GLN

ASN

SER

ASP

TRP

VAL

3

THR

ASP

ILE

GLN

VAL

LYS

VAL

ARG

ASP

4

THR

TYR

LEU

ASP

THR

GLN

VAL

GLY

GLN

5

THR

GLY

VAL

ILE

ARG

SER

VAL

THR

GLY

6

MET

CYS

SER

VAL

TYR

LEU

LYS

ASP

SER

GLU

7

LYS

VAL

SER

ILE

SER

GLU

HIS

LEU

8

GLU

PRO

ILE

THR

PRO

THR

LYS

ASN

LYS

9

VAL

LYS

VAL

ILE

LEU

GLY

GLU

ASP

ARG

GLU

10

ALA

THR

GLY

VAL

LEU

SER

ILE

ASP

GLY

11

GLU

ASP

GLY

ILE

VAL

ARG

MET

ASP

LEU

ASP

12

GLU

GLN

LEU

LYS

ILE

LEU

ASN

LEU

ARG

PHE

13

LEU

GLY

LYS

LEU

GLU

ALA

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks