BMRB Entry 34184

Name: 4th KOW domain of human hSpt5
Published: 2018-10-12

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PDB ID: 6eqy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34184
MolProbity Validation Chart

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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: 4th KOW domain of human hSpt5 PubMed: 30076330

Deposition date: 2017-10-16 Original release date: 2018-10-12

Authors: Zuber, P.; 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, 129 residues, 14414.549 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: AMGSETASGVDVGGQHEWGE LVQLDPQTVGVIVRLERETF QVLNMYGKVVTVRHQAVTRK KDNRFAVALDSEQNNIHVKD IVKVIDGPHSGREGEIRHLF RSFAFLHCKKLVENGGMFVC KTRHLVLAG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	522
15N chemical shifts	126
1H chemical shifts	844

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_1 129 residues - 14414.549 Da.

1

ALA

MET

GLY

SER

GLU

THR

ALA

SER

GLY

VAL

2

ASP

VAL

GLY

GLN

HIS

GLU

TRP

GLY

GLU

3

LEU

VAL

GLN

LEU

ASP

PRO

GLN

THR

VAL

GLY

4

VAL

ILE

VAL

ARG

LEU

GLU

ARG

GLU

THR

PHE

5

GLN

VAL

LEU

ASN

MET

TYR

GLY

LYS

VAL

6

THR

VAL

ARG

HIS

GLN

ALA

VAL

THR

ARG

LYS

7

LYS

ASP

ASN

ARG

PHE

ALA

VAL

ALA

LEU

ASP

8

SER

GLU

GLN

ASN

ILE

HIS

VAL

LYS

ASP

9

ILE

VAL

LYS

VAL

ILE

ASP

GLY

PRO

HIS

SER

10

GLY

ARG

GLU

GLY

GLU

ILE

ARG

HIS

LEU

PHE

11

ARG

SER

PHE

ALA

PHE

LEU

HIS

CYS

LYS

12

LEU

VAL

GLU

ASN

GLY

MET

PHE

VAL

CYS

13

LYS

THR

ARG

HIS

LEU

VAL

LEU

ALA

GLY

Samples:

sample_1: KOW4, [U-99% 13C; U-99% 15N], 0.6 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	anisotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	anisotropic	sample_conditions_1
3D HNCO	sample_1	anisotropic	sample_conditions_1
3D HNCA	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	anisotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	anisotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	anisotropic	sample_conditions_1
3D HNCACB	sample_1	anisotropic	sample_conditions_1
3D C(CO)NH	sample_1	anisotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	anisotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

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