BMRB Entry 27287

Name: Catalytic Domain of Human Aprataxin
Published: 2018-07-17

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27287

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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:

Catalytic Domain of Human Aprataxin

Deposition date:

2017-10-18

Original release date:

2018-07-17

Authors:

Mueller, Geoffrey; Tumbale, Percy; Schellenberg, Matthew; Williams, Scott; London, Robert

Citation:

Citation: Tumbale, Percy; Schellenberg, Matthew; Mueller, Geoffrey; Fairweather, Emma; Watson, Mandy; Little, Jessica; Krahn, Juno; Waddell, Ian; London, Robert; Williams, R Scott. "Mechanism of APTX nicked DNA sensing and pleiotropic inactivation in neurodegenerative disease" EMBO J. 37, e98875-e98875 (2018).
PubMed: 29934293

Assembly members:

Assembly members:
hAPTX, polymer, 192 residues, Formula weight is not available

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 Vector: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hAPTX: GSHMKDAPIKKESLGHWSQG LKISMQDPKMQVYKDEQVVV IKDKYPKARYHWLVLPWTSI SSLKAVAREHLELLKHMHTV GEKVIVDFAGSSKLRFRLGY HAIPSMSHVHLHVISQDFDS PCLKNKKHWNSFNTEYFLES QAVIEMVQEAGRVTVRDGMP ELLKLPLRCHECQQLLPSIP QLKEHLRKHWTQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	312
15N chemical shifts	149
1H chemical shifts	149

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	APTX	1

Entities:

Entity 1, APTX 192 residues - Formula weight is not available

1

GLY

SER

HIS

MET

LYS

ASP

ALA

PRO

ILE

LYS

2

LYS

GLU

SER

LEU

GLY

HIS

TRP

SER

GLN

GLY

3

LEU

LYS

ILE

SER

MET

GLN

ASP

PRO

LYS

MET

4

GLN

VAL

TYR

LYS

ASP

GLU

GLN

VAL

5

ILE

LYS

ASP

LYS

TYR

PRO

LYS

ALA

ARG

TYR

6

HIS

TRP

LEU

VAL

LEU

PRO

TRP

THR

SER

ILE

7

SER

LEU

LYS

ALA

VAL

ALA

ARG

GLU

HIS

8

LEU

GLU

LEU

LYS

HIS

MET

HIS

THR

VAL

9

GLY

GLU

LYS

VAL

ILE

VAL

ASP

PHE

ALA

GLY

10

SER

LYS

LEU

ARG

PHE

ARG

LEU

GLY

TYR

11

HIS

ALA

ILE

PRO

SER

MET

SER

HIS

VAL

HIS

12

LEU

HIS

VAL

ILE

SER

GLN

ASP

PHE

ASP

SER

13

PRO

CYS

LEU

LYS

ASN

LYS

HIS

TRP

ASN

14

SER

PHE

ASN

THR

GLU

TYR

PHE

LEU

GLU

SER

15

GLN

ALA

VAL

ILE

GLU

MET

VAL

GLN

GLU

ALA

16

GLY

ARG

VAL

THR

VAL

ARG

ASP

GLY

MET

PRO

17

GLU

LEU

LYS

LEU

PRO

LEU

ARG

CYS

HIS

18

GLU

CYS

GLN

LEU

PRO

SER

ILE

PRO

19

GLN

LEU

LYS

GLU

HIS

LEU

ARG

LYS

HIS

TRP

20

THR

GLN

Samples:

sample_1: hAPTX, [U-100% 13C; U-100% 15N], 1 mM; Na phosphate NaH2PO4 5 mM; KCl 1.3 mM; NaCl 67 mM; K phosphate KH2PO4 0.8 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks