BMRB Entry 27131

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for 98-243
Published: 2017-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27131

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for 98-243

Deposition date:

2017-06-09

Original release date:

2017-09-14

Authors:

Sugitani, Norie; Voehler, Markus; Roh, Michelle; Topolska-Wo, Agnieszka; Chazin, Walter

Citation:

Citation: Sugitani, Norie; Voehler, Markus; Roh, Michelle; Topolska-Wo, Agnieszka; Chazin, Walter. "Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates" J. Biol. Chem. 292, 16847-16857 (2017).
PubMed: 28860187

Assembly members:

Assembly members:
XPA98-239, polymer, 146 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: pBG100

Entity Sequences (FASTA):

Entity Sequences (FASTA):
XPA98-239: GPGSMEFDYVICEECGKEFM DSYLMNHFDLPTCDNCRDAD DKHKLITKTEAKQEYLLKDC DLEKREPPLKFIVKKNPHHS QWGDMKLYLKLQIVKRSLEV WGSQEALEEAKEVRQENREK MKQKKFDKKVKELRRAVRSS VWKRET

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	415
15N chemical shifts	137
1H chemical shifts	137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	XPA98-239	1

Entities:

Entity 1, XPA98-239 146 residues - Formula weight is not available

1

GLY

PRO

GLY

SER

MET

GLU

PHE

ASP

TYR

VAL

2

ILE

CYS

GLU

CYS

GLY

LYS

GLU

PHE

MET

3

ASP

SER

TYR

LEU

MET

ASN

HIS

PHE

ASP

LEU

4

PRO

THR

CYS

ASP

ASN

CYS

ARG

ASP

ALA

ASP

5

ASP

LYS

HIS

LYS

LEU

ILE

THR

LYS

THR

GLU

6

ALA

LYS

GLN

GLU

TYR

LEU

LYS

ASP

CYS

7

ASP

LEU

GLU

LYS

ARG

GLU

PRO

LEU

LYS

8

PHE

ILE

VAL

LYS

ASN

PRO

HIS

SER

9

GLN

TRP

GLY

ASP

MET

LYS

LEU

TYR

LEU

LYS

10

LEU

GLN

ILE

VAL

LYS

ARG

SER

LEU

GLU

VAL

11

TRP

GLY

SER

GLN

GLU

ALA

LEU

GLU

ALA

12

LYS

GLU

VAL

ARG

GLN

GLU

ASN

ARG

GLU

LYS

13

MET

LYS

GLN

LYS

PHE

ASP

LYS

VAL

14

LYS

GLU

LEU

ARG

ALA

VAL

ARG

SER

15

VAL

TRP

LYS

ARG

GLU

THR

Samples:

sample_1: XPA, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 500 mM; TCEP 1 mM; DSS .5 mM

sample_conditions_1: ionic strength: 500 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRView v9.2.0-b2, Johnson, One Moon Scientific - data analysis

TALOS v3.80F1 Rev 2012.080.14.41, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - data analysis

TOPSPIN v3.5, Bruker Biospin - collection, processing

PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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