BMRB Entry 26752

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26752

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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 resonance assignments of the OB domain of the single stranded DNA binding protein hSSB1 (NABP2/OBFC2B)

Deposition date:

2016-03-07

Original release date:

2016-07-14

Authors:

Kariawasam, Ruvini; Touma, Christine; Cubeddu, Liza; Gamsjaeger, Roland

Citation:

Citation: Kariawasam, Ruvini; Touma, Christine; Cubeddu, Liza; Gamsjaeger, Roland. "Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA-binding protein hSSB1 (NABP2/OBFC2B) and chemical shift mapping of the DNA-binding interface" Biomol. NMR Assign. 10, 297-300 (2016).
PubMed: 27193589

Assembly members:

Assembly members:
hSSB1, polymer, 128 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: pGex6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hSSB1: GPLGSMTTETFVKDIKPGLK NLNLIFIVLETGRVTKTKDG HEVRTCKVADKTGSINISVW DDVGNLIQPGDIIRLTKGYA SVFKGCLTLYTGRGGDLQKI GEFCMVYSEVPNFSEPNPEY STQQAPNK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	116
1H chemical shifts	116

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hSSB1 protein	1

Entities:

Entity 1, hSSB1 protein 128 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

MET

THR

GLU

THR

2

PHE

VAL

LYS

ASP

ILE

LYS

PRO

GLY

LEU

LYS

3

ASN

LEU

ASN

LEU

ILE

PHE

ILE

VAL

LEU

GLU

4

THR

GLY

ARG

VAL

THR

LYS

THR

LYS

ASP

GLY

5

HIS

GLU

VAL

ARG

THR

CYS

LYS

VAL

ALA

ASP

6

LYS

THR

GLY

SER

ILE

ASN

ILE

SER

VAL

TRP

7

ASP

VAL

GLY

ASN

LEU

ILE

GLN

PRO

GLY

8

ASP

ILE

ARG

LEU

THR

LYS

GLY

TYR

ALA

9

SER

VAL

PHE

LYS

GLY

CYS

LEU

THR

LEU

TYR

10

THR

GLY

ARG

GLY

ASP

LEU

GLN

LYS

ILE

11

GLY

GLU

PHE

CYS

MET

VAL

TYR

SER

GLU

VAL

12

PRO

ASN

PHE

SER

GLU

PRO

ASN

PRO

GLU

TYR

13

SER

THR

GLN

ALA

PRO

ASN

LYS

Samples:

sample_1: hSSB1, [U-100% 13C; U-100% 15N], 200 – 800 uM; H2O 90%; D2O 10%; NaCl 50 mM; MES 10 mM; TCEP 3 mM

sample_conditions_1: ionic strength: 60 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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