BMRB Entry 36352

Name: Solution structure of a DNA binding protein from Sulfolobus islandicus
Published: 2025-10-24

Click here to enlarge.

PDB ID: 7bzh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36352
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of a DNA binding protein from Sulfolobus islandicus

Deposition date:

2020-04-28

Original release date:

2025-10-24

Authors:

Zhang, Z.; Liu, X.

Citation:

Citation: Huang, Can; Liu, Xuehui; Chen, Yuanyuan; Zhou, Junshi; Li, Wenqian; Ding, Niannian; Huang, Li; Chen, Jingyu; Zhang, Zhenfeng. "A Novel Family of Winged-Helix Single-Stranded DNA-Binding Proteins from Archaea." Int. J. Mol. Sci. 23, 3455-3455 (2022).
PubMed: 35408816

Assembly members:

Assembly members:
Sul7s, polymer, 59 residues, 7226.358 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 43080 Superkingdom: Archaea Kingdom: Thermoproteati Genus/species: Saccharolobus islandicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sul7s: MEDVKQSVEKIIKDREWVTF NDLLKYIPYPAPEVYDALSQ LIKENKVGRRGRYFYYIKR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	253
15N chemical shifts	58
1H chemical shifts	454

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 59 residues - 7226.358 Da.

1

MET

GLU

ASP

VAL

LYS

GLN

SER

VAL

GLU

LYS

2

ILE

LYS

ASP

ARG

GLU

TRP

VAL

THR

PHE

3

ASN

ASP

LEU

LYS

TYR

ILE

PRO

TYR

PRO

4

ALA

PRO

GLU

VAL

TYR

ASP

ALA

LEU

SER

GLN

5

LEU

ILE

LYS

GLU

ASN

LYS

VAL

GLY

ARG

6

GLY

ARG

TYR

PHE

TYR

ILE

LYS

ARG

Samples:

15N_13C_sample: Sul7s, [U-100% 13C; U-100% 15N], 0.7 mM; NaN3 0.02 w/v; NaCl 30 mM; PBS 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 30 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
Nhsqc	15N_13C_sample	isotropic	sample_conditions_1
Chsqc	15N_13C_sample	isotropic	sample_conditions_1
3D HNCO	15N_13C_sample	isotropic	sample_conditions_1
3D HNCACB	15N_13C_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	15N_13C_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_13C_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	15N_13C_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	15N_13C_sample	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis, CCPN - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Agilent DD2 600 MHz

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