BMRB Entry 34120

Name: Solution structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)
Published: 2017-06-30

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PDB ID: 5nko
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34120
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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:

Solution structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)

Deposition date:

2017-03-31

Original release date:

2017-06-30

Authors:

Usachev, K.; Khusainov, I.; Ayupov, R.; Validov, S.; Kieffer, B.; Yusupov, M.

Citation:

Citation: Khusainov, Iskander; Vicens, Quentin; Ayupov, Rustam; Usachev, Konstantin; Myasnikov, Alexander; Simonetti, Angelita; Validov, Shamil; Kieffer, Bruno; Yusupova, Gulnara; Yusupov, Marat; Hashem, Yaser. "Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF" EMBO J. 36, 2073-2087 (2017).
PubMed: 28645916

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, 7124.070 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 93061 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pGS21A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MIEIIRSKEFSLKPMDSEEA VLQMNLLGHDFFVFTDRETD GTSIVYRRKDGKYGLIQTSE Q

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	516
15N chemical shifts	120
1H chemical shifts	760

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 61 residues - 7124.070 Da.

1

MET

ILE

GLU

ILE

ARG

SER

LYS

GLU

PHE

2

SER

LEU

LYS

PRO

MET

ASP

SER

GLU

ALA

3

VAL

LEU

GLN

MET

ASN

LEU

GLY

HIS

ASP

4

PHE

VAL

PHE

THR

ASP

ARG

GLU

THR

ASP

5

GLY

THR

SER

ILE

VAL

TYR

ARG

LYS

ASP

6

GLY

LYS

TYR

GLY

LEU

ILE

GLN

THR

SER

GLU

7

GLN

Samples:

sample_1: C-terminal domain of SaHPF, [U-99% 13C; U-99% 15N], 2.0 mM; NH4Cl 250 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.6; pressure: 1 bar; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceIII 700 MHz

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