BMRB Entry 27532

Name: Backbone and side chain NMR assignments for the ribosome Binding Factor A (RbfA) from Staphylococcus aureus
Published: 2018-10-03

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PDB ID: 6ye5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27532
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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 and side chain NMR assignments for the ribosome Binding Factor A (RbfA) from Staphylococcus aureus

Deposition date:

2018-07-03

Original release date:

2018-10-03

Authors:

Usachev, Konstantin; Blokhin, Dmitriy; Bikmullin, Aydar; Nurullina, Liliya; Validov, Shamil; Garaeva, Natalia; Klochkov, Vladimir; Aganov, Albert; Khusainov, Iskander; Yusupov, Marat

Citation:

Citation: Blokhin, Dmitriy; Bikmullin, Aydar; Nurullina, Liliya; Garaeva, Natalia; Validov, Shamil; Klochkov, Vladimir; Aganov, Albert; Khusainov, Iskander; Yusupov, Marat; Usachev, Konstantin. "Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus" Biomol. NMR Assignments 13, 27-30 (2019).
PubMed: 30225569

Assembly members:

Assembly members:
RbfA, polymer, 118 residues, 13669.7691 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RbfA: GSSMRAERVGEQMKKELMDI INNKVKDPRVGFITITDVVL TNDLSQAKVFLTVLGNDKEV ENTFKALDKAKGFIKSELGS RMRLRIMPELMYEYDQSIEY GNKIERMIQDLHKQDRVE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
coupling_constants
- coupling_constant_list

Data type	Count
13C chemical shifts	339
15N chemical shifts	102
1H chemical shifts	390
coupling constants	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RbfA	1

Entities:

Entity 1, RbfA 118 residues - 13669.7691 Da.

1

GLY

SER

MET

ARG

ALA

GLU

ARG

VAL

GLY

2

GLU

GLN

MET

LYS

GLU

LEU

MET

ASP

ILE

3

ILE

ASN

LYS

VAL

LYS

ASP

PRO

ARG

VAL

4

GLY

PHE

ILE

THR

ILE

THR

ASP

VAL

LEU

5

THR

ASN

ASP

LEU

SER

GLN

ALA

LYS

VAL

PHE

6

LEU

THR

VAL

LEU

GLY

ASN

ASP

LYS

GLU

VAL

7

GLU

ASN

THR

PHE

LYS

ALA

LEU

ASP

LYS

ALA

8

LYS

GLY

PHE

ILE

LYS

SER

GLU

LEU

GLY

SER

9

ARG

MET

ARG

LEU

ARG

ILE

MET

PRO

GLU

LEU

10

MET

TYR

GLU

TYR

ASP

GLN

SER

ILE

GLU

TYR

11

GLY

ASN

LYS

ILE

GLU

ARG

MET

ILE

GLN

ASP

12

LEU

HIS

LYS

GLN

ASP

ARG

VAL

GLU

Samples:

sample_1: RbfA, [U-100% 13C; U-100% 15N], 0.9 mM; phosphate buffer 50 mM; NH4Cl 250 mM

CondSet1: ionic strength: 0.250 M; pH: 7.600; pressure: 1.000 atm; temperature: 308.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	sample_1	isotropic	CondSet1
2D 1H-13C HSQC/HMQC	sample_1	isotropic	CondSet1
2D 1H-13C HSQC/HMQC	sample_1	isotropic	CondSet1
3D HNCA	sample_1	isotropic	CondSet1
3D HNCACB	sample_1	isotropic	CondSet1
3D CBCA(CO)NH	sample_1	isotropic	CondSet1
3D HNCO	sample_1	isotropic	CondSet1
HN(CA)CO (H[N[ca[CO]]])	sample_1	isotropic	CondSet1
CC(CO)NH (HNco_C.relayed)	sample_1	isotropic	CondSet1
3D H(CCO)NH	sample_1	isotropic	CondSet1
3D HNHA	sample_1	isotropic	CondSet1

Software:

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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