BMRB Entry 51440

Name: Identification and characterization of an RRM-containing, RNA binding protein in Acinetobacter Baumannii
Published: 2022-09-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51440

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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:

Identification and characterization of an RRM-containing, RNA binding protein in Acinetobacter Baumannii

Deposition date:

2022-05-13

Original release date:

2022-09-19

Authors:

Ciani, Caterina; Perez-Rafols, Anna; Bonomo, Isabelle; Micaelli, Mariachiara; Esposito, Alfonso; Zucal, Chiara; Belli, Romina; D'Agostino, Vito Giuseppe; Bianconi, Irene; Calderone, Vito; Cerofolini, Linda; Fragai, Marco; Provenzani, Alessandro

Citation:

Citation: Ciani, Caterina; Perez-Rafols, Anna; Bonomo, Isabelle; Micaelli, Mariachiara; Esposito, Alfonso; Zucal, Chiara; Belli, Romina; D'Agostino, Vito Giuseppe; Bianconi, Irene; Calderone, Vito; Cerofolini, Linda; Massidda, Orietta; Whalen, Michael Bernard; Fragai, Marco; Provenzani, Alessandro. "Identification and characterization of an RRM-containing, RNA binding protein in Acinetobacter Baumannii" Biomolecules 12, 922-922 (2022).
PubMed: 35883478

Assembly members:

Assembly members:
entity_1, polymer, 107 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Acinetobacter Baumannii Taxonomy ID: 470 Superkingdom: Bacteria Kingdom: not available Genus/species: Acinetobacter Baumannii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-30a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHMILKCILAFLLMVNEGWK MKILVRNLDRSVTEAEVLEL FKAYGKVESCVVVTDKDTGK SKGFGFVEMPNPREAIKAIK GLNTLKVKGYGIRVKAAEEL EHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	232
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AB-Elavl	1

Entities:

Entity 1, AB-Elavl 107 residues - Formula weight is not available

1

MET

HIS

MET

ILE

LEU

LYS

CYS

ILE

LEU

ALA

2

PHE

LEU

MET

VAL

ASN

GLU

GLY

TRP

LYS

3

MET

LYS

ILE

LEU

VAL

ARG

ASN

LEU

ASP

ARG

4

SER

VAL

THR

GLU

ALA

GLU

VAL

LEU

GLU

LEU

5

PHE

LYS

ALA

TYR

GLY

LYS

VAL

GLU

SER

CYS

6

VAL

THR

ASP

LYS

ASP

THR

GLY

LYS

7

SER

LYS

GLY

PHE

GLY

PHE

VAL

GLU

MET

PRO

8

ASN

PRO

ARG

GLU

ALA

ILE

LYS

ALA

ILE

LYS

9

GLY

LEU

ASN

THR

LEU

LYS

VAL

LYS

GLY

TYR

10

GLY

ILE

ARG

VAL

LYS

ALA

GLU

LEU

11

GLU

HIS

Samples:

sample_1: AB-Elavl, [U-100% 13C; U-100% 15N], 300 uM; HEPES 20 mM; NaCl 150 mM; MgCl2 3 mM; AEBSF protease inhibitor 1 mM

sample_conditions_1: ionic strength: 0.309 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v4.1.3 - collection, processing

CARA v1.8 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 900 MHz

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