BMRB Entry 18532

Name: RNA Aptamer for B. anthracis Ribosomal Protein S8
Published: 2013-12-16

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PDB ID: 2lun
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18532
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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:

RNA Aptamer for B. anthracis Ribosomal Protein S8

Deposition date:

2012-06-18

Original release date:

2013-12-16

Authors:

Nikonowicz, Edward; Wang, Jiachen

Citation:

Citation: Donarski, James; Wang, Jiachen; Nikonowicz, Edward. "An RNA Aptamer Takes an Unexpected Twist to Bind r-Protein S8" Unknown ., .-..

Assembly members:

Assembly members:
RNA, polymer, 28 residues, 111.103 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: enzymatic semisynthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA: GGGCAGUGAUGCUUCGGCAU AUCAGCCC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	201
15N chemical shifts	65
1H chemical shifts	195

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNA, 1	1
2	RNA, 2	1
3	RNA, 3	1
4	RNA, 4	1
5	RNA, 5	1
6	RNA, 6	1
7	RNA, 7	1
8	RNA, 8	1
9	RNA, 9	1

Entities:

Entity 1, RNA, 1 28 residues - 111.103 Da.

1

G

C

A

G

U

G

A

U

2

G

C

U

C

G

C

A

U

3

A

U

C

A

G

C

Samples:

sample_1: RNA, [U-98% 13C; U-98% 15N], 1.5 ± 0.1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: RNA, [U-98% 13C; U-98% 15N], 1.6 ± 0.1 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

sample_conditions_2: ionic strength: 50 mM; pH*: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
3D HCCH-COSY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-31P HetCor	sample_2	isotropic	sample_conditions_2
2D 1H-15N HNC-TOCSY-CH	sample_1	isotropic	sample_conditions_2
2D 1H-13C H(N)CO	sample_1	isotropic	sample_conditions_1
2D 1H-13C CCH-COSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HCNC	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-15N HCN	sample_2	isotropic	sample_conditions_2

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

FELIX, Accelrys Software Inc. - data analysis

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz
Varian INOVA 500 MHz