BMRB Entry 17675

Name: Backbone 1H,15N,13C and 13CB chemical shifts of folded state and denatured state for the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant
Published: 2011-10-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17675

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H,15N,13C and 13CB chemical shifts of folded state and denatured state for the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant

Deposition date:

2011-05-30

Original release date:

2011-10-12

Authors:

Meng, Wenli; Raleigh, Daniel

Citation:

Citation: Meng, Wenli; Raleigh, Daniel. "Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions." Proteins 79, 3500-3510 (2011).
PubMed: 21915914

Assembly members:

Assembly members:
NTL9_V3AI4A, polymer, 56 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Geobacillus stearothermophilus Taxonomy ID: 1422 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacillus stearothermophilus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NTL9_V3AI4A: MKAAFLKDVKGKGKKGEIKN VADGYANNFLFKQGLAIEAT PANLKALEAQKQKEQR

Data sets:

assigned_chemical_shifts
- folded_state_assignment
- denatured_state_assignment

Data type	Count
13C chemical shifts	317
15N chemical shifts	105
1H chemical shifts	210

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	folded state	1
2	denatured state	1

Entities:

Entity 1, folded state 56 residues - Formula weight is not available

1

MET

LYS

ALA

PHE

LEU

LYS

ASP

VAL

LYS

2

GLY

LYS

GLY

LYS

GLY

GLU

ILE

LYS

ASN

3

VAL

ALA

ASP

GLY

TYR

ALA

ASN

PHE

LEU

4

PHE

LYS

GLN

GLY

LEU

ALA

ILE

GLU

ALA

THR

5

PRO

ALA

ASN

LEU

LYS

ALA

LEU

GLU

ALA

GLN

6

LYS

GLN

LYS

GLU

GLN

ARG

Samples:

15N_sample: NTL9_V3AI4A, [U-99% 15N], 0.5 mM; DSS 0.4 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 20 mM; H2O 90%; D2O 10%

13C15N_sample: NTL9_V3AI4A, [U-99% 13C; U-99% 15N], 0.5 mM; DSS 0.4 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.12 M; pH: 5.5; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C15N_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C15N_sample	isotropic	sample_conditions_1
3D HNCACB	13C15N_sample	isotropic	sample_conditions_1
3D HNCACB	13C15N_sample	isotropic	sample_conditions_1
3D HNCO	13C15N_sample	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N_sample	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 800 MHz