BMRB Entry 16610

Name: Solution structure of the N-terminal domain (residues 1-111) of Brugia malayi asparaginyl-tRNA synthetase
Published: 2012-08-03

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PDB ID: 2kqr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16610
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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 N-terminal domain (residues 1-111) of Brugia malayi asparaginyl-tRNA synthetase

Deposition date:

2009-11-16

Original release date:

2012-08-03

Authors:

Volkman, B.; Peterson, F.; Kron, M.

Citation:

Citation: Kron, Michael; Volkman, Brian; Peterson, Francis. "TBD" To be published ., .-..

Assembly members:

Assembly members:
AsnRS, polymer, 113 residues, 12667.689 Da.

Natural source:

Natural source: Common Name: B. malayi Taxonomy ID: 6279 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Brugia malayi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE30-8HT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AsnRS: GSMTVYICPETGDDGNDGSE LKPLRTLYQAMIITKSSKGD FLIRTKKDGKQVWEAASKTA LKKSWKRYEQEMLKNEKVAA KMLEKDATEVGVKAALEEAK KVQIELDTSLSYI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	505
15N chemical shifts	124
1H chemical shifts	846

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AsnRS	1

Entities:

Entity 1, AsnRS 113 residues - 12667.689 Da.

1

GLY

SER

MET

THR

VAL

TYR

ILE

CYS

PRO

GLU

2

THR

GLY

ASP

GLY

ASN

ASP

GLY

SER

GLU

3

LEU

LYS

PRO

LEU

ARG

THR

LEU

TYR

GLN

ALA

4

MET

ILE

THR

LYS

SER

LYS

GLY

ASP

5

PHE

LEU

ILE

ARG

THR

LYS

ASP

GLY

LYS

6

GLN

VAL

TRP

GLU

ALA

SER

LYS

THR

ALA

7

LEU

LYS

SER

TRP

LYS

ARG

TYR

GLU

GLN

8

GLU

MET

LEU

LYS

ASN

GLU

LYS

VAL

ALA

9

LYS

MET

LEU

GLU

LYS

ASP

ALA

THR

GLU

VAL

10

GLY

VAL

LYS

ALA

LEU

GLU

ALA

LYS

11

LYS

VAL

GLN

ILE

GLU

LEU

ASP

THR

SER

LEU

12

SER

TYR

ILE

Samples:

sample_1: AsnRS, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 53 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY (AROMATIC)	sample_1	isotropic	sample_conditions_1

Software:

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

XEASY, Bartels et al. - data analysis

GARANT v2.2, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance III 500 MHz

PDB	2KQR
EMBL	CDQ01803 CDQ01804 CDQ05032 CDQ06500
GB	AAA27849 AAA27852
REF	XP_001898693 XP_002372115
SP	P10723
AlphaFold	P10723