BMRB Entry 28113

Name: revmodN_ACC
Published: 2020-07-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28113

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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:

revmodN_ACC

Deposition date:

2020-04-11

Original release date:

2020-07-01

Authors:

Liu, Sheng; Refaei, Mary Anne; Decker, Aaron; Hinerman, Jennifer; Herr, Andrew; Liu, Shuohui; Howell, Michael; Musier-Forsyth, Karin; Tsang, Pearl

Citation:

Citation: Liu, Sheng; Refaei, Maryanne; Liu, Shuohui; Decker, Aaron; Hinerman, Jennifer; Herr, Andrew; Howell, Mike; Musier-Forsyth, Karin; Tsang, Pearl. "Hairpin RNA-induced conformational change of a eukaryotic-specific lysyl-tRNA synthetase extension and role of adjacent anticodon-binding domain" J. Biol. Chem. 295, 12071-12085 (2020).
PubMed: 32611767

Assembly members:

Assembly members:
tRNAlys_Acceptor_stem, polymer, 35 residues, 11225.8 Da.
revmodN_protein, polymer, 76 residues, 8311.3 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
tRNAlys_Acceptor_stem: GCCCGGACAGGGUUCAAGUC CCUGUUCGGGCGCCA
revmodN_protein: MAAVQAAEVKVDGSEPKLSK NELKRRLKAEKKVAEKEAKQ KELSEKQLSQATAAATNHTT DNGVLPETGGHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	198
15N chemical shifts	68
1H chemical shifts	68

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lysyl tRNA acceptor stem	1
2	revmodN	2

Entities:

Entity 1, Lysyl tRNA acceptor stem 35 residues - 11225.8 Da.

This is the acceptor stem loop of human Lysyl tRNA isoacceptor 3

1

G

C

G

A

C

A

G

2

G

U

C

A

G

U

C

3

C

U

G

U

C

G

4

C

G

C

A

Entity 2, revmodN 76 residues - 8311.3 Da.

Residues 70-76 are appended to this domain for enzyme ligation

1

MET

ALA

VAL

GLN

ALA

GLU

VAL

LYS

2

VAL

ASP

GLY

SER

GLU

PRO

LYS

LEU

SER

LYS

3

ASN

GLU

LEU

LYS

ARG

LEU

LYS

ALA

GLU

4

LYS

VAL

ALA

GLU

LYS

GLU

ALA

LYS

GLN

5

LYS

GLU

LEU

SER

GLU

LYS

GLN

LEU

SER

GLN

6

ALA

THR

ALA

THR

ASN

HIS

THR

7

ASP

ASN

GLY

VAL

LEU

PRO

GLU

THR

GLY

8

HIS

Samples:

sample_1: revmodN protein, [U-99% 13C; U-99% 15N], 200 ± 20 uM; sodium phosphate 20 ± .05 mM; sodium chloride 15 ± .05 mM; potassium chloride 35 ± .05 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

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