BMRB Entry 19993

Name: Lysyl t-RNA synthetase 1-72
Published: 2017-07-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19993

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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:

Lysyl t-RNA synthetase 1-72

Deposition date:

2014-05-29

Original release date:

2017-07-05

Authors:

Mushtaq, Ameeq; Cho, Hye; Jeon, Young

Citation:

Citation: Cho, Hye Young; Ul Mushtaq, Ameeq; Lee, Jin Young; Kim, Dae Gyu; Seok, Min Sook; Jang, Minseok; Han, Byung-Woo; Kim, Sunghoon; Jeon, Young Ho. "Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR" FEBS Lett. 588, 2851-2858 (2014).
PubMed: 24983501

Assembly members:

Assembly members:
LysRS1-72, polymer, 72 residues, Formula weight is not available

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: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LysRS1-72: MAAVQAAEVKVDGSEPKLSK NELKRRLKAEKKVAEKEAKQ KELSEKQLSQATAAATNHTT DNGVGPEEESVD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	166
15N chemical shifts	61
1H chemical shifts	226
T1 relaxation values	43
T2 relaxation values	43
heteronuclear NOE values	40

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lysyl t-RNA synthetase1-72	1

Entities:

Entity 1, Lysyl t-RNA synthetase1-72 72 residues - Formula weight is not available

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

GLY

PRO

GLU

SER

8

VAL

ASP

Samples:

sample_1: LysRS residues 1-72, [U-13C; U-15N], 0.2 mM; sodium chloride 100 mM; HEPES 20 mM; DTT 1 mM; PMSF 1 mM; D2O 10%; H2O 90%

sample_2: LysRS residues 1-72, [U-15N], 0.2 mM; sodium chloride 100 mM; HEPES 20 mM; DTT 1 mM; PMSF 1 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC -T2	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC-T1	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC-NOE	sample_2	isotropic	sample_conditions_1

Software:

CCPN v2.1.5, CCPN, Goddard - Relaxation data analysis, chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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