BMRB Entry 19995

Name: LysRS Anticodon Binding Domian 72-207
Published: 2017-07-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19995

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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:

LysRS Anticodon Binding Domian 72-207

Deposition date:

2014-05-30

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:
LysRS_ABD_72-207, polymer, 136 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LysRS_ABD_72-207: DPNQYYKIRSQAIHQLKVNG EDPYPHKFHVDISLTDFIQK YSHLQPGDHLTDITLKVAGR IHAKRASGGKLIFYDLRGEG VKLQVMANSRNYKSEEEFIH INNKLRRGDIIGVQGNPGKT KKGELSIIPYEITLLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	317
15N chemical shifts	102
1H chemical shifts	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LysRS ABD 72-207	1

Entities:

Entity 1, LysRS ABD 72-207 136 residues - Formula weight is not available

1

ASP

PRO

ASN

GLN

TYR

LYS

ILE

ARG

SER

2

GLN

ALA

ILE

HIS

GLN

LEU

LYS

VAL

ASN

GLY

3

GLU

ASP

PRO

TYR

PRO

HIS

LYS

PHE

HIS

VAL

4

ASP

ILE

SER

LEU

THR

ASP

PHE

ILE

GLN

LYS

5

TYR

SER

HIS

LEU

GLN

PRO

GLY

ASP

HIS

LEU

6

THR

ASP

ILE

THR

LEU

LYS

VAL

ALA

GLY

ARG

7

ILE

HIS

ALA

LYS

ARG

ALA

SER

GLY

LYS

8

LEU

ILE

PHE

TYR

ASP

LEU

ARG

GLY

GLU

GLY

9

VAL

LYS

LEU

GLN

VAL

MET

ALA

ASN

SER

ARG

10

ASN

TYR

LYS

SER

GLU

PHE

ILE

HIS

11

ILE

ASN

LYS

LEU

ARG

GLY

ASP

ILE

12

ILE

GLY

VAL

GLN

GLY

ASN

PRO

GLY

LYS

THR

13

LYS

GLY

GLU

LEU

SER

ILE

PRO

TYR

14

GLU

ILE

THR

LEU

SER

Samples:

sample_1: LysRS ABD 72-207, [U-100% 13C; U-100% 15N], 0.2 mM; sodium chloride 100 mM; HEPES 20 mM; PMSF 1 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 100 mM; 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CCPN v2.1.5, CCPN - 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