BMRB Entry 31231

Name: Structure of the 5&#039;SL-bound La Domain of the Human La-related Protein 6
Published: 2025-05-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31231

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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:

Structure of the 5'SL-bound La Domain of the Human La-related Protein 6

Deposition date:

2025-02-22

Original release date:

2025-05-07

Authors:

Gordon, B.; Silvers, R.

Citation:

Citation: Gordon, B.; Silvers, R.. "1H, 13C, and 15N resonance assignment of the 5'SL-bound La domain of the human La-related protein 6" Biomol. NMR Assign. ., .-. (2025).
PubMed: 40304844

Assembly members:

Assembly members:
entity_1, polymer, 106 residues, 12639.463 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEDLEQEWKPPDEELIKKLV DQIEFYFSDENLEKDAFLLK HVRRNKLGYVSVKLLTSFKK VKHLTRDWRTTAHALKYSVV LELNEDHRKVRRTTPVPLFP NENLPS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	517
15N chemical shifts	113
1H chemical shifts	818

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 106 residues - 12639.463 Da.

1

GLY

GLU

ASP

LEU

GLU

GLN

GLU

TRP

LYS

PRO

2

PRO

ASP

GLU

LEU

ILE

LYS

LEU

VAL

3

ASP

GLN

ILE

GLU

PHE

TYR

PHE

SER

ASP

GLU

4

ASN

LEU

GLU

LYS

ASP

ALA

PHE

LEU

LYS

5

HIS

VAL

ARG

ASN

LYS

LEU

GLY

TYR

VAL

6

SER

VAL

LYS

LEU

THR

SER

PHE

LYS

7

VAL

LYS

HIS

LEU

THR

ARG

ASP

TRP

ARG

THR

8

THR

ALA

HIS

ALA

LEU

LYS

TYR

SER

VAL

9

LEU

GLU

LEU

ASN

GLU

ASP

HIS

ARG

LYS

VAL

10

ARG

THR

PRO

VAL

PRO

LEU

PHE

PRO

11

ASN

GLU

ASN

LEU

PRO

SER

Samples:

sample_1: LARP6(79-183), [U-98% 13C; U-98% 15N], 1.7 mM; A2M5 1.7 mM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_2: LARP6(79-183), [U-98% 13C; U-98% 15N], 370 uM; A2M5 370 uM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_3: LARP6(79-183), [U-98% 15N], 300 uM; A2M5 300 uM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_4: LARP6(79-183), [U-98% 13C; U-98% 15N], 1.1 mM; A2M5 1.1 mM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_5: LARP6(79-183), [U-98% 15N; 1,3-13C-glycerol], 1.6 mM; A2M5 1.6 mM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_6: LARP6(79-183), [U-98% 15N; 2-13C-glycerol], 1.3 mM; A2M5 1.3 mM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_7: LARP6(79-183), [13C, 15N]-Arg, 1.9 mM; A2M5 1.9 mM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_8: LARP6(79-183), [13C]-Pro, 1 mM; A2M5 1 mM; MES 10 mM; potassium chloride 50 mM; DSS 0.01 mg/mL

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CC)(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_4	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_5	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_5	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_5	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_5	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_6	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_6	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_6	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_6	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_7	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_7	isotropic	sample_conditions_1
2D 1H-13C CTHSQC	sample_8	isotropic	sample_conditions_1

Software:

TopSpin v3.6.5, Bruker Biospin - collection

TopSpin v4.3.0, Bruker Biospin - processing

NMRFAM-SPARKY, National Magnetic Resonance Facility at Madison - chemical shift assignment, peak picking

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - peak picking

TALOS-N v4.12, Y. Shen and A. Bax - geometry optimization

CYANA v3.98.15, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber v22, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

NMR spectrometers:

Bruker AVANCE III 700 MHz

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