BMRB Entry 51254

Name: Solution NMR backbone chemical shift assignment for the extended xRRM2 domain of human La-related protein 7
Published: 2022-03-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51254

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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 NMR backbone chemical shift assignment for the extended xRRM2 domain of human La-related protein 7

Deposition date:

2021-12-22

Original release date:

2022-03-28

Authors:

Yang, Yuan; Eichhorn, Catherine; Hadjian, Tanya; Feigon, Juli

Citation:

Citation: Yang, Yuan; Liu, Shiheng; Egloff, Sylvain; Eichhorn, Catherine; Hadjian, Tanya; Zhen, James; Kiss, Tamas; Zhou, Z. Hong; Feigon, Juli. "Structural basis of RNA conformational switching in the transcriptional regulator 7SK RNP" Mol. Cell 82, 1724-1736 (2022).
PubMed: 35320752

Assembly members:

Assembly members:
entity_1, polymer, 213 residues, 24357 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: pETDuet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEEVIPLRVLSKSEWMDLKK EYLALQKASMASLKKTISQI KSESEMETDSGVPQNTGMKN EKTANREECRTQEKVNATGP QFVSGVIVKIISTEPLPGRK QVRDTLAAISEVLYVDLLEG DTECHARFKTPEDAQAVINA YTEINKKHCWKLEILSGDHE QRYWQKILVDRQAKLNQPRE KKRGTEKLITKAEKIRLAKT QQASKHIRFSEYD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	528
15N chemical shifts	198
1H chemical shifts	198

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Larp7 extended xRRM2 domain	1

Entities:

Entity 1, Larp7 extended xRRM2 domain 213 residues - 24357 Da.

1

GLY

GLU

VAL

ILE

PRO

LEU

ARG

VAL

LEU

2

SER

LYS

SER

GLU

TRP

MET

ASP

LEU

LYS

3

GLU

TYR

LEU

ALA

LEU

GLN

LYS

ALA

SER

MET

4

ALA

SER

LEU

LYS

THR

ILE

SER

GLN

ILE

5

LYS

SER

GLU

SER

GLU

MET

GLU

THR

ASP

SER

6

GLY

VAL

PRO

GLN

ASN

THR

GLY

MET

LYS

ASN

7

GLU

LYS

THR

ALA

ASN

ARG

GLU

CYS

ARG

8

THR

GLN

GLU

LYS

VAL

ASN

ALA

THR

GLY

PRO

9

GLN

PHE

VAL

SER

GLY

VAL

ILE

VAL

LYS

ILE

10

ILE

SER

THR

GLU

PRO

LEU

PRO

GLY

ARG

LYS

11

GLN

VAL

ARG

ASP

THR

LEU

ALA

ILE

SER

12

GLU

VAL

LEU

TYR

VAL

ASP

LEU

GLU

GLY

13

ASP

THR

GLU

CYS

HIS

ALA

ARG

PHE

LYS

THR

14

PRO

GLU

ASP

ALA

GLN

ALA

VAL

ILE

ASN

ALA

15

TYR

THR

GLU

ILE

ASN

LYS

HIS

CYS

TRP

16

LYS

LEU

GLU

ILE

LEU

SER

GLY

ASP

HIS

GLU

17

GLN

ARG

TYR

TRP

GLN

LYS

ILE

LEU

VAL

ASP

18

ARG

GLN

ALA

LYS

LEU

ASN

GLN

PRO

ARG

GLU

19

LYS

ARG

GLY

THR

GLU

LYS

LEU

ILE

THR

20

LYS

ALA

GLU

LYS

ILE

ARG

LEU

ALA

LYS

THR

21

GLN

ALA

SER

LYS

HIS

ILE

ARG

PHE

SER

22

GLU

TYR

ASP

Samples:

sample_1: Larp7 extended xRRM2 domain, [U-13C; U-15N], 0.2 mM; sodium phosphate 20 mM; potassium chloride 50 mM; TCEP 1 mM; D2O 5%

sample_conditions_1: ionic strength: 0.07 M; pH: 6.13; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	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 HNCA	sample_1	isotropic	sample_conditions_1
3D CCONH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN vv4.0.7 - collection

TOPSPIN vv3.5pl7 - collection

NMRPipe vv2016.273.11.31 - processing

NMRFAM-SPARKY vv1.470 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE III HD 600 MHz

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