BMRB Entry 11456

Name: Solution structure of the N-terminal dsRBD from RNA helicase A
Published: 2012-08-29

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PDB ID: 2rs6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11456
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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 structure of the N-terminal dsRBD from RNA helicase A

Deposition date:

2011-11-29

Original release date:

2012-08-29

Authors:

Nagata, Takashi; Muto, Yutaka; Tsuda, Kengo; Inoue, Makoto; Kigawa, Takanori; Terada, Takaho; Shirouzu, Mikako; Yokoyama, Shigeyuki

Citation:

Citation: Nagata, Takashi; Tsuda, Kengo; Kobayashi, Naohiro; Shirouzu, Mikako; Kigawa, Takanori; Guntert, Peter; Yokoyama, Shigeyuki; Muto, Yutaka. "Solution structures of the double-stranded RNA-binding domains from RNA helicase A" Proteins 80, 1699-1706 (2012).
PubMed: 22454253

Assembly members:

Assembly members:
entity, polymer, 99 residues, 10733.203 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: E. coli - cell free Vector: not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSSGSSGIKNFLYAWCGKRK MTPAYEIRAVGNKNRQKFMC EVRVEGFNYAGMGNSTNKKD AQSNAARDFVNYLVRINEVK SEEVPAVGIVPPPSGPSSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	104
1H chemical shifts	622

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNA helicase A	1

Entities:

Entity 1, RNA helicase A 99 residues - 10733.203 Da.

1

GLY

SER

GLY

SER

GLY

ILE

LYS

ASN

2

PHE

LEU

TYR

ALA

TRP

CYS

GLY

LYS

ARG

LYS

3

MET

THR

PRO

ALA

TYR

GLU

ILE

ARG

ALA

VAL

4

GLY

ASN

LYS

ASN

ARG

GLN

LYS

PHE

MET

CYS

5

GLU

VAL

ARG

VAL

GLU

GLY

PHE

ASN

TYR

ALA

6

GLY

MET

GLY

ASN

SER

THR

ASN

LYS

ASP

7

ALA

GLN

SER

ASN

ALA

ARG

ASP

PHE

VAL

8

ASN

TYR

LEU

VAL

ARG

ILE

ASN

GLU

VAL

LYS

9

SER

GLU

VAL

PRO

ALA

VAL

GLY

ILE

VAL

10

PRO

SER

GLY

PRO

SER

GLY

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 700 MHz
Bruker Avance 600 MHz

PDB	1WHQ 2RS6
DBJ	BAB28848 BAE24846 BAE41336
GB	AAC05301 AAC05725 AAH33911 AAH89159 AAI69284
REF	NP_001100654 NP_031868 XP_005363931 XP_005363932 XP_006250057
SP	O70133
AlphaFold	O70133