BMRB Entry 11457

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

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PDB ID: 2rs7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11457
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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 second 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, 113 residues, 12507.041 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: GSSGSSGLESEEVDLNAGLH GNWTLENAKARLNQYFQKEK IQGEYKYTQVGPDHNRSFIA EMTIYIKQLGRRIFAREHGS NKKLAAQSCALSLVRQLYHL GVIEAYSSGPSSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	485
15N chemical shifts	122
1H chemical shifts	771

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	second dsRBD	1

Entities:

Entity 1, second dsRBD 113 residues - 12507.041 Da.

1

GLY

SER

GLY

SER

GLY

LEU

GLU

SER

2

GLU

VAL

ASP

LEU

ASN

ALA

GLY

LEU

HIS

3

GLY

ASN

TRP

THR

LEU

GLU

ASN

ALA

LYS

ALA

4

ARG

LEU

ASN

GLN

TYR

PHE

GLN

LYS

GLU

LYS

5

ILE

GLN

GLY

GLU

TYR

LYS

TYR

THR

GLN

VAL

6

GLY

PRO

ASP

HIS

ASN

ARG

SER

PHE

ILE

ALA

7

GLU

MET

THR

ILE

TYR

ILE

LYS

GLN

LEU

GLY

8

ARG

ILE

PHE

ALA

ARG

GLU

HIS

GLY

SER

9

ASN

LYS

LEU

ALA

GLN

SER

CYS

ALA

10

LEU

SER

LEU

VAL

ARG

GLN

LEU

TYR

HIS

LEU

11

GLY

VAL

ILE

GLU

ALA

TYR

SER

GLY

PRO

12

SER

GLY

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.16 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 - refinement

NMR spectrometers:

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

PDB	1UIL 2RS7 3VYX
DBJ	BAB28848 BAE24846 BAE88384 BAH90798
EMBL	CAA58036 CAA71668 CAH92036
GB	AAB48855 AAC05725 AAH08773 AAH14246 AAH25245
PIR	A47363
REF	NP_001100654 NP_001253117 NP_001348 NP_031868 NP_776461
SP	O70133 Q08211 Q28141 Q5R874
TPG	DAA21040
AlphaFold	O70133 Q08211 Q28141 Q5R874