BMRB Entry 11370

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PDB ID: 2rne
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11370
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated

Deposition date:

2010-09-08

Original release date:

2010-11-30

Authors:

Takahashi, M.; Kuwasako, K.; Abe, C.; Tsuda, K.; Inoue, M.; Terada, T.; Shirouzu, M.; Kobayashi, N.; Kigawa, T.; Taguchi, S.; Guntert, P.; Hayashizaki, Y.; Tanaka, A.; Muto, Y.; Yokoyama, S.

Citation:

Citation: Kuwasako, Kanako; Takahashi, Mari; Tochio, Naoya; Abe, Chikage; Tsuda, Kengo; Inoue, Makoto; Terada, Takaho; Shirouzu, Mikako; Kobayashi, Naohiro; Kigawa, Takanori; Taguchi, Seiichi; Tanaka, Akiko; Hayashizaki, Yoshihide; Guntert, Peter; Muto, Yutaka; Yokoyama, Shigeyuki. "Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode." Biochemistry 47, 6437-6450 (2008).
PubMed: 18500819

Assembly members:

Assembly members:
RRM domain C terminal truncated, polymer, 87 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM domain C terminal truncated: GQKKDTSNHFHVFVGDLSPE ITTEDIKAAFAPFGRISDAR VVKDMATGKSKGYGFVSFFN KWDAENAIQQMGGQWLGGRQ IRTNWAT

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	246
15N chemical shifts	82
1H chemical shifts	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM domain C terminal truncated	1

Entities:

Entity 1, RRM domain C terminal truncated 87 residues - Formula weight is not available

1

GLY

GLN

LYS

ASP

THR

SER

ASN

HIS

PHE

2

HIS

VAL

PHE

VAL

GLY

ASP

LEU

SER

PRO

GLU

3

ILE

THR

GLU

ASP

ILE

LYS

ALA

PHE

4

ALA

PRO

PHE

GLY

ARG

ILE

SER

ASP

ALA

ARG

5

VAL

LYS

ASP

MET

ALA

THR

GLY

LYS

SER

6

LYS

GLY

TYR

GLY

PHE

VAL

SER

PHE

ASN

7

LYS

TRP

ASP

ALA

GLU

ASN

ALA

ILE

GLN

8

MET

GLY

GLN

TRP

LEU

GLY

ARG

GLN

9

ILE

ARG

THR

ASN

TRP

ALA

THR

Samples:

sample_1: RRM domain C terminal truncated, [U-99% 13C; U-99% 15N], 1 mM; TRIS, [U-99% 2H], 20 mM; sodium chloride 100 mM; DTT, [U-98% 2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	condition_1
3D 1H-13C NOESY	sample_1	isotropic	condition_1

Software:

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	11371 11372 11373 11374 11375 11376
PDB	2DGO 2RNE
GB	EAW99825
REF	XP_005430921 XP_007654274