BMRB Entry 11413

Name: Refinement of RNA binding domain in human Tra2 beta protein
Published: 2011-09-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11413

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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:

Refinement of RNA binding domain in human Tra2 beta protein

Deposition date:

2010-09-09

Original release date:

2011-09-08

Authors:

Tsuda, K.; Kuwasako, K.; Takahashi, M.; Someya, T.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Sugano, S.; Muto, Y.; Yokoyama, S.

Citation:

Citation: Tsuda, K.; Kuwasako, K.; Someya, T.; Takahashi, M.; He, F.; Inoue, M.; Harada, T.; Watanabe, S.; Terada, T.; Kobayashi, N.; Shirouzu, M.; Kigawa, T.; Tanaka, A.; Sugano, S.; Guntert, P.; Yokoyama, S.; Muto, Y.. "Refinement of RNA binding domain in human Tra2 beta protein" .

Assembly members:

Assembly members:
RNA recognition motif, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA recognition motif: GPLGSRANPDPNCCLGVFGL SLYTTERDLREVFSKYGPIA DVSIVYDQQSRRSRGFAFVY FENVDDAKEAKERANGMELD GRRIRVDFSITKRPHT

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	333
15N chemical shifts	96
1H chemical shifts	650

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNA recognition motif	1

Entities:

Entity 1, RNA recognition motif 96 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

ARG

ALA

ASN

PRO

ASP

2

PRO

ASN

CYS

LEU

GLY

VAL

PHE

GLY

LEU

3

SER

LEU

TYR

THR

GLU

ARG

ASP

LEU

ARG

4

GLU

VAL

PHE

SER

LYS

TYR

GLY

PRO

ILE

ALA

5

ASP

VAL

SER

ILE

VAL

TYR

ASP

GLN

SER

6

ARG

SER

ARG

GLY

PHE

ALA

PHE

VAL

TYR

7

PHE

GLU

ASN

VAL

ASP

ALA

LYS

GLU

ALA

8

LYS

GLU

ARG

ALA

ASN

GLY

MET

GLU

LEU

ASP

9

GLY

ARG

ILE

ARG

VAL

ASP

PHE

SER

ILE

10

THR

LYS

ARG

PRO

HIS

THR

Samples:

sample_1: Human transformer 2 beta-1, [U-13C; U-15N], 1 mM; 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:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, Kollm - refinement

xwinnmr v3.6, Bruker, Biospin - collection

NMRPipe v20060801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, and, Bax - processing

NMRView v5.0.4, Johnson, One, Moon, Scientific - data analysis

Kujira v0.9843, N. Kobayashi - data analysis

CYANA v2.1, Guntert, Mumenthaler, and, Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

BMRB	16920
PDB	2KXN 2RRB
DBJ	BAA08556 BAC05256 BAC33819 BAD92445 BAE88784
EMBL	CAA56518 CAH18071
GB	AAB08701 AAC28242 AAD19277 AAD19278 AAH00160
REF	NP_001029948 NP_001070689 NP_001230808 NP_001248265 NP_001271939
SP	P62995 P62996 P62997 Q3ZBT6
TPG	DAA33375
AlphaFold	P62995 P62996 P62997 Q3ZBT6