BMRB Entry 11409

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11409

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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:

Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA)

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.. "Solution structure of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA)" .

Assembly members:

Assembly members:
RNA recognition motif, polymer, 99 residues, Formula weight is not available
5'-R(*GP*AP*AP*GP*AP*A)-3, polymer, 6 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: Escherichia coli Vector: P040517-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA recognition motif: GSSGSSGNRANPDPNCCLGV FGLSLYTTERDLREVFSKYG PIADVSIVYDQQSRRSRGFA FVYFENVDDAKEAKERANGM ELDGRRIRVDFSITKRPHT
5'-R(*GP*AP*AP*GP*AP*A)-3: GAAGAA

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	409
15N chemical shifts	96
1H chemical shifts	648

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNA recognition motif	1
2	5'-R(GPAPAPGPAPA)-3	2

Entities:

Entity 1, RNA recognition motif 99 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ASN

ARG

ALA

2

ASN

PRO

ASP

PRO

ASN

CYS

LEU

GLY

VAL

3

PHE

GLY

LEU

SER

LEU

TYR

THR

GLU

ARG

4

ASP

LEU

ARG

GLU

VAL

PHE

SER

LYS

TYR

GLY

5

PRO

ILE

ALA

ASP

VAL

SER

ILE

VAL

TYR

ASP

6

GLN

SER

ARG

SER

ARG

GLY

PHE

ALA

7

PHE

VAL

TYR

PHE

GLU

ASN

VAL

ASP

ALA

8

LYS

GLU

ALA

LYS

GLU

ARG

ALA

ASN

GLY

MET

9

GLU

LEU

ASP

GLY

ARG

ILE

ARG

VAL

ASP

10

PHE

SER

ILE

THR

LYS

ARG

PRO

HIS

THR

Entity 2, 5'-R(*GP*AP*AP*GP*AP*A)-3 6 residues - Formula weight is not available

1

G

A

G

A

Samples:

sample_1: Human transformer 2 beta-1, [U-13C; U-15N], 1 mM; RNA (5'-R(GAAGAA)-3')-2 2 mM; salt 100 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 283 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
2D 1H-1H 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	11400 11410 11411 11412 16920
PDB	2CQC 2KXN 2RRA
DBJ	BAA08556 BAC05256 BAC33819 BAD92445 BAE88784
EMBL	CAA56518 CAH18071 CAH90742
GB	AAB08701 AAC28242 AAD19277 AAD19278 AAG35783
REF	NP_001006878 NP_001029948 NP_001070689 NP_001125414 NP_001230808
SP	P62995 P62996 P62997 Q3ZBT6
TPG	DAA33375
AlphaFold	P62995 P62996 P62997 Q3ZBT6