BMRB Entry 25496

Name: NMR structure of the RRM3 domain of Gbp2
Published: 2015-11-30

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PDB ID: 2mzq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25496
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of the RRM3 domain of Gbp2 PubMed: 26602689

Deposition date: 2015-02-23 Original release date: 2015-11-30

Authors: Martinez-Lumbreras, Santiago; Seraphin, Bertrand; Perez-Canadillas, Jose Manuel

Citation: Martinez-Lumbreras, Santiago; Taverniti, Valerio; Zorrilla, Silvia; Seraphin, Bertrand; Perez-Canadillas, Jose Manuel. "Gbp2 interacts with THO/TREX through a novel type of RRM domain" Nucleic Acids Res. 44, 437-448 (2016).

Assembly members:
RRM3, polymer, 101 residues, 11094.291 Da.

Natural source: Common Name: Baker's Yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
RRM3: GSHIDETAAKFTEGVNPGGD RNCFIYCSNLPFSTARSDLF DLFGPIGKINNAELKPQENG QPTGVAVVEYENLVDADFCI QKLNNYNYGGCSLQISYARR D

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	369
15N chemical shifts	112
1H chemical shifts	663

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM3 domain of Gbp2	1

Entities:

Entity 1, RRM3 domain of Gbp2 101 residues - 11094.291 Da.

From 329 to 427

1

GLY

SER

HIS

ILE

ASP

GLU

THR

ALA

LYS

2

PHE

THR

GLU

GLY

VAL

ASN

PRO

GLY

ASP

3

ARG

ASN

CYS

PHE

ILE

TYR

CYS

SER

ASN

LEU

4

PRO

PHE

SER

THR

ALA

ARG

SER

ASP

LEU

PHE

5

ASP

LEU

PHE

GLY

PRO

ILE

GLY

LYS

ILE

ASN

6

ASN

ALA

GLU

LEU

LYS

PRO

GLN

GLU

ASN

GLY

7

GLN

PRO

THR

GLY

VAL

ALA

VAL

GLU

TYR

8

GLU

ASN

LEU

VAL

ASP

ALA

ASP

PHE

CYS

ILE

9

GLN

LYS

LEU

ASN

TYR

ASN

TYR

GLY

10

CYS

SER

LEU

GLN

ILE

SER

TYR

ALA

ARG

11

ASP

Samples:

sample_1: RRM3, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 10%; H2O 90%

sample_2: RRM3, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

TOPSPIN, Bruker Biospin - collection

CcpNMR_Analysis, CCPN - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts