BMRB Entry 25497

Name: NMR structure of the RRM1 domain of Hrb1
Published: 2015-11-30

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PDB ID: 2mzr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25497
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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:

NMR structure of the RRM1 domain of Hrb1

Deposition date:

2015-02-23

Original release date:

2015-11-30

Authors:

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

Citation:

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).
PubMed: 26602689

Assembly members:

Assembly members:
RRM1, polymer, 95 residues, 10934.025 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM1: GSARELDSTYEEKVNRNYSN SIFVGNLTYDSTPEDLTEFF SQIGKVVRADIITSRGHHRG MGTVEFTNSDDVDRAIRQYD GAFFMDRKIFVRQDN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	371
15N chemical shifts	89
1H chemical shifts	576

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM1	1

Entities:

Entity 1, RRM1 95 residues - 10934.025 Da.

From 144 to 236

1

GLY

SER

ALA

ARG

GLU

LEU

ASP

SER

THR

TYR

2

GLU

LYS

VAL

ASN

ARG

ASN

TYR

SER

ASN

3

SER

ILE

PHE

VAL

GLY

ASN

LEU

THR

TYR

ASP

4

SER

THR

PRO

GLU

ASP

LEU

THR

GLU

PHE

5

SER

GLN

ILE

GLY

LYS

VAL

ARG

ALA

ASP

6

ILE

THR

SER

ARG

GLY

HIS

ARG

GLY

7

MET

GLY

THR

VAL

GLU

PHE

THR

ASN

SER

ASP

8

ASP

VAL

ASP

ARG

ALA

ILE

ARG

GLN

TYR

ASP

9

GLY

ALA

PHE

MET

ASP

ARG

LYS

ILE

PHE

10

VAL

ARG

GLN

ASP

ASN

Samples:

sample_1: RRM1, [U-100% 13C; U-100% 15N], 0.2 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 10%; H2O 90%

sample_2: RRM1, [U-100% 13C; U-100% 15N], 0.2 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 TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	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 HCCH-TOCSY	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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks